P0A872 (TALB_SHIFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 55.
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: Transaldolase B EC=2.2.1.2 | ||||
| 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 | 317 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway By similarity. HAMAP MF_00492 |
| Catalytic activity | Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP MF_00492 |
| Pathway | Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. HAMAP MF_00492 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00492 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00492. |
| Sequence similarities | Belongs to the transaldolase family. Type 1 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pentose shunt |
| Cellular component | Cytoplasm |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 317 | 316 | Transaldolase B HAMAP MF_00492 | PRO_0000173596 | |||||
Sites | |||||||||
| Active site | 132 | 1 | 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: AAN41675.2. AE014073 Genomic DNA. Translation: AAP15554.1. |
| RefSeq | NP_705968.2. NC_004337.2. NP_835749.1. NC_004741.1. |
3D structure databases | |
| ProteinModelPortal | P0A872. |
| SMR | P0A872. Positions 2-317. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000088514; EBESCP00000085336; EBESCG00000087558. EBESCT00000091152; EBESCP00000087788; EBESCG00000090196. |
| GeneID | 1027387. 1076428. |
| GenomeReviews | Gene locus SF0009 in contig AE005674_GR. Gene locus S0008 in contig AE014073_GR. |
| KEGG | sfl:SF0009. sfx:S0008. |
| PATRIC | 18700934. VBIShiFle31049_0009. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000009451. |
| HOGENOM | HBG286747. |
| ProtClustDB | PRK05269. |
Enzyme and pathway databases | |
| BioCyc | SFLE198214:AAN41675.1-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00492. Transaldolase_1. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004730. Transaldolase_1. IPR018225. Transaldolase_AS. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| KO | K00616. |
| PANTHER | PTHR10683. Transaldolase. 1 hit. |
| Pfam | PF00923. Transaldolase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00874. TalAB. 1 hit. |
| PROSITE | PS01054. TRANSALDOLASE_1. 1 hit. PS00958. TRANSALDOLASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TALB_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P0A872 Secondary accession number(s): P30148 | ||||||||
| 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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