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Conserved domains on  [gi|522178364|ref|WP_020686913|]
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MULTISPECIES: fructose-6-phosphate aldolase [Enterobacter]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 1-220 1.54e-116

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member PRK12653:

Pssm-ID: 473867 [Multi-domain]  Cd Length: 220  Bit Score: 330.97  E-value: 1.54e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   1 MELYLDTANVAEVERLARVFPLAGVTTNPSIIAASRESIWEVLPRLQNAIGPKGRLFAQTMSRDAEGMVAEAKRLSNAIP 80
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  81 DIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAPES 160
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364 161 KVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNAFGNLNL 220
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDWQGAFGRTSI 220
 
Name Accession Description Interval E-value
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-220 1.54e-116

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 330.97  E-value: 1.54e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   1 MELYLDTANVAEVERLARVFPLAGVTTNPSIIAASRESIWEVLPRLQNAIGPKGRLFAQTMSRDAEGMVAEAKRLSNAIP 80
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  81 DIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAPES 160
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364 161 KVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNAFGNLNL 220
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDWQGAFGRTSI 220
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-215 3.47e-101

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: 291.76  E-value: 3.47e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364    1 MELYLDTANVAEVERLARVFPLAGVTTNPSIIAASRESIWEVLPRLQNAIgpKGRLFAQTMSRDAEGMVAEAKRLSNAIP 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAV--EGPVSAETISLDAEGMVEEAKELAKLAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   81 DIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAPES 160
Cdd:TIGR00875  79 NIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 522178364  161 KVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNAF 215
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAAF 213
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 2-212 4.92e-81

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: 240.55  E-value: 4.92e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   2 ELYLDTANVAEVERLARVFPLAGVTTNPSIIAAS-RESIWEVLPRLQNAIgpKGRLFAQTMSRDAEGMVAEAKRLSNAIP 80
Cdd:cd00956    1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSgRIDFEAVLKEICEII--DGPVSAQVVSTDAEGMVAEARKLASLGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  81 DIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAPES 160
Cdd:cd00956   79 NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 522178364 161 KVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWK 212
Cdd:cd00956  159 KILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQ 210
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-214 1.18e-75

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: 227.27  E-value: 1.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   1 MELYLDTANVAEVERLARVFPLAGVTTNPSIIA-ASRESIWEVLPRLQNAIgpKGRLFAQTMSRDAEGMVAEAKRLSNAI 79
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAkAGIKDFVEDIREICDIV--DGPVSAEVLATDTEGMIAEARRLAALY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  80 PD-IVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAP 158
Cdd:COG0176   79 RPnVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 522178364 159 ESKVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNA 214
Cdd:COG0176  159 RTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-218 2.60e-56

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: 178.50  E-value: 2.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364    3 LYLDTANVAEVERLARVFPLAGVTTNPSIIA---ASRESIWEVLPRLQNAIgpKGRLFAQTMSR---DAEGMVAEAKRLS 76
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLkaiEYSALYDEAIAEIKEIG--DGPVSLEVDPRladDTEGTIEEARRLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   77 NAI--PDIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGG----------DGIR 144
Cdd:pfam00923  79 ALYgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGDkrlgaalrgdDGIA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522178364  145 MVQELQSLLEQHAPESKVLAASFKTPRQALDclLAGCEAITLPLDVAQQMlgtpAVESAIEKFEQDWKNAFGNL 218
Cdd:pfam00923 159 NAKEIYQIYKKYGWSTGVLAASFRNVLYVLA--LAGCDTITIPPDTLEAL----AKDEGVRKFAKDWEKLLGSI 226
 
Name Accession Description Interval E-value
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-220 1.54e-116

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 330.97  E-value: 1.54e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   1 MELYLDTANVAEVERLARVFPLAGVTTNPSIIAASRESIWEVLPRLQNAIGPKGRLFAQTMSRDAEGMVAEAKRLSNAIP 80
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  81 DIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAPES 160
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364 161 KVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNAFGNLNL 220
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDWQGAFGRTSI 220
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-215 3.47e-101

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: 291.76  E-value: 3.47e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364    1 MELYLDTANVAEVERLARVFPLAGVTTNPSIIAASRESIWEVLPRLQNAIgpKGRLFAQTMSRDAEGMVAEAKRLSNAIP 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAV--EGPVSAETISLDAEGMVEEAKELAKLAP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   81 DIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAPES 160
Cdd:TIGR00875  79 NIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 522178364  161 KVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNAF 215
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAAF 213
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 2-212 4.92e-81

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: 240.55  E-value: 4.92e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   2 ELYLDTANVAEVERLARVFPLAGVTTNPSIIAAS-RESIWEVLPRLQNAIgpKGRLFAQTMSRDAEGMVAEAKRLSNAIP 80
Cdd:cd00956    1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSgRIDFEAVLKEICEII--DGPVSAQVVSTDAEGMVAEARKLASLGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  81 DIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAPES 160
Cdd:cd00956   79 NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 522178364 161 KVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWK 212
Cdd:cd00956  159 KILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQ 210
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-214 1.18e-75

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: 227.27  E-value: 1.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   1 MELYLDTANVAEVERLARVFPLAGVTTNPSIIA-ASRESIWEVLPRLQNAIgpKGRLFAQTMSRDAEGMVAEAKRLSNAI 79
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAkAGIKDFVEDIREICDIV--DGPVSAEVLATDTEGMIAEARRLAALY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  80 PD-IVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQHAP 158
Cdd:COG0176   79 RPnVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 522178364 159 ESKVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNA 214
Cdd:COG0176  159 RTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-218 2.60e-56

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: 178.50  E-value: 2.60e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364    3 LYLDTANVAEVERLARVFPLAGVTTNPSIIA---ASRESIWEVLPRLQNAIgpKGRLFAQTMSR---DAEGMVAEAKRLS 76
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLkaiEYSALYDEAIAEIKEIG--DGPVSLEVDPRladDTEGTIEEARRLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   77 NAI--PDIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGG----------DGIR 144
Cdd:pfam00923  79 ALYgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGDkrlgaalrgdDGIA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522178364  145 MVQELQSLLEQHAPESKVLAASFKTPRQALDclLAGCEAITLPLDVAQQMlgtpAVESAIEKFEQDWKNAFGNL 218
Cdd:pfam00923 159 NAKEIYQIYKKYGWSTGVLAASFRNVLYVLA--LAGCDTITIPPDTLEAL----AKDEGVRKFAKDWEKLLGSI 226
Transaldolase cd00439
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
 2-211 9.81e-53

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: 170.22  E-value: 9.81e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   2 ELYLDTANVAEVERLARVFPLAGVTTNPSIIAASRE---------------------SIWE-----------VLPRLQNA 49
Cdd:cd00439    1 SPWYDTLDRPATDLLPLIRGVRGVTTNPSIIQAAIStsnayndqfrtlvesgkdiesAYWElvvkdiqdackLFEPIYDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  50 IGPKGRLFAQTMSR---DAEGMVAEAKRLSNAI--PDIVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAG 124
Cdd:cd00439   81 TEADGRVSVEVSARladDTQGMVEAAKYLSKVVnrRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364 125 AKYVAPYVNRVDAQGGD-------------GIRMVQELQSLLEQHAPESKVLAASFKTPRQALDCLlaGCEAITLPLDVA 191
Cdd:cd00439  161 TSVASPFVSRIDTLMDKmleqigldlrgkaGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLI--GCDTVTTMPDQA 238

                        250       260
                 ....*....|....*....|
gi 522178364 192 QQMlgtpavesAIEKFEQDW 211
Cdd:cd00439  239 LEA--------GVDKFKKDF 250
PRK12656 PRK12656
fructose-6-phosphate aldolase; Reviewed
 1-216 6.92e-46

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183656 [Multi-domain]  Cd Length: 222  Bit Score: 151.82  E-value: 6.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   1 MELYLDTANVAEVERLARVFPLAGVTTNPSIiaASRE---SIWEVLPRLQNAIGPKGRLFAQTMSRDAEGMVAEAKRLSN 77
Cdd:PRK12656   1 MEFMLDTLNLEAIKKWHEILPLAGVTSNPSI--AKKEgdiDFFERIREVREIIGDEASIHVQVVAQDYEGILKDAHEIRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  78 AIPD-IVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVNRVDAQGGDGIRMVQELQSLLEQH 156
Cdd:PRK12656  79 QCGDdVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENLNIDSNAVIGQLAEAIDRE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364 157 APESKVLAASFKTPRQALDCLLAGCEAITLPLDVAQQMLGTPAVESAIEKFEQDWKNAFG 216
Cdd:PRK12656 159 NSDSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFADDWEAIHG 218
PTZ00411 PTZ00411
transaldolase-like protein; Provisional
 61-199 1.35e-07

transaldolase-like protein; Provisional


Pssm-ID: 240406  Cd Length: 333  Bit Score: 50.89  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  61 MSRDAEGMVAEAKRL-----SNAIPD--IVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVN 133
Cdd:PTZ00411 111 LSFDKQAMVDKARKIikmyeEAGISKdrILIKLASTWEGIQAAKALEKEGIHCNLTLLFSFAQAVACAQAGVTLISPFVG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522178364 134 RV-----DAQGGD--------GIRMVQELQSLLEQHAPESKVLAASFKTPRQALDclLAGCEAITLPLDVAQQMLGTPA 199
Cdd:PTZ00411 191 RIldwykKPEKAEsyvgaqdpGVISVTKIYNYYKKHGYKTIVMGASFRNTGEILE--LAGCDKLTISPKLLEELANTED 267
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
 24-113 1.50e-07

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: 50.79  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  24 GVTTNPSI----IAASR----------------ESIWEVLPR--LQNAIGPKGRLFAQT--------------MSRDAEG 67
Cdd:cd00955   28 GVTSNPAIfekaIAGSAayddqiralkgqgldaEAIYEALAIedIQDACDLLAPVYEQTggndgyvslevsprLADDTQG 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 522178364  68 MVAEAKRLSNAI--PDIVVKIPVTAQGLIAIKALKTAGITTLGTAVYS 113
Cdd:cd00955  108 TIAEAKRLWKAVgrPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFS 155
PRK03903 PRK03903
transaldolase; Provisional
 64-113 8.48e-07

transaldolase; Provisional


Pssm-ID: 235171  Cd Length: 274  Bit Score: 48.44  E-value: 8.48e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 522178364  64 DAEGMVAEAKRLSNAI--PDIVVKIPVTAQGLIAIKALKTAGITTLGTAVYS 113
Cdd:PRK03903  56 DAAGSIEEGKRLYKTIgrPNVMIKVPATKAGYEAMSALMKKGISVNATLIFS 107
PRK03343 PRK03343
transaldolase; Validated
 12-104 8.97e-07

transaldolase; Validated


Pssm-ID: 235117  Cd Length: 368  Bit Score: 48.66  E-value: 8.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  12 EVERLARVFPLAGVTTNPSI----IAASR----------------ESIWE--VLPRLQNAIGPKGRLFAQT--------- 60
Cdd:PRK03343  29 NLARLIDEKGVVGVTSNPAIfqkaIAGGDaydaqiaelaaagadvEEAYEelTTADVRNACDVLRPVYEATggvdgrvsi 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 522178364  61 -----MSRDAEGMVAEAKRLSNAI--PDIVVKIPVTAQGLIAIKALKTAGI 104
Cdd:PRK03343 109 evsprLAHDTEATIAEARRLWAAVdrPNLMIKIPATPEGLPAIEALIAEGI 159
Transaldolase_TalAB cd00957
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ...
 6-195 2.74e-06

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: 46.84  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364   6 DTANVAEVERlarvFPLAGVTTNPSIIAAS------------------------RESIWEVLPRLQNAIGPK------GR 55
Cdd:cd00957   15 DTGDFEAIKK----FKPQDATTNPSLILAAaklpeynklvdeaiayakkkggsdEDQISNALDKLLVNFGTEilklipGR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  56 LFAQTMSR---DAEGMVAEAKRLSN-----AIPD--IVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGA 125
Cdd:cd00957   91 VSTEVDARlsfDTNATIAKARKLIKlyeeaGIDKerILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAVACAEAGV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364 126 KYVAPYVNRV-D---AQGGD---------GIRMVQELQSLLEQHAPESKVLAASFKTPRQALDclLAGCEAITLPLDVAQ 192
Cdd:cd00957  171 TLISPFVGRIlDwykKHSGDkaytaeedpGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILA--LAGCDYLTISPALLE 248


                 ...
gi 522178364 193 QML 195
Cdd:cd00957  249 ELK 251
PRK09533 PRK09533
bifunctional transaldolase/phosoglucose isomerase; Validated
 63-104 1.91e-05

bifunctional transaldolase/phosoglucose isomerase; Validated


Pssm-ID: 236551 [Multi-domain]  Cd Length: 948  Bit Score: 44.96  E-value: 1.91e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 522178364  63 RDAEGMVAEAKRLSNAI--PDIVVKIPVTAQGLIAIKALKTAGI 104
Cdd:PRK09533 116 LDTEGTIAEARRLWAAVdrPNLMIKVPATPEGLPAIRQLIAEGI 159
PRK12346 PRK12346
transaldolase A; Provisional
 61-186 9.94e-04

transaldolase A; Provisional


Pssm-ID: 183458  Cd Length: 316  Bit Score: 39.32  E-value: 9.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522178364  61 MSRDAEGMVAEAKRL-----SNAIPD--IVVKIPVTAQGLIAIKALKTAGITTLGTAVYSAAQGLLAALAGAKYVAPYVN 133
Cdd:PRK12346 100 LSFDREKSIEKARHLvdlyqQQGIDKsrILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEAGVFLISPFVG 179

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522178364 134 RV-------------DAQGGDGIRMVQELQSLLEQHAPESKVLAASFKTPRQALDclLAGCEAITL 186
Cdd:PRK12346 180 RIydwyqarkpmdpyVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILA--LAGCDRLTI 243
 
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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