Q734J6 (Q734J6_BACC1) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 69.
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: Probable transaldolase HAMAP-Rule MF_00494 EC=2.2.1.2 HAMAP-Rule MF_00494 | ||||
| Gene names |
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| Organism | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] EMBL AAS42317.1 | ||||
| Taxonomic identifier | 222523 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 222 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. HAMAP-Rule MF_00494 SAAS SAAS004731 |
| Catalytic activity | Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule MF_00494 SAAS SAAS004731 |
| 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-Rule MF_00494 SAAS SAAS004731 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00494 SAAS SAAS004731. |
| Sequence similarities | Belongs to the transaldolase family. Type 3B subfamily. HAMAP-Rule MF_00494 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pentose shunt HAMAP-Rule MF_00494 SAAS SAAS004731 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00494 SAAS SAAS004731 |
| Molecular function | Transferase SAAS SAAS004731 HAMAP-Rule MF_00494 |
| 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 | 90 | 1 | By similarity HAMAP-Rule MF_00494 | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J., Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987 EMBL AAS42317.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017194 Genomic DNA. Translation: AAS42317.1. |
| RefSeq | NP_979709.1. NC_003909.8. |
3D structure databases | |
| ProteinModelPortal | Q734J6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 222523.BCE_3409. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAS42317; AAS42317; BCE_3409. |
| GeneID | 2752145. |
| KEGG | bca:BCE_3409. |
| PATRIC | 18855506. VBIBacCer118379_3252. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0176. |
| HOGENOM | HOG000226073. |
| KO | K00616. |
| OMA | GVKFEDR. |
| ProtClustDB | PRK01362. |
Enzyme and pathway databases | |
| UniPathway | UPA00115; UER00414. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_00494. Transaldolase_3b. |
| InterPro | IPR013785. Aldolase_TIM. IPR001585. Transaldolase. IPR004731. Transaldolase_3A/3B. IPR022999. Transaldolase_3B. IPR018225. Transaldolase_AS. [Graphical view] |
| PANTHER | PTHR10683. PTHR10683. 1 hit. |
| Pfam | PF00923. Transaldolase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00875. fsa_talC_mipB. 1 hit. |
| PROSITE | PS01054. TRANSALDOLASE_1. 1 hit. PS00958. TRANSALDOLASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q734J6_BACC1 | ||||||||
| Accession | Primary (citable) accession number: Q734J6 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
