B1LQL8 (ULAF_ECOSM) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 29.
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 |
| ||||
| Organism | Escherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 439855 [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_1000188849 | |||||
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
| ||||||||||||||||||
References
| [1] | "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5." Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R. J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SMS-3-5 / SECEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000970 Genomic DNA. Translation: ACB17376.1. |
| RefSeq | YP_001746593.1. NC_010498.1. |
3D structure databases | |
| ProteinModelPortal | B1LQL8. |
| SMR | B1LQL8. Positions 1-219. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B1LQL8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000062313; EBESCP00000059955; EBESCG00000061360. |
| GeneID | 6145109. |
| GenomeReviews | Gene locus EcSMS35_4669 in contig CP000970_GR. |
| KEGG | ecm:EcSMS35_4669. |
| PATRIC | 18438249. VBIEscCol6161_4775. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009319. |
| HOGENOM | HBG541069. |
| OMA | IDSYLMN. |
| ProtClustDB | PRK12348. |
Enzyme and pathway databases | |
| BioCyc | ECOL439855:ECSMS35_4669-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. |
| 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 | ULAF_ECOSM | ||||||||
| Accession | Primary (citable) accession number: B1LQL8 | ||||||||
| Entry history |
| ||||||||
| 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 |

Clusters with