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Conserved domains on  [gi|1242549958|gb|ATA70767|]
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fructose-6-phosphate aldolase [Capnocytophaga sputigena]

Protein Classification

transaldolase family protein( domain architecture ID 10097258)

transaldolase family protein such as transaldolase, which is important for the balance of metabolites in the pentose-phosphate pathway and catalyzes the reversible transfer of a three-carbon ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate

CATH:  3.20.20.70
EC:  2.2.1.2
PubMed:  22212631|12206759
SCOP:  4003216

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 2-215 2.15e-111

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: 317.59  E-value: 2.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   2 KFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGitgKAAILQHYKNICEIVEGDVSAEVIATDFEGIVREGEELAALH 81
Cdd:cd00956     1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSG---RIDFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEARKLASLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  82 PQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNYNFE 161
Cdd:cd00956    78 GNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242549958 162 TQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLADAKK 215
Cdd:cd00956   158 TKILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
 
Name Accession Description Interval E-value
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 2-215 2.15e-111

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: 317.59  E-value: 2.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   2 KFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGitgKAAILQHYKNICEIVEGDVSAEVIATDFEGIVREGEELAALH 81
Cdd:cd00956     1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSG---RIDFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEARKLASLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  82 PQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNYNFE 161
Cdd:cd00956    78 GNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242549958 162 TQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLADAKK 215
Cdd:cd00956   158 TKILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-216 6.11e-109

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: 311.24  E-value: 6.11e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   1 MKFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGITGkaaILQHYKNICEIVEGDVSAEVIATDFEGIVREGEELAAL 80
Cdd:COG0176     1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAGIKD---FVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  81 -HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNYN 159
Cdd:COG0176    78 yRPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1242549958 160 FETQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLADAKKL 216
Cdd:COG0176   158 ARTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-212 3.21e-94

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: 274.04  E-value: 3.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   1 MKFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGITgkaaILQHYKNICEIVEGDVSAEVIATDFEGIVREGEELAAL 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRS----FWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  81 HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNYNF 160
Cdd:TIGR00875  77 APNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAP 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242549958 161 ETQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLAD 212
Cdd:TIGR00875 157 DTEVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKD 208
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-217 7.21e-76

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: 228.19  E-value: 7.21e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   3 FFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEgITGKAAILQHYKNICEIVEGDVSAEVIA---TDFEGIVREGEELAA 79
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKA-IEYSALYDEAIAEIKEIGDGPVSLEVDPrlaDDTEGTIEEARRLIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  80 LH--PQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDI----------SADGLSL 147
Cdd:pfam00923  80 LYgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWgdkrlgaalrGDDGIAN 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 148 IEEIRLIYDNYNFETQILAASVRHTMHILecAKIGADVITAPLSAITGLLKhpltDSGLAQFLADAKKLG 217
Cdd:pfam00923 160 AKEIYQIYKKYGWSTGVLAASFRNVLYVL--ALAGCDTITIPPDTLEALAK----DEGVRKFAKDWEKLL 223
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-212 8.79e-44

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 146.08  E-value: 8.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   1 MKFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKegitGKAAILQHYKNICEIVEGD--VSAEVIATDFEGIVREGEELA 78
Cdd:PRK12653    1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAA----GKKPLEVVLPQLHEAMGGQgrLFAQVMATTAEGMVNDARKLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  79 ALHPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNY 158
Cdd:PRK12653   77 SIIADIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242549958 159 NFETQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLAD 212
Cdd:PRK12653  157 APQAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQD 210
 
Name Accession Description Interval E-value
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 2-215 2.15e-111

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: 317.59  E-value: 2.15e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   2 KFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGitgKAAILQHYKNICEIVEGDVSAEVIATDFEGIVREGEELAALH 81
Cdd:cd00956     1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSG---RIDFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEARKLASLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  82 PQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNYNFE 161
Cdd:cd00956    78 GNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242549958 162 TQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLADAKK 215
Cdd:cd00956   158 TKILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-216 6.11e-109

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: 311.24  E-value: 6.11e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   1 MKFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGITGkaaILQHYKNICEIVEGDVSAEVIATDFEGIVREGEELAAL 80
Cdd:COG0176     1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAGIKD---FVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  81 -HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNYN 159
Cdd:COG0176    78 yRPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1242549958 160 FETQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLADAKKL 216
Cdd:COG0176   158 ARTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-212 3.21e-94

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: 274.04  E-value: 3.21e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   1 MKFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGITgkaaILQHYKNICEIVEGDVSAEVIATDFEGIVREGEELAAL 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRS----FWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  81 HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNYNF 160
Cdd:TIGR00875  77 APNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAP 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242549958 161 ETQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLAD 212
Cdd:TIGR00875 157 DTEVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKD 208
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-217 7.21e-76

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: 228.19  E-value: 7.21e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   3 FFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEgITGKAAILQHYKNICEIVEGDVSAEVIA---TDFEGIVREGEELAA 79
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKA-IEYSALYDEAIAEIKEIGDGPVSLEVDPrlaDDTEGTIEEARRLIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  80 LH--PQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDI----------SADGLSL 147
Cdd:pfam00923  80 LYgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWgdkrlgaalrGDDGIAN 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 148 IEEIRLIYDNYNFETQILAASVRHTMHILecAKIGADVITAPLSAITGLLKhpltDSGLAQFLADAKKLG 217
Cdd:pfam00923 160 AKEIYQIYKKYGWSTGVLAASFRNVLYVL--ALAGCDTITIPPDTLEALAK----DEGVRKFAKDWEKLL 223
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-212 8.79e-44

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 146.08  E-value: 8.79e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   1 MKFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKegitGKAAILQHYKNICEIVEGD--VSAEVIATDFEGIVREGEELA 78
Cdd:PRK12653    1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAA----GKKPLEVVLPQLHEAMGGQgrLFAQVMATTAEGMVNDARKLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  79 ALHPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDNY 158
Cdd:PRK12653   77 SIIADIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMH 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1242549958 159 NFETQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLAD 212
Cdd:PRK12653  157 APQAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQD 210
PRK12656 PRK12656
fructose-6-phosphate aldolase; Reviewed
 1-212 5.42e-29

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183656 [Multi-domain]  Cd Length: 222  Bit Score: 107.90  E-value: 5.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   1 MKFFIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGitgKAAILQHYKNICEIV--EGDVSAEVIATDFEGIVREGEEL- 77
Cdd:PRK12656    1 MEFMLDTLNLEAIKKWHEILPLAGVTSNPSIAKKEG---DIDFFERIREVREIIgdEASIHVQVVAQDYEGILKDAHEIr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  78 AALHPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGRLDDISADGLSLIEEIRLIYDN 157
Cdd:PRK12656   78 RQCGDDVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENLNIDSNAVIGQLAEAIDR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1242549958 158 YNFETQILAASVRHTMHILECAKIGADVITAPLSAITGLLKHPLTDSGLAQFLAD 212
Cdd:PRK12656  158 ENSDSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFADD 212
Transaldolase_TalAB cd00957
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ...
 5-190 8.37e-23

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: 93.45  E-value: 8.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   5 IDTANLSQIQEAQdlgvLDGVTTNPSLmakegITgKAAILQHYKNI-------------------------------CEI 53
Cdd:cd00957    14 ADTGDFEAIKKFK----PQDATTNPSL-----IL-AAAKLPEYNKLvdeaiayakkkggsdedqisnaldkllvnfgTEI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  54 ---VEGDVSAEV---IATDFEGIVREGEELAAL-------HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQAL 120
Cdd:cd00957    84 lklIPGRVSTEVdarLSFDTNATIAKARKLIKLyeeagidKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 121 LAAKAGATYVSPFIGRLDD------------ISAD-GLSLIEEIRLIYDNYNFETQILAASVRHTMHILECAkiGADVIT 187
Cdd:cd00957   164 ACAEAGVTLISPFVGRILDwykkhsgdkaytAEEDpGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALA--GCDYLT 241


                  ...
gi 1242549958 188 APL 190
Cdd:cd00957   242 ISP 244
Transaldolase cd00439
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
 4-215 2.05e-22

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: 91.64  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   4 FIDTANLSQIQEAQDLGVLDGVTTNPSLMAKEGITGKAAILQH----------------------------YKNICEIVE 55
Cdd:cd00439     3 WYDTLDRPATDLLPLIRGVRGVTTNPSIIQAAISTSNAYNDQFrtlvesgkdiesaywelvvkdiqdacklFEPIYDQTE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  56 GD--VSAEV---IATDFEGIVREGEELAAL--HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGAT 128
Cdd:cd00439    83 ADgrVSVEVsarLADDTQGMVEAAKYLSKVvnRRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADAGTS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 129 YVSPFIGRLDD--------ISAD--GLSLIEEIRLIYDNYN---FETQILAASVRHTMHILECakIGADVITAPLSAitg 195
Cdd:cd00439   163 VASPFVSRIDTlmdkmleqIGLDlrGKAGVAQVTLAYKLYKqkfKKQRVLWASFSDTLYVAPL--IGCDTVTTMPDQ--- 237

                         250       260
                  ....*....|....*....|
gi 1242549958 196 llkhpLTDSGLAQFLADAKK 215
Cdd:cd00439   238 -----ALEAGVDKFKKDFES 252
PRK12346 PRK12346
transaldolase A; Provisional
 26-187 4.91e-19

transaldolase A; Provisional


Pssm-ID: 183458  Cd Length: 316  Bit Score: 83.23  E-value: 4.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  26 TTNPSLMAKegitgkAAILQHYKN----------------------------------ICEIVEGDVSAEVIAT---DFE 68
Cdd:PRK12346   32 TTNPSLLLK------AAGLPQYQHliddaiawgkkqggtqeqqvvaacdklavnfgaeILKSVPGRVSTEVDARlsfDRE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  69 GIVREGEELAALHPQ-------IVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGATYVSPFIGR----- 136
Cdd:PRK12346  106 KSIEKARHLVDLYQQqgidksrILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRiydwy 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1242549958 137 -----LDDISADGLSLIEEIRLIYDNY---NFETQILAASVRHTMHILECAkiGADVIT 187
Cdd:PRK12346  186 qarkpMDPYVVEEDPGVKSVRNIYDYYkqhRYETIVMGASFRRTEQILALA--GCDRLT 242
PTZ00411 PTZ00411
transaldolase-like protein; Provisional
 5-189 3.24e-18

transaldolase-like protein; Provisional


Pssm-ID: 240406  Cd Length: 333  Bit Score: 81.32  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   5 IDTANLSQIQEAQDlgvlDGVTTNPSLMAK------------EGIT-GKAAILQHYKN---------------------- 49
Cdd:PTZ00411   16 ADTGDFSLLKKFQP----EDATTNPSLVLAaaqmpeyahlidDAIKyAKANVSRLRDPllsdeekeelvelvvdkltvnf 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  50 ---ICEIVEGDVSAEVIAT---DFEGIVREGEELAALHPQ-------IVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSA 116
Cdd:PTZ00411   92 gveILKIVPGRVSTEVDARlsfDKQAMVDKARKIIKMYEEagiskdrILIKLASTWEGIQAAKALEKEGIHCNLTLLFSF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 117 GQALLAAKAGATYVSPFIGRLDDISAD-------------GLSLIEEIRLIYDNYNFETQILAASVRHTMHILECAkiGA 183
Cdd:PTZ00411  172 AQAVACAQAGVTLISPFVGRILDWYKKpekaesyvgaqdpGVISVTKIYNYYKKHGYKTIVMGASFRNTGEILELA--GC 249


                  ....*.
gi 1242549958 184 DVITAP 189
Cdd:PTZ00411  250 DKLTIS 255
PRK05269 PRK05269
transaldolase B; Provisional
 6-208 4.37e-17

transaldolase B; Provisional


Pssm-ID: 235381 [Multi-domain]  Cd Length: 318  Bit Score: 77.89  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   6 DTANLSQIQ--EAQDlgvldgVTTNPSLmakegITgKAAILQHYKNI-------------------------------CE 52
Cdd:PRK05269   17 DTGDIEAIKkyQPQD------ATTNPSL-----IL-KAAQIPEYAPLiddavawakqqsgdraqqiddaidklavnfgLE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  53 I---VEGDVSAEVIAT---DFEGIVREGEELAALHPQ-------IVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQA 119
Cdd:PRK05269   85 IlklIPGRVSTEVDARlsfDTEATIAKARKLIALYEEagiskdrILIKIASTWEGIRAAEQLEKEGINCNLTLLFSFAQA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 120 LLAAKAGATYVSPFIGRLDD---ISADGLSL-IEE------IRLIYDNY---NFETQILAASVRHTMHILECAkiGADVI 186
Cdd:PRK05269  165 RACAEAGVFLISPFVGRILDwykKNTGKKEYaPAEdpgvvsVTKIYNYYkkhGYKTVVMGASFRNTGQILELA--GCDRL 242

                         250       260
                  ....*....|....*....|....*...
gi 1242549958 187 T-AP-----LSAITGLLKHPLTDSGLAQ 208
Cdd:PRK05269  243 TiSPalleeLAASEGELERKLSPPGEAK 270
PRK12309 PRK12309
transaldolase;
48-187 1.66e-16

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 77.08  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  48 KNICEIVEGDVSAEVIAT---DFEGIVREGEELAALH-------PQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAG 117
Cdd:PRK12309   87 LKILKIVPGRVSTEVDARlsyDTEATIAKARKLISLYedagisrDRVLIKIASTWEGIKAAEVLEKEGIHCNLTLLFGFH 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 118 QALLAAKAGATYVSPFIGR-LDDISAD------------GLSLIEEIRLIYDNYNFETQILAASVRHTMHILECAkiGAD 184
Cdd:PRK12309  167 QAIACAEAGVTLISPFVGRiLDWYKKEtgrdsypgaedpGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIELA--GCD 244


                  ...
gi 1242549958 185 VIT 187
Cdd:PRK12309  245 LLT 247
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
 4-141 2.13e-09

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: 56.18  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   4 FIDTANLSQIQEAQdlGVlDGVTTNPSLMAK-----------------EGITGKAA----ILQHYKNICEIVE------- 55
Cdd:cd00955    11 FIDNGFLKRLIEEQ--GV-VGVTSNPAIFEKaiagsaayddqiralkgQGLDAEAIyealAIEDIQDACDLLApvyeqtg 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  56 ---GDVSAEV---IATDFEGIVREGEEL--AALHPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKAGA 127
Cdd:cd00955    88 gndGYVSLEVsprLADDTQGTIAEAKRLwkAVGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYEAVAEAYL 167

                         170
                  ....*....|....
gi 1242549958 128 TYVSPFIGRLDDIS 141
Cdd:cd00955   168 RGLERRVEGGGDLS 181
PRK03343 PRK03343
transaldolase; Validated
 5-125 1.75e-07

transaldolase; Validated


Pssm-ID: 235117  Cd Length: 368  Bit Score: 50.59  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   5 IDTANLSQIQEAQDLGvldGVTTNPSLMAK-----------------EGITGKAAI----LQHYKNICEI---------- 53
Cdd:PRK03343   25 LTSGNLARLIDEKGVV---GVTSNPAIFQKaiaggdaydaqiaelaaAGADVEEAYeeltTADVRNACDVlrpvyeatgg 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242549958  54 VEGDVSAEV---IATDFEGIVREGEELAAL--HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQALLAAKA 125
Cdd:PRK03343  102 VDGRVSIEVsprLAHDTEATIAEARRLWAAvdRPNLMIKIPATPEGLPAIEALIAEGISVNVTLIFSVERYRAVADA 178
PRK09533 PRK09533
bifunctional transaldolase/phosoglucose isomerase; Validated
 4-138 1.23e-06

bifunctional transaldolase/phosoglucose isomerase; Validated


Pssm-ID: 236551 [Multi-domain]  Cd Length: 948  Bit Score: 48.43  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958   4 FIDTANLSQIQEAQDLgvlDGVTTNPSLMAKeGITG--------KAAILQHYKNICEIVE-------------------- 55
Cdd:PRK09533   23 FIAKGELKRLVEEDGL---RGVTSNPAIFEK-AIGSsdeyddaiKAALAEGDRSVIELYEtlaiediqaaadvlrpvyda 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  56 -----GDVSAEV---IATDFEGIVREGEEL-AAL-HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFS---------- 115
Cdd:PRK09533   99 tdgadGFVSLEVspyLALDTEGTIAEARRLwAAVdRPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFSqdvyeevaea 178

                         170       180       190
                  ....*....|....*....|....*....|
gi 1242549958 116 --AGQALLAAKAG-----ATYVSPFIGRLD 138
Cdd:PRK09533  179 yiSGLEARAAKGGdpshvASVASFFVSRID 208
PRK03903 PRK03903
transaldolase; Provisional
 56-217 2.95e-06

transaldolase; Provisional


Pssm-ID: 235171  Cd Length: 274  Bit Score: 46.51  E-value: 2.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958  56 GDVSAEV---IATDFEGIVREGEELAAL--HPQIVVKVPMIKDGIKAIKYFTDKGIRTNCTLVFSAGQA---LLAAKAGA 127
Cdd:PRK03903   43 GFISIEIdpfLEDDAAGSIEEGKRLYKTigRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAkecAEALNEGL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242549958 128 --------TYVSPFIGRLD-----DISADGLSL-------IEEIRLIYDNYNFETQILAAS-------VRHTMHILE-CA 179
Cdd:PRK03903  123 kkntkdpkAVISVFVSRFDrlldpKLAPKNLQAksgimnaTKCYNQIEQHANKNIRTLFAStgvkgddLPKDYYIKElLF 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1242549958 180 KigADVITAPLSAITGLL-------KHPLTDSGLAQFLADAKKLG 217
Cdd:PRK03903  203 K--NSINTAPLDTIEAFLkdgntepKKPLKIEEIEAFFKELKSHN 245
 
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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