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Conserved domains on  [gi|446347035|ref|WP_000424890|]
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MULTISPECIES: fructose-6-phosphate aldolase [Enterobacteriaceae]

Protein Classification

fructose-6-phosphate aldolase( domain architecture ID 10793686)

fructose-6-phosphate aldolase catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-220 7.70e-145

fructose-6-phosphate aldolase; Reviewed


:

Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 402.62  E-value: 7.70e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLDVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQA 160
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDWLGAFGRTSI 220
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDWQGAFGRTSI 220
 
Name Accession Description Interval E-value
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-220 7.70e-145

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 402.62  E-value: 7.70e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLDVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQA 160
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDWLGAFGRTSI 220
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDWQGAFGRTSI 220
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 2-211 2.40e-94

Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea, which are member of the MipB/TalC subfamily of class I aldolases. FSA catalyze an aldol cleavage of fructose 6-phosphate and do not utilize fructose, fructose 1-phosphate, fructose 1,6-phosphate, or dihydroxyacetone phosphate. The enzymes belong to the transaldolase family that serves in transfer reactions in the pentose phosphate cycle, and are more distantly related to fructose 1,6-bisphosphate aldolase.


Pssm-ID: 188643 [Multi-domain]  Cd Length: 211  Bit Score: 274.45  E-value: 2.40e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   2 ELYLDTSDVVAVKALSRIFPLAGVTTNPSIIA-AGKKPLDVVLPQLHEAMggQGRLFAQVMATTAEGMVNDARKLRSIIA 80
Cdd:cd00956    1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAkSGRIDFEAVLKEICEII--DGPVSAQVVSTDAEGMVAEARKLASLGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQA 160
Cdd:cd00956   79 NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446347035 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDW 211
Cdd:cd00956  159 KILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDW 209
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-215 4.00e-91

fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes the E. coli transaldolase homologs TalC and MipB, both shown to be fructose-6-phosphate aldolases rather than transaldolases as previously thought. It is related to but distinct from the transaldolase family of E. coli TalA and TalB. The member from Bacillus subtilis becomes phosphorylated during early stationary phase but not during exponential growth. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 129953 [Multi-domain]  Cd Length: 213  Bit Score: 266.34  E-value: 4.00e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035    1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLDVVLPQLHEAMggQGRLFAQVMATTAEGMVNDARKLRSIIA 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAV--EGPVSAETISLDAEGMVEEAKELAKLAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQA 160
Cdd:TIGR00875  79 NIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446347035  161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDWLGAF 215
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAAF 213
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-211 9.20e-81

Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439946 [Multi-domain]  Cd Length: 214  Bit Score: 239.98  E-value: 9.20e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIA-AGKKPLDVVLPQLHEAMGGqgRLFAQVMATTAEGMVNDARKLRSII 79
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAkAGIKDFVEDIREICDIVDG--PVSAEVLATDTEGMIAEARRLAALY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  80 AD-IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAP 158
Cdd:COG0176   79 RPnVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446347035 159 QAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDW 211
Cdd:COG0176  159 RTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADW 211
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-216 2.56e-64

Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.


Pssm-ID: 395737 [Multi-domain]  Cd Length: 226  Bit Score: 198.92  E-value: 2.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035    3 LYLDTSDVVAVKALSRIFPLAGVTTNPSIIA---AGKKPLDVVLPQLHEAmgGQGRLFAQVMA---TTAEGMVNDARKLR 76
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLkaiEYSALYDEAIAEIKEI--GDGPVSLEVDPrlaDDTEGTIEEARRLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   77 SII--ADIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGS----------GIQ 144
Cdd:pfam00923  79 ALYgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGDKrlgaalrgddGIA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446347035  145 TVTDLHQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITLPLDVAQQMISypavEAAVAKFEQDWLGAFG 216
Cdd:pfam00923 159 NAKEIYQIYKKYGWSTGVLAASFRNVLYVLA--LAGCDTITIPPDTLEALAK----DEGVRKFAKDWEKLLG 224
 
Name Accession Description Interval E-value
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-220 7.70e-145

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 402.62  E-value: 7.70e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLDVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQA 160
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDWLGAFGRTSI 220
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDWQGAFGRTSI 220
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 2-211 2.40e-94

Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea, which are member of the MipB/TalC subfamily of class I aldolases. FSA catalyze an aldol cleavage of fructose 6-phosphate and do not utilize fructose, fructose 1-phosphate, fructose 1,6-phosphate, or dihydroxyacetone phosphate. The enzymes belong to the transaldolase family that serves in transfer reactions in the pentose phosphate cycle, and are more distantly related to fructose 1,6-bisphosphate aldolase.


Pssm-ID: 188643 [Multi-domain]  Cd Length: 211  Bit Score: 274.45  E-value: 2.40e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   2 ELYLDTSDVVAVKALSRIFPLAGVTTNPSIIA-AGKKPLDVVLPQLHEAMggQGRLFAQVMATTAEGMVNDARKLRSIIA 80
Cdd:cd00956    1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAkSGRIDFEAVLKEICEII--DGPVSAQVVSTDAEGMVAEARKLASLGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQA 160
Cdd:cd00956   79 NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446347035 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDW 211
Cdd:cd00956  159 KILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDW 209
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-215 4.00e-91

fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes the E. coli transaldolase homologs TalC and MipB, both shown to be fructose-6-phosphate aldolases rather than transaldolases as previously thought. It is related to but distinct from the transaldolase family of E. coli TalA and TalB. The member from Bacillus subtilis becomes phosphorylated during early stationary phase but not during exponential growth. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 129953 [Multi-domain]  Cd Length: 213  Bit Score: 266.34  E-value: 4.00e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035    1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLDVVLPQLHEAMggQGRLFAQVMATTAEGMVNDARKLRSIIA 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAV--EGPVSAETISLDAEGMVEEAKELAKLAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAPQA 160
Cdd:TIGR00875  79 NIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446347035  161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDWLGAF 215
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAAF 213
Transaldolase cd00439
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
 2-213 7.53e-85

Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.


Pssm-ID: 188631 [Multi-domain]  Cd Length: 252  Bit Score: 251.89  E-value: 7.53e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   2 ELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKK--------------------------------PLDVVLPQLHEA 49
Cdd:cd00439    1 SPWYDTLDRPATDLLPLIRGVRGVTTNPSIIQAAIStsnayndqfrtlvesgkdiesaywelvvkdiqDACKLFEPIYDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  50 MGGQGRLFAQVMA---TTAEGMVNDARKLRSIIA--DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAG 124
Cdd:cd00439   81 TEADGRVSVEVSArlaDDTQGMVEAAKYLSKVVNrrNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035 125 AEYVAPYVNRIDAQGG-------------SGIQTVTDLHQLLKMHAPQAKVLAASFKTPRQALDCLlaGCESITLPLDVA 191
Cdd:cd00439  161 TSVASPFVSRIDTLMDkmleqigldlrgkAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLI--GCDTVTTMPDQA 238

                        250       260
                 ....*....|....*....|..
gi 446347035 192 QQMisypaveaAVAKFEQDWLG 213
Cdd:cd00439  239 LEA--------GVDKFKKDFES 252
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-211 9.20e-81

Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439946 [Multi-domain]  Cd Length: 214  Bit Score: 239.98  E-value: 9.20e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIA-AGKKPLDVVLPQLHEAMGGqgRLFAQVMATTAEGMVNDARKLRSII 79
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAkAGIKDFVEDIREICDIVDG--PVSAEVLATDTEGMIAEARRLAALY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  80 AD-IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAP 158
Cdd:COG0176   79 RPnVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446347035 159 QAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDW 211
Cdd:COG0176  159 RTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADW 211
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-216 2.56e-64

Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.


Pssm-ID: 395737 [Multi-domain]  Cd Length: 226  Bit Score: 198.92  E-value: 2.56e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035    3 LYLDTSDVVAVKALSRIFPLAGVTTNPSIIA---AGKKPLDVVLPQLHEAmgGQGRLFAQVMA---TTAEGMVNDARKLR 76
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLkaiEYSALYDEAIAEIKEI--GDGPVSLEVDPrlaDDTEGTIEEARRLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   77 SII--ADIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGS----------GIQ 144
Cdd:pfam00923  79 ALYgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGDKrlgaalrgddGIA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446347035  145 TVTDLHQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITLPLDVAQQMISypavEAAVAKFEQDWLGAFG 216
Cdd:pfam00923 159 NAKEIYQIYKKYGWSTGVLAASFRNVLYVLA--LAGCDTITIPPDTLEALAK----DEGVRKFAKDWEKLLG 224
PRK12656 PRK12656
fructose-6-phosphate aldolase; Reviewed
 1-220 2.77e-53

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183656 [Multi-domain]  Cd Length: 222  Bit Score: 170.69  E-value: 2.77e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIA-AGKKPLDVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSII 79
Cdd:PRK12656   1 MEFMLDTLNLEAIKKWHEILPLAGVTSNPSIAKkEGDIDFFERIREVREIIGDEASIHVQVVAQDYEGILKDAHEIRRQC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  80 AD-IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLHQLLKMHAP 158
Cdd:PRK12656  81 GDdVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENLNIDSNAVIGQLAEAIDRENS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446347035 159 QAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVEAAVAKFEQDWLGAFGRTSI 220
Cdd:PRK12656 161 DSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFADDWEAIHGRKSI 222
Transaldolase_TalAB cd00957
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ...
 6-193 5.72e-15

Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The enzyme catalyses the reversible transfer of a dyhydroxyacetone moiety, derived from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. The catalytic mechanism is similar to other class I aldolases. The enzyme is found in the non-oxidative branch of the pentose phosphate pathway and forms a dimer in solution.


Pssm-ID: 188644 [Multi-domain]  Cd Length: 313  Bit Score: 72.27  E-value: 5.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   6 DTSDVVAVKAlsriFPLAGVTTNPSII-AAGKKP-----LDVVLPQLHEAMGGQG--------RLFAQV---MATTAEGM 68
Cdd:cd00957   15 DTGDFEAIKK----FKPQDATTNPSLIlAAAKLPeynklVDEAIAYAKKKGGSDEdqisnaldKLLVNFgteILKLIPGR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  69 VN---DAR----------KLRSIIA----------DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGA 125
Cdd:cd00957   91 VStevDARlsfdtnatiaKARKLIKlyeeagidkeRILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAVACAEAGV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035 126 EYVAPYVNRI-------------DAQGGSGIQTVTDLHQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITLPLDVAQ 192
Cdd:cd00957  171 TLISPFVGRIldwykkhsgdkayTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILA--LAGCDYLTISPALLE 248


                 .
gi 446347035 193 Q 193
Cdd:cd00957  249 E 249
PTZ00411 PTZ00411
transaldolase-like protein; Provisional
 65-187 4.70e-12

transaldolase-like protein; Provisional


Pssm-ID: 240406  Cd Length: 333  Bit Score: 63.99  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  65 AEGMVNDARKLRSIIAD-------IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRI-- 135
Cdd:PTZ00411 115 KQAMVDKARKIIKMYEEagiskdrILIKLASTWEGIQAAKALEKEGIHCNLTLLFSFAQAVACAQAGVTLISPFVGRIld 194

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446347035 136 ---DAQGGS--------GIQTVTDLHQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITLP 187
Cdd:PTZ00411 195 wykKPEKAEsyvgaqdpGVISVTKIYNYYKKHGYKTIVMGASFRNTGEILE--LAGCDKLTIS 255
PRK12309 PRK12309
transaldolase;
6-186 3.74e-10

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 58.59  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   6 DTSDVVAVKAlsriFPLAGVTTNPSII-AAGKKP-----LDVVLPQLHEAMGGQ-------------------------- 53
Cdd:PRK12309  18 DTGDIQAIEK----FTPRDATTNPSLItAAAQMPqyqsiVDETLRQARKELGSDapvedvvalafdrlavafglkilkiv 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  54 -GRLFAQVMATTA---EGMVNDARKLRSIIAD-------IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSAL 122
Cdd:PRK12309  94 pGRVSTEVDARLSydtEATIAKARKLISLYEDagisrdrVLIKIASTWEGIKAAEVLEKEGIHCNLTLLFGFHQAIACAE 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446347035 123 AGAEYVAPYVNRI----------DAQGGS---GIQTVTDLHQLLKMHAPQAKVLAASFKTPRQAldCLLAGCESITL 186
Cdd:PRK12309 174 AGVTLISPFVGRIldwykketgrDSYPGAedpGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEI--IELAGCDLLTI 248
PRK12346 PRK12346
transaldolase A; Provisional
 54-186 1.04e-08

transaldolase A; Provisional


Pssm-ID: 183458  Cd Length: 316  Bit Score: 54.34  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  54 GRLFAQVMATTA---EGMVNDARKLRSIIAD-------IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALA 123
Cdd:PRK12346  90 GRVSTEVDARLSfdrEKSIEKARHLVDLYQQqgidksrILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEA 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446347035 124 GAEYVAPYVNRI-------------DAQGGSGIQTVTDLHQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITL 186
Cdd:PRK12346 170 GVFLISPFVGRIydwyqarkpmdpyVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILA--LAGCDRLTI 243
PRK05269 PRK05269
transaldolase B; Provisional
 6-194 1.45e-06

transaldolase B; Provisional


Pssm-ID: 235381 [Multi-domain]  Cd Length: 318  Bit Score: 47.85  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035   6 DTSDVVAVKALSrifPLaGVTTNPSII-AAGKKP-----LDVVLPQLHEAMGGQGRLFAQVMATTA-------------- 65
Cdd:PRK05269  17 DTGDIEAIKKYQ---PQ-DATTNPSLIlKAAQIPeyaplIDDAVAWAKQQSGDRAQQIDDAIDKLAvnfgleilklipgr 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  66 -------------EGMVNDARKLRSIIAD-------IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGA 125
Cdd:PRK05269  93 vstevdarlsfdtEATIAKARKLIALYEEagiskdrILIKIASTWEGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035 126 EYVAPYVNRI----------DAQGGS---GIQTVTDLHQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITLPLDVAQ 192
Cdd:PRK05269 173 FLISPFVGRIldwykkntgkKEYAPAedpGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILE--LAGCDRLTISPALLE 250


                 ..
gi 446347035 193 QM 194
Cdd:PRK05269 251 EL 252
PRK03343 PRK03343
transaldolase; Validated
 22-105 8.52e-06

transaldolase; Validated


Pssm-ID: 235117  Cd Length: 368  Bit Score: 45.58  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  22 LAGVTTNPSI--------------IAAGKKP-------------------LDVVLPQlHEAMGGQ-GRLFAQV---MATT 64
Cdd:PRK03343  39 VVGVTSNPAIfqkaiaggdaydaqIAELAAAgadveeayeelttadvrnaCDVLRPV-YEATGGVdGRVSIEVsprLAHD 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446347035  65 AEGMVNDARKLRSIIA--DIVVKVPVTAEGLAAIKMLKAEGIP 105
Cdd:PRK03343 118 TEATIAEARRLWAAVDrpNLMIKIPATPEGLPAIEALIAEGIS 160
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
 24-136 1.19e-04

Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants and bacteria. Transaldolase is found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.


Pssm-ID: 188642 [Multi-domain]  Cd Length: 338  Bit Score: 42.31  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  24 GVTTNPSI--------------IAAGK-------------------KPLDVVLPqLHEAMGGQ-GRLFAQV---MATTAE 66
Cdd:cd00955   28 GVTSNPAIfekaiagsaayddqIRALKgqgldaeaiyealaiediqDACDLLAP-VYEQTGGNdGYVSLEVsprLADDTQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446347035  67 GMVNDARKLRSIIA--DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQ----------GLLSALAGAEYVAP---- 130
Cdd:cd00955  107 GTIAEAKRLWKAVGrpNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQyeavaeaylrGLERRVEGGGDLSQvasv 186


                 ....*....
gi 446347035 131 ---YVNRID 136
Cdd:cd00955  187 asfFVSRVD 195
PRK09533 PRK09533
bifunctional transaldolase/phosoglucose isomerase; Validated
 61-104 4.47e-03

bifunctional transaldolase/phosoglucose isomerase; Validated


Pssm-ID: 236551 [Multi-domain]  Cd Length: 948  Bit Score: 37.64  E-value: 4.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446347035  61 MATTAEGMVNDARKLRSIIA--DIVVKVPVTAEGLAAIKMLKAEGI 104
Cdd:PRK09533 114 LALDTEGTIAEARRLWAAVDrpNLMIKVPATPEGLPAIRQLIAEGI 159
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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