D9R9N2 (D9R9N2_CLOSW) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 20.
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 | Clostridium saccharolyticum (strain ATCC 35040 / DSM 2544 / NRCC 2533 / WM1) [Complete proteome] [HAMAP] EMBL ADL04082.1 | ||||
| Taxonomic identifier | 610130 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › ![]() |
Protein attributes
| Sequence length | 217 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 SAAS018225 |
| Catalytic activity | Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. HAMAP-Rule MF_00494 SAAS SAAS018225 |
| 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 SAAS018225 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00494 SAAS SAAS018225. |
| 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 SAAS018225 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00494 SAAS SAAS018225 |
| Molecular function | Transferase HAMAP-Rule MF_00494 SAAS SAAS018225 |
| 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 | 85 | 1 | By similarity HAMAP-Rule MF_00494 | ||||||
Sequences
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References
| [1] | "Complete sequence of Clostridium saccharolyticum WM1." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N. Woyke T.Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35040 / DSM 2544 / NRCC 2533 / WM1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002109 Genomic DNA. Translation: ADL04082.1. |
| RefSeq | YP_003821705.1. NC_014376.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADL04082; ADL04082; Closa_1484. |
| GeneID | 9506772. |
| KEGG | csh:Closa_1484. |
| PATRIC | 42264450. VBICloSac91065_1604. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000226073. |
| KO | K00616. |
Enzyme and pathway databases | |
| BioCyc | CSAC610130:GHTP-1535-MONOMER. |
| 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 | D9R9N2_CLOSW | ||||||||
| Accession | Primary (citable) accession number: D9R9N2 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
