HAMAP rule MF_00494
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_00494 |
| Accession | MF_00494 |
| Dates | 28-FEB-2005 (Created)
26-NOV-2025 (Last updated, Version ) |
| Name | Transaldolase_3b |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P19669; P0A870; [ Recover all ] |
| Triggered by |
HAMAP; MF_00494 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | TAL |
| Protein name | RecName: Full=Transaldolase; EC=2.2.1.2; |
| Gene name | Name=tal; |
Comments
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| FUNCTION | Transaldolase involved in the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate. Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. |
| CATALYTIC ACTIVITY | Reaction=D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2; |
| 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. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the transaldolase family. Type 3B subfamily. |
Keywords
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Gene Ontology
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| GO:0004801; Molecular function:transaldolase activity |
| GO:0006098; Biological process:pentose-phosphate shunt |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| NCBIfam | TIGR00875; fsa_talC_mipB; 1; |
| Pfam | PF00923; TAL_FSA; 1; |
| PROSITE | PS01054; TRANSALDOLASE_1; 1; |
| PROSITE | PS00958; TRANSALDOLASE_2; 1; |
Features
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| From: TAL_BACSU (P19669) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 58 | 58 | /note="Proton donor/acceptor" | E | ||||||||
| ACT_SITE | 84 | 84 | /note="Nucleophile; Schiff-base intermediate with substrate" | K | ||||||||
| BINDING | 6 | 6 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
D | ||||||||
| BINDING | 28 | 28 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
N | ||||||||
| BINDING | 84 | 84 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
K | ||||||||
| BINDING | 106 | 106 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
N | ||||||||
| BINDING | 128 | 128 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
S | ||||||||
| BINDING | 133 | 133 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
R | ||||||||
| BINDING | 165 | 165 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
[SA] | ||||||||
| BINDING | 167 | 167 | /ligand="D-fructose 6-phosphate" /ligand_id="ChEBI:CHEBI:61527" |
R | ||||||||
Additional information
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| Size range | 212-234 amino acids |
| Related rules |
MF_00492 MF_00493 MF_00496 |
| Fusion | Nter: None Cter: None |