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Conserved domains on  [gi|521289019|ref|WP_020453287|]
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MULTISPECIES: fructose-6-phosphate aldolase [Bacillus]

Protein Classification

transaldolase family protein( domain architecture ID 17615348)

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, or fructose-6-P aldolase, which catalyzes an aldol cleavage of fructose 6-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-211 7.66e-121

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: 341.45  E-value: 7.66e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019    1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENISFHDRLREITEVVSGSVSAEVISLKAEEMIEEGKELAKIAPNI 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKLAPNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   81 TVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDTQI 160
Cdd:TIGR00875  81 VVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDTEV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 521289019  161 IAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADWNK 211
Cdd:TIGR00875 161 IAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNA 211
 
Name Accession Description Interval E-value
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-211 7.66e-121

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: 341.45  E-value: 7.66e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019    1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENISFHDRLREITEVVSGSVSAEVISLKAEEMIEEGKELAKIAPNI 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKLAPNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   81 TVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDTQI 160
Cdd:TIGR00875  81 VVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDTEV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 521289019  161 IAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADWNK 211
Cdd:TIGR00875 161 IAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNA 211
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 3-211 5.05e-115

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: 326.45  E-value: 5.05e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   3 FFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENIS-FHDRLREITEVVSGSVSAEVISLKAEEMIEEGKELAKIAPNIT 81
Cdd:cd00956    2 IFLDTADLEEIKKASETGLLDGVTTNPSLIAKSGRIdFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEARKLASLGGNVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  82 VKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDTQII 161
Cdd:cd00956   82 VKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDTKIL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 521289019 162 AASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADWNK 211
Cdd:cd00956  162 AASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-211 1.14e-112

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: 320.48  E-value: 1.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENI-SFHDRLREITEVVSGSVSAEVISLKAEEMIEEGKELAKI-AP 78
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAGIkDFVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAALyRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  79 NITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDT 158
Cdd:COG0176   81 NVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGART 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521289019 159 QIIAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADWNK 211
Cdd:COG0176  161 RILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEK 213
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-211 4.58e-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: 4.58e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019    3 FFIDTANLDEIKEAHALGVLAGVTTNPSLVAKE---NISFHDRLREITEVVSGSVSAEVISL---KAEEMIEEGKELAKI 76
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKAieySALYDEAIAEIKEIGDGPVSLEVDPRladDTEGTIEEARRLIAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   77 A--PNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIG----------HNGLDLI 144
Cdd:pfam00923  81 YgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGdkrlgaalrgDDGIANA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521289019  145 SEIKQIFDVHGLDTQIIAASIRHAQHVTEAAlrGAHIGTMPLKVIHQLtkhpLTDKGIEQFLADWNK 211
Cdd:pfam00923 161 KEIYQIYKKYGWSTGVLAASFRNVLYVLALA--GCDTITIPPDTLEAL----AKDEGVRKFAKDWEK 221
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-209 1.23e-49

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 160.72  E-value: 1.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENISFHDRLREITEVVSGS--VSAEVISLKAEEMIEEGKELAKIAP 78
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQgrLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  79 NITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDT 158
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521289019 159 QIIAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADW 209
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDW 211
 
Name Accession Description Interval E-value
fsa_talC_mipB TIGR00875
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ...
 1-211 7.66e-121

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: 341.45  E-value: 7.66e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019    1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENISFHDRLREITEVVSGSVSAEVISLKAEEMIEEGKELAKIAPNI 80
Cdd:TIGR00875   1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKLAPNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   81 TVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDTQI 160
Cdd:TIGR00875  81 VVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDTEV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 521289019  161 IAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADWNK 211
Cdd:TIGR00875 161 IAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNA 211
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 3-211 5.05e-115

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: 326.45  E-value: 5.05e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   3 FFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENIS-FHDRLREITEVVSGSVSAEVISLKAEEMIEEGKELAKIAPNIT 81
Cdd:cd00956    2 IFLDTADLEEIKKASETGLLDGVTTNPSLIAKSGRIdFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEARKLASLGGNVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  82 VKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDTQII 161
Cdd:cd00956   82 VKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDTKIL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 521289019 162 AASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADWNK 211
Cdd:cd00956  162 AASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 1-211 1.14e-112

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: 320.48  E-value: 1.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENI-SFHDRLREITEVVSGSVSAEVISLKAEEMIEEGKELAKI-AP 78
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAGIkDFVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAALyRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  79 NITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDT 158
Cdd:COG0176   81 NVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGART 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521289019 159 QIIAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADWNK 211
Cdd:COG0176  161 RILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEK 213
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 3-211 4.58e-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: 4.58e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019    3 FFIDTANLDEIKEAHALGVLAGVTTNPSLVAKE---NISFHDRLREITEVVSGSVSAEVISL---KAEEMIEEGKELAKI 76
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKAieySALYDEAIAEIKEIGDGPVSLEVDPRladDTEGTIEEARRLIAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   77 A--PNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIG----------HNGLDLI 144
Cdd:pfam00923  81 YgrPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGdkrlgaalrgDDGIANA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521289019  145 SEIKQIFDVHGLDTQIIAASIRHAQHVTEAAlrGAHIGTMPLKVIHQLtkhpLTDKGIEQFLADWNK 211
Cdd:pfam00923 161 KEIYQIYKKYGWSTGVLAASFRNVLYVLALA--GCDTITIPPDTLEAL----AKDEGVRKFAKDWEK 221
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 1-209 1.23e-49

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 160.72  E-value: 1.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKENISFHDRLREITEVVSGS--VSAEVISLKAEEMIEEGKELAKIAP 78
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQgrLFAQVMATTAEGMVNDARKLRSIIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  79 NITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGLDT 158
Cdd:PRK12653  81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521289019 159 QIIAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADW 209
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDW 211
PRK12656 PRK12656
fructose-6-phosphate aldolase; Reviewed
 1-209 4.03e-39

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183656 [Multi-domain]  Cd Length: 222  Bit Score: 134.10  E-value: 4.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   1 MLFFIDTANLDEIKEAHALGVLAGVTTNPSLVAKE-NISFHDRLREITEVV--SGSVSAEVISLKAEEMIEEGKELAKIA 77
Cdd:PRK12656   1 MEFMLDTLNLEAIKKWHEILPLAGVTSNPSIAKKEgDIDFFERIREVREIIgdEASIHVQVVAQDYEGILKDAHEIRRQC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  78 P-NITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGRLDDIGHNGLDLISEIKQIFDVHGL 156
Cdd:PRK12656  81 GdDVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENLNIDSNAVIGQLAEAIDRENS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521289019 157 DTQIIAASIRHAQHVTEAALRGAHIGTMPLKVIHQLTKHPLTDKGIEQFLADW 209
Cdd:PRK12656 161 DSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFADDW 213
Transaldolase cd00439
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
 4-211 3.62e-25

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: 98.58  E-value: 3.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   4 FIDTANLDEIKEAHALGVLAGVTTNPSLVAK-ENISFHDRLREITEVVS------------------------------- 51
Cdd:cd00439    3 WYDTLDRPATDLLPLIRGVRGVTTNPSIIQAaISTSNAYNDQFRTLVESgkdiesaywelvvkdiqdacklfepiydqte 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  52 --GSVSAEV---ISLKAEEMIEEGKELAKI--APNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGAT 124
Cdd:cd00439   83 adGRVSVEVsarLADDTQGMVEAAKYLSKVvnRRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADAGTS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019 125 YVSPFLGRLDDIGHNGLDLISE-------IKQIFDVHGL------DTQIIAASIRHAQHVteAALRGAHIGTMPLKVIHQ 191
Cdd:cd00439  163 VASPFVSRIDTLMDKMLEQIGLdlrgkagVAQVTLAYKLykqkfkKQRVLWASFSDTLYV--APLIGCDTVTTMPDQALE 240

                        250       260
                 ....*....|....*....|
gi 521289019 192 LtkhpltdkGIEQFLADWNK 211
Cdd:cd00439  241 A--------GVDKFKKDFES 252
Transaldolase_TalAB cd00957
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ...
 5-200 3.71e-25

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: 99.61  E-value: 3.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   5 IDTANLDEIKE---AHAlgvlagvTTNPSLVAKE---------------------------NISFHDRLR-----EITEV 49
Cdd:cd00957   14 ADTGDFEAIKKfkpQDA-------TTNPSLILAAaklpeynklvdeaiayakkkggsdedqISNALDKLLvnfgtEILKL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  50 VSGSVSAEV---ISLKAEEMIEEGKELAK------IAPN-ITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAA 119
Cdd:cd00957   87 IPGRVSTEVdarLSFDTNATIAKARKLIKlyeeagIDKErILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAVACA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019 120 RAGATYVSPFLGRLDD--IGHN-----------GLDLISEIKQIFDVHGLDTQIIAASIRHAQHVTEAAlrGAHIGTMPL 186
Cdd:cd00957  167 EAGVTLISPFVGRILDwyKKHSgdkaytaeedpGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALA--GCDYLTISP 244

                        250
                 ....*....|....*.
gi 521289019 187 KVIHQL--TKHPLTDK 200
Cdd:cd00957  245 ALLEELknSTAKVERK 260
PTZ00411 PTZ00411
transaldolase-like protein; Provisional
 5-198 2.38e-21

transaldolase-like protein; Provisional


Pssm-ID: 240406  Cd Length: 333  Bit Score: 89.80  E-value: 2.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   5 IDTANLDEIKEAHAlgvlAGVTTNPSLV-------------------AKENISFH------------------DRLR--- 44
Cdd:PTZ00411  16 ADTGDFSLLKKFQP----EDATTNPSLVlaaaqmpeyahliddaikyAKANVSRLrdpllsdeekeelvelvvDKLTvnf 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  45 --EITEVVSGSVSAEV---ISLKAEEMIEEGKELAKI-------APNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSA 112
Cdd:PTZ00411  92 gvEILKIVPGRVSTEVdarLSFDKQAMVDKARKIIKMyeeagisKDRILIKLASTWEGIQAAKALEKEGIHCNLTLLFSF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019 113 NQALLAARAGATYVSPFLGRLDDIGHN-------------GLDLISEIKQIFDVHGLDTQIIAASIRHAQHVTEaaLRGA 179
Cdd:PTZ00411 172 AQAVACAQAGVTLISPFVGRILDWYKKpekaesyvgaqdpGVISVTKIYNYYKKHGYKTIVMGASFRNTGEILE--LAGC 249

                        250
                 ....*....|....*....
gi 521289019 180 HIGTMPLKVIHQLTKHPLT 198
Cdd:PTZ00411 250 DKLTISPKLLEELANTEDG 268
PRK05269 PRK05269
transaldolase B; Provisional
 6-175 2.08e-19

transaldolase B; Provisional


Pssm-ID: 235381 [Multi-domain]  Cd Length: 318  Bit Score: 84.06  E-value: 2.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   6 DTANLDEIK-----EAhalgvlagvTTNPSLV-------------------AKENISFH--------DRL-----REITE 48
Cdd:PRK05269  17 DTGDIEAIKkyqpqDA---------TTNPSLIlkaaqipeyapliddavawAKQQSGDRaqqiddaiDKLavnfgLEILK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  49 VVSGSVSAEV---ISLKAEEMIEEGKEL------AKIAPN-ITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLA 118
Cdd:PRK05269  88 LIPGRVSTEVdarLSFDTEATIAKARKLialyeeAGISKDrILIKIASTWEGIRAAEQLEKEGINCNLTLLFSFAQARAC 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019 119 ARAGATYVSPFLGR-----------LDDIGHN--GLDLISEIKQIFDVHGLDTQIIAASIRHAQHVTEAA 175
Cdd:PRK05269 168 AEAGVFLISPFVGRildwykkntgkKEYAPAEdpGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELA 237
PRK12309 PRK12309
transaldolase;
22-200 4.70e-17

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 78.24  E-value: 4.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  22 LAGVTTNPSLVAKENIsfhDRL-----REITEVVSGSVSAEV---ISLKAEEMIEEGKEL------AKIAPN-ITVKIPM 86
Cdd:PRK12309  63 ELGSDAPVEDVVALAF---DRLavafgLKILKIVPGRVSTEVdarLSYDTEATIAKARKLislyedAGISRDrVLIKIAS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  87 TSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGATYVSPFLGR-LD----DIGHN--------GLDLISEIKQIFDV 153
Cdd:PRK12309 140 TWEGIKAAEVLEKEGIHCNLTLLFGFHQAIACAEAGVTLISPFVGRiLDwykkETGRDsypgaedpGVQSVTQIYNYYKK 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 521289019 154 HGLDTQIIAASIRHAQHVTEAAlrGAHIGTMPLKVIHQL--TKHPLTDK 200
Cdd:PRK12309 220 FGYKTEVMGASFRNIGEIIELA--GCDLLTISPKLLEQLrsTEAELPRK 266
PRK12346 PRK12346
transaldolase A; Provisional
 6-175 2.38e-13

transaldolase A; Provisional


Pssm-ID: 183458  Cd Length: 316  Bit Score: 67.44  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   6 DTANLDEIKEAHAlgvlAGVTTNPSLV-------------------AKEN--------ISFHDRLR-----EITEVVSGS 53
Cdd:PRK12346  16 DSGDIESIRHYHP----QDATTNPSLLlkaaglpqyqhliddaiawGKKQggtqeqqvVAACDKLAvnfgaEILKSVPGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  54 VSAEV---ISLKAEEMIEEGKELAKI-------APNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGA 123
Cdd:PRK12346  92 VSTEVdarLSFDREKSIEKARHLVDLyqqqgidKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEAGV 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521289019 124 TYVSPFLGRLDDI--GHNGLDL--------ISEIKQIFDV---HGLDTQIIAASIRHAQHVTEAA 175
Cdd:PRK12346 172 FLISPFVGRIYDWyqARKPMDPyvveedpgVKSVRNIYDYykqHRYETIVMGASFRRTEQILALA 236
PRK03343 PRK03343
transaldolase; Validated
 5-121 6.88e-13

transaldolase; Validated


Pssm-ID: 235117  Cd Length: 368  Bit Score: 66.38  E-value: 6.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   5 IDTANLDE-IKEAHalgvLAGVTTNPSLVAK----------------------ENISFH----------DRLREI---TE 48
Cdd:PRK03343  25 LTSGNLARlIDEKG----VVGVTSNPAIFQKaiaggdaydaqiaelaaagadvEEAYEElttadvrnacDVLRPVyeaTG 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521289019  49 VVSGSVSAEV---ISLKAEEMIEEGKELAKIA--PNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARA 121
Cdd:PRK03343 101 GVDGRVSIEVsprLAHDTEATIAEARRLWAAVdrPNLMIKIPATPEGLPAIEALIAEGISVNVTLIFSVERYRAVADA 178
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
 4-138 4.78e-12

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: 63.88  E-value: 4.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   4 FIDTANLDEIKEAHALgvlAGVTTNPSLVAK---ENISFHDRLR--------------------------------EITE 48
Cdd:cd00955   11 FIDNGFLKRLIEEQGV---VGVTSNPAIFEKaiaGSAAYDDQIRalkgqgldaeaiyealaiediqdacdllapvyEQTG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  49 VVSGSVSAEV---ISLKAEEMIEEGKELAKIA--PNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGA 123
Cdd:cd00955   88 GNDGYVSLEVsprLADDTQGTIAEAKRLWKAVgrPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYEAVAEAYL 167

                        170
                 ....*....|....*
gi 521289019 124 TYVSPFLGRLDDIGH 138
Cdd:cd00955  168 RGLERRVEGGGDLSQ 182
PRK03903 PRK03903
transaldolase; Provisional
 52-134 1.68e-11

transaldolase; Provisional


Pssm-ID: 235171  Cd Length: 274  Bit Score: 61.92  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019  52 GSVSAEV---ISLKAEEMIEEGKELAKI--APNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQA---LLAARAGA 123
Cdd:PRK03903  43 GFISIEIdpfLEDDAAGSIEEGKRLYKTigRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAkecAEALNEGL 122

                         90
                 ....*....|....*....
gi 521289019 124 --------TYVSPFLGRLD 134
Cdd:PRK03903 123 kkntkdpkAVISVFVSRFD 141
tal_mycobact TIGR00876
transaldolase, mycobacterial type; This model describes one of three related but easily ...
 4-124 8.83e-11

transaldolase, mycobacterial type; This model describes one of three related but easily separable famiiles of known and putative transaldolases. This family and the family typified by E. coli TalA and TalB both contain experimentally verified examples. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 129954  Cd Length: 350  Bit Score: 60.13  E-value: 8.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019    4 FIDTANLDEIKEAhalGVLAGVTTNPSLVAK--------------------------ENISFHDRLR---------EITE 48
Cdd:TIGR00876  14 FLENGDFLELIDK---GAICGATSNPSIFCEaisegafydaeiaelaakgadadaiiETLALDDILQacdalmplwEDSD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289019   49 VVSGSVSAEV---ISLKAEEMIEEGKELAKIA--PNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFSANQALLAARAGA 123
Cdd:TIGR00876  91 GNDGRISIEIdpfLADDAAKSIDEAIELFKILdrPNLFIKIPASEAGIEAISALLAAGIPVNVTLIFSPKIAGEIADALA 170


                  .
gi 521289019  124 T 124
Cdd:TIGR00876 171 K 171
PRK09533 PRK09533
bifunctional transaldolase/phosoglucose isomerase; Validated
 41-111 1.78e-08

bifunctional transaldolase/phosoglucose isomerase; Validated


Pssm-ID: 236551 [Multi-domain]  Cd Length: 948  Bit Score: 53.82  E-value: 1.78e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521289019  41 DRLR---EITEVVSGSVSAEV---ISLKAEEMIEEGKEL-AKIA-PNITVKIPMTSDGLKAVKALTDLGIKTNVTLIFS 111
Cdd:PRK09533  90 DVLRpvyDATDGADGFVSLEVspyLALDTEGTIAEARRLwAAVDrPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFS 168
 
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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