D3QM42 (D3QM42_ECOCB) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 28.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Transaldolase HAMAP-Rule MF_00492 EC=2.2.1.2 HAMAP-Rule MF_00492 | ||||||
| Gene names |
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| Organism | Escherichia coli O55:H7 (strain CB9615 / EPEC) [Complete proteome] [HAMAP] EMBL ADD57517.1 | ||||||
| Taxonomic identifier | 701177 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 316 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway By similarity. RuleBase RU004155 SAAS SAAS018225 HAMAP-Rule MF_00492 |
| Catalytic activity | Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. RuleBase RU004155 SAAS SAAS018225 HAMAP-Rule 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. RuleBase RU004155 SAAS SAAS018225 HAMAP-Rule MF_00492 |
| Subunit structure | Homodimer By similarity. SAAS SAAS018225 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00492 SAAS SAAS001585. |
| Sequence similarities | Belongs to the transaldolase family. Type 1 subfamily. RuleBase RU004155 HAMAP-Rule MF_00492 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pentose shunt RuleBase RU004155 SAAS SAAS018225 HAMAP-Rule MF_00492 |
| Cellular component | Cytoplasm SAAS SAAS001585 HAMAP-Rule MF_00492 |
| Molecular function | Transferase RuleBase RU004155 SAAS SAAS018225 HAMAP-Rule MF_00492 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | pentose-phosphate shunt Inferred from electronic annotation. Source: HAMAP |
| 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: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 131 | 1 | By similarity HAMAP-Rule MF_00492 | ||||||
Sequences
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References
| [1] | "Derivation of Escherichia coli O157:H7 from its O55:H7 precursor." Zhou Z., Li X., Liu B., Beutin L., Xu J., Ren Y., Feng L., Lan R., Reeves P.R., Wang L. PLoS ONE 5:E8700-E8700(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CB9615 / EPEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001846 Genomic DNA. Translation: ADD57517.1. |
| RefSeq | YP_003500501.1. NC_013941.1. |
3D structure databases | |
| ProteinModelPortal | D3QM42. |
| SMR | D3QM42. Positions 2-313. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | D3QM42. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADD57517; ADD57517; G2583_2986. |
| GeneID | 8871948. |
| KEGG | eok:G2583_2986. |
| PATRIC | 35345102. VBIEscCol154499_3017. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000281234. |
| KO | K00616. |
Enzyme and pathway databases | |
| BioCyc | ECOL701177:GI1N-3095-MONOMER. |
| UniPathway | UPA00115; UER00414. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_00492. Transaldolase_1. |
| InterPro | IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004730. Transaldolase_1. IPR018225. Transaldolase_AS. [Graphical view] |
| PANTHER | PTHR10683. PTHR10683. 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 | D3QM42_ECOCB | ||||||||
| Accession | Primary (citable) accession number: D3QM42 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
