B7MLK3 (ULAF_ECO45) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 23.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: L-ribulose-5-phosphate 4-epimerase UlaF EC=5.1.3.4 Alternative name(s): L-ascorbate utilization protein F Phosphoribulose isomerase | ||||
| Gene names |
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| Organism | Escherichia coli O45:K1 (strain S88 / ExPEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 585035 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 228 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 Potential. |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | L-ribulose-phosphate 4-epimerase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 228 | 228 | L-ribulose-5-phosphate 4-epimerase UlaF HAMAP MF_01952 | PRO_1000188840 | |||||
Sites | |||||||||
| Metal binding | 74 | 1 | Zinc By similarity | ||||||
| Metal binding | 93 | 1 | Zinc By similarity | ||||||
| Metal binding | 95 | 1 | Zinc By similarity | ||||||
| Metal binding | 167 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [1] | "Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. Denamur E.PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S88 / ExPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU928161 Genomic DNA. Translation: CAR05933.1. |
| RefSeq | YP_002394270.1. NC_011742.1. |
3D structure databases | |
| ProteinModelPortal | B7MLK3. |
| SMR | B7MLK3. Positions 1-219. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B7MLK3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000140507; EBESCP00000130268; EBESCG00000138409. |
| GeneID | 7130410. |
| GenomeReviews | Gene locus ECS88_4784 in contig CU928161_GR. |
| PATRIC | 18417240. VBIEscCol91599_4677. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009319. |
| HOGENOM | HBG541069. |
| OMA | IDSYLMN. |
| ProtClustDB | PRK12348. |
Enzyme and pathway databases | |
| BioCyc | ECOL585035:ECS88_4784-MONOMER. |
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. |
| 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 | ULAF_ECO45 | ||||||||
| Accession | Primary (citable) accession number: B7MLK3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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