Q83P26 (ULAF_SHIFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 63.
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 | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella |
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_0000233249 | |||||
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] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005674 Genomic DNA. Translation: AAN45770.2. AE014073 Genomic DNA. Translation: AAP19552.1. |
| RefSeq | NP_710063.2. NC_004337.2. NP_839740.1. NC_004741.1. |
3D structure databases | |
| ProteinModelPortal | Q83P26. |
| SMR | Q83P26. Positions 1-219. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000085297; EBESCP00000082119; EBESCG00000084343. EBESCT00000093473; EBESCP00000090109; EBESCG00000092517. |
| GeneID | 1025396. 1080823. |
| GenomeReviews | Gene locus SF4353 in contig AE005674_GR. Gene locus S4623 in contig AE014073_GR. |
| KEGG | sfl:SF4353. sfx:S4623. |
| PATRIC | 18711292. VBIShiFle31049_5044. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009319. |
| HOGENOM | HBG541069. |
| ProtClustDB | PRK12348. |
Enzyme and pathway databases | |
| BioCyc | SFLE198214:AAN45770.1-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_SHIFL | ||||||||
| Accession | Primary (citable) accession number: Q83P26 Secondary accession number(s): Q7UAK5 | ||||||||
| 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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