Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004801 | molecular_function | transaldolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0004801 | molecular_function | transaldolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| C | 0004801 | molecular_function | transaldolase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006098 | biological_process | pentose-phosphate shunt |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016832 | molecular_function | aldehyde-lyase activity |
| D | 0004801 | molecular_function | transaldolase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006098 | biological_process | pentose-phosphate shunt |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016832 | molecular_function | aldehyde-lyase activity |
| E | 0004801 | molecular_function | transaldolase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0006098 | biological_process | pentose-phosphate shunt |
| E | 0016740 | molecular_function | transferase activity |
| E | 0016832 | molecular_function | aldehyde-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ASP137 |
| E | ARG176 |
| E | GOL301 |
| E | HOH408 |
| A | ASN170 |
| A | ILE172 |
| A | HIS173 |
| A | ARG176 |
| A | HOH407 |
| E | ASN170 |
| E | ILE172 |
| E | HIS173 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue G3P B 302 |
| Chain | Residue |
| B | ASP6 |
| B | ASN28 |
| B | TYR132 |
| B | ARG135 |
| B | SER167 |
| B | ARG169 |
| B | PDO301 |
| B | HOH479 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| B | ASN170 |
| B | HIS173 |
| B | ARG176 |
| B | HOH407 |
| D | ASP137 |
| D | ASN170 |
| D | ILE172 |
| D | HIS173 |
| D | ARG176 |
| D | GOL301 |
| D | HOH408 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue ACT B 304 |
| Chain | Residue |
| B | ARG169 |
| B | ASN170 |
| B | HOH420 |
| B | HOH442 |
| B | HOH509 |
| D | ARG169 |
| D | ASN170 |
| D | HOH481 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue G3P C 302 |
| Chain | Residue |
| C | ASP6 |
| C | TYR132 |
| C | ARG135 |
| C | ALA166 |
| C | SER167 |
| C | ARG169 |
| C | PDO301 |
| C | HOH443 |
| C | HOH471 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| C | ASP137 |
| C | ASN170 |
| C | ASN170 |
| C | ILE172 |
| C | ILE172 |
| C | HIS173 |
| C | HIS173 |
| C | ARG176 |
| C | ARG176 |
| C | HOH412 |
| C | HOH412 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue ACT C 304 |
| Chain | Residue |
| C | ARG169 |
| C | ARG169 |
| C | ASN170 |
| C | ASN170 |
| C | HOH414 |
| C | HOH414 |
| C | HOH501 |
| C | HOH501 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue GOL D 301 |
| Chain | Residue |
| B | ASP137 |
| B | ASN170 |
| B | ILE172 |
| B | HIS173 |
| B | ARG176 |
| B | GOL303 |
| B | HOH407 |
| D | ASN170 |
| D | ILE172 |
| D | HIS173 |
| D | ARG176 |
| D | HOH408 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue GOL E 301 |
| Chain | Residue |
| A | ASN170 |
| A | ILE172 |
| A | HIS173 |
| A | ARG176 |
| A | GOL301 |
| A | HOH407 |
| E | ASP137 |
| E | ASN170 |
| E | ILE172 |
| E | HIS173 |
| E | ARG176 |
| E | HOH408 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue ACT E 302 |
| Chain | Residue |
| A | ARG169 |
| A | ASN170 |
| A | HOH424 |
| E | ARG169 |
| E | ASN170 |
| E | HOH420 |
| E | HOH443 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue ACT E 303 |
| Chain | Residue |
| E | PHE154 |
| E | ASN155 |
| E | ILE158 |
| E | ILE159 |
| E | LYS160 |
| E | HOH433 |
| E | ARG151 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide PDO B 301 and LYS B 86 |
| Chain | Residue |
| B | ASP6 |
| B | THR26 |
| B | THR27 |
| B | ASN28 |
| B | VAL59 |
| B | GLN60 |
| B | VAL61 |
| B | VAL84 |
| B | VAL85 |
| B | ILE87 |
| B | ASN108 |
| B | SER130 |
| B | G3P302 |
| B | HOH405 |
| site_id | AD4 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide PDO C 301 and LYS C 86 |
| Chain | Residue |
| C | ASP6 |
| C | THR26 |
| C | THR27 |
| C | ASN28 |
| C | VAL59 |
| C | GLN60 |
| C | VAL61 |
| C | VAL84 |
| C | VAL85 |
| C | ILE87 |
| C | ASN108 |
| C | SER130 |
| C | G3P302 |
| C | HOH406 |
Functional Information from PROSITE/UniProt
| site_id | PS00958 |
| Number of Residues | 18 |
| Details | TRANSALDOLASE_2 Transaldolase active site. AvVKIPmTeDGLrAiKtL |
| Chain | Residue | Details |
| A | ALA83-LEU100 | |
| site_id | PS01054 |
| Number of Residues | 9 |
| Details | TRANSALDOLASE_1 Transaldolase signature 1. GVTTNPTLI |
| Chain | Residue | Details |
| A | GLY24-ILE32 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000250"}]} |