A9N514 (ULAF_SALPB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 41.
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 | Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1016998 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › ![]() |
Protein attributes
| Sequence length | 228 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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-Rule MF_01952 |
| Catalytic activity | L-ribulose 5-phosphate = D-xylulose 5-phosphate. HAMAP-Rule 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-Rule MF_01952 |
| Induction | Induced by L-ascorbate. Repressed by UlaR By similarity. HAMAP-Rule 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) | |
| Biological_process | L-ascorbic acid catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 228 | 228 | L-ribulose-5-phosphate 4-epimerase UlaF HAMAP-Rule MF_01952 | PRO_1000088486 | |||||
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] | The Salmonella enterica serovar Paratyphi B Genome Sequencing Project McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-1250 / SPB7. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000886 Genomic DNA. Translation: ABX70791.1. |
| RefSeq | YP_001591624.1. NC_010102.1. |
3D structure databases | |
| ProteinModelPortal | A9N514. |
| SMR | A9N514. Positions 1-219. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272994.SPAB_05522. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABX70791; ABX70791; SPAB_05522. |
| GeneID | 5779130. |
| KEGG | spq:SPAB_05522. |
| PATRIC | 18537339. VBISalEnt120821_4465. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0235. |
| HOGENOM | HOG000218183. |
| KO | K03077. |
| OMA | KDAHEAV. |
| ProtClustDB | PRK12348. |
Enzyme and pathway databases | |
| BioCyc | SENT28901:GH9O-5509-MONOMER. |
| UniPathway | UPA00263; UER00380. |
Family and domain databases | |
| Gene3D | 3.40.225.10. 1 hit. |
| HAMAP | MF_01952. UlaF. |
| InterPro | IPR001303. Aldolase_II/adducin_N. IPR023499. UlaF. [Graphical view] |
| 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_SALPB | ||||||||
| Accession | Primary (citable) accession number: A9N514 | ||||||||
| 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 |

Clusters with
