|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
1-220 |
2.57e-145 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 403.78 E-value: 2.57e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 1 MELYLDTSDVAAVKKLARIFPLAGVTTNPSIVAAGKTPLDELLPALHDALGGKGRLFAQVMATTAEGMVEDARKLRAIIN 80
Cdd:PRK12653 1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 81 DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAPQS 160
Cdd:PRK12653 81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQGAFGRTSI 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 |
5.08e-93 |
|
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: 271.35 E-value: 5.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 1 MELYLDTSDVAAVKKLARIFPLAGVTTNPSIVAAGKTPLDELLPALHDALggKGRLFAQVMATTAEGMVEDARKLRAIIN 80
Cdd:TIGR00875 1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAV--EGPVSAETISLDAEGMVEEAKELAKLAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 81 DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAPQS 160
Cdd:TIGR00875 79 NIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317696659 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQGAF 215
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAAF 213
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
2-213 |
9.58e-91 |
|
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: 265.21 E-value: 9.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 2 ELYLDTSDVAAVKKLARIFPLAGVTTNPSIVA-AGKTPLDELLPALHDAlgGKGRLFAQVMATTAEGMVEDARKLRAIIN 80
Cdd:cd00956 1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAkSGRIDFEAVLKEICEI--IDGPVSAQVVSTDAEGMVAEARKLASLGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 81 DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAPQS 160
Cdd:cd00956 79 NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317696659 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQG 213
Cdd:cd00956 159 KILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
1-214 |
8.38e-83 |
|
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: 245.37 E-value: 8.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 1 MELYLDTSDVAAVKKLARIFPLAGVTTNPSIVA-AGKTPLDELLPALHDALggKGRLFAQVMATTAEGMVEDARKLRAII 79
Cdd:COG0176 1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAkAGIKDFVEDIREICDIV--DGPVSAEVLATDTEGMIAEARRLAALY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 80 ND-LVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAP 158
Cdd:COG0176 79 RPnVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317696659 159 QSKVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQGA 214
Cdd:COG0176 159 RTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
3-216 |
3.14e-64 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 198.53 E-value: 3.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 3 LYLDTSDVAAVKKLARIFPLAGVTTNPSIVA---AGKTPLDELLPALHDAlgGKGRLFAQVMA---TTAEGMVEDARKLR 76
Cdd:pfam00923 1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLkaiEYSALYDEAIAEIKEI--GDGPVSLEVDPrlaDDTEGTIEEARRLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 77 AIIN--DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGG----------DGIQ 144
Cdd:pfam00923 79 ALYGrpNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGDkrlgaalrgdDGIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317696659 145 TVIELQQLLALHAPQSKVLAASFKTPRQALDclLAGCESITLPLDVAQQFITspavDAAIVKFEQDWQGAFG 216
Cdd:pfam00923 159 NAKEIYQIYKKYGWSTGVLAASFRNVLYVLA--LAGCDTITIPPDTLEALAK----DEGVRKFAKDWEKLLG 224
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
1-220 |
2.57e-145 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 403.78 E-value: 2.57e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 1 MELYLDTSDVAAVKKLARIFPLAGVTTNPSIVAAGKTPLDELLPALHDALGGKGRLFAQVMATTAEGMVEDARKLRAIIN 80
Cdd:PRK12653 1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQLHEAMGGQGRLFAQVMATTAEGMVNDARKLRSIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 81 DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAPQS 160
Cdd:PRK12653 81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQGAFGRTSI 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 |
5.08e-93 |
|
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: 271.35 E-value: 5.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 1 MELYLDTSDVAAVKKLARIFPLAGVTTNPSIVAAGKTPLDELLPALHDALggKGRLFAQVMATTAEGMVEDARKLRAIIN 80
Cdd:TIGR00875 1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAV--EGPVSAETISLDAEGMVEEAKELAKLAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 81 DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAPQS 160
Cdd:TIGR00875 79 NIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1317696659 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQGAF 215
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAAF 213
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
2-213 |
9.58e-91 |
|
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: 265.21 E-value: 9.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 2 ELYLDTSDVAAVKKLARIFPLAGVTTNPSIVA-AGKTPLDELLPALHDAlgGKGRLFAQVMATTAEGMVEDARKLRAIIN 80
Cdd:cd00956 1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAkSGRIDFEAVLKEICEI--IDGPVSAQVVSTDAEGMVAEARKLASLGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 81 DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAPQS 160
Cdd:cd00956 79 NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1317696659 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQG 213
Cdd:cd00956 159 KILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
1-214 |
8.38e-83 |
|
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: 245.37 E-value: 8.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 1 MELYLDTSDVAAVKKLARIFPLAGVTTNPSIVA-AGKTPLDELLPALHDALggKGRLFAQVMATTAEGMVEDARKLRAII 79
Cdd:COG0176 1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAkAGIKDFVEDIREICDIV--DGPVSAEVLATDTEGMIAEARRLAALY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 80 ND-LVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAP 158
Cdd:COG0176 79 RPnVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317696659 159 QSKVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQGA 214
Cdd:COG0176 159 RTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
2-213 |
1.80e-72 |
|
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: 220.69 E-value: 1.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 2 ELYLDTSDVAAVKKLARIFPLAGVTTNPSIVAAGKT--------------------------------PLDELLPALHDA 49
Cdd:cd00439 1 SPWYDTLDRPATDLLPLIRGVRGVTTNPSIIQAAIStsnayndqfrtlvesgkdiesaywelvvkdiqDACKLFEPIYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 50 LGGKGRLFAQVMA---TTAEGMVEDARKLRAIIN--DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAG 124
Cdd:cd00439 81 TEADGRVSVEVSArlaDDTQGMVEAAKYLSKVVNrrNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 125 AEYVAPYVNRVDAQGGD-------------GIQTVIELQQLLALHAPQSKVLAASFKTPRQALDCLlaGCESITLPLDVA 191
Cdd:cd00439 161 TSVASPFVSRIDTLMDKmleqigldlrgkaGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLI--GCDTVTTMPDQA 238
|
250 260
....*....|....*....|..
gi 1317696659 192 QQfitspavdAAIVKFEQDWQG 213
Cdd:cd00439 239 LE--------AGVDKFKKDFES 252
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
3-216 |
3.14e-64 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 198.53 E-value: 3.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 3 LYLDTSDVAAVKKLARIFPLAGVTTNPSIVA---AGKTPLDELLPALHDAlgGKGRLFAQVMA---TTAEGMVEDARKLR 76
Cdd:pfam00923 1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLkaiEYSALYDEAIAEIKEI--GDGPVSLEVDPrlaDDTEGTIEEARRLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 77 AIIN--DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGG----------DGIQ 144
Cdd:pfam00923 79 ALYGrpNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIDDWGDkrlgaalrgdDGIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317696659 145 TVIELQQLLALHAPQSKVLAASFKTPRQALDclLAGCESITLPLDVAQQFITspavDAAIVKFEQDWQGAFG 216
Cdd:pfam00923 159 NAKEIYQIYKKYGWSTGVLAASFRNVLYVLA--LAGCDTITIPPDTLEALAK----DEGVRKFAKDWEKLLG 224
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
1-220 |
1.44e-56 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 178.78 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 1 MELYLDTSDVAAVKKLARIFPLAGVTTNPSIVA-AGKTPLDELLPALHDALGGKGRLFAQVMATTAEGMVEDARKLRAII 79
Cdd:PRK12656 1 MEFMLDTLNLEAIKKWHEILPLAGVTSNPSIAKkEGDIDFFERIREVREIIGDEASIHVQVVAQDYEGILKDAHEIRRQC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 80 NDLV-VKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQGGDGIQTVIELQQLLALHAP 158
Cdd:PRK12656 81 GDDVyIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENLNIDSNAVIGQLAEAIDRENS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317696659 159 QSKVLAASFKTPRQALDCLLAGCESITLPLDVAQQFITSPAVDAAIVKFEQDWQGAFGRTSI 220
Cdd:PRK12656 161 DSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFADDWEAIHGRKSI 222
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
6-193 |
1.97e-12 |
|
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: 64.95 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 6 DTSDVAAVKKlariFPLAGVTTNPS-IVAAGKTP-----LDEllpALHDALGGKG-----------RLFAQV---MATTA 65
Cdd:cd00957 15 DTGDFEAIKK----FKPQDATTNPSlILAAAKLPeynklVDE---AIAYAKKKGGsdedqisnaldKLLVNFgteILKLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 66 EGMVE---DAR----------KLRAII----------NDLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSAL 122
Cdd:cd00957 88 PGRVStevDARlsfdtnatiaKARKLIklyeeagidkERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAVACAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 123 AGAEYVAPYVNRV-D---AQGGD---------GIQTVIELQQLLALHAPQSKVLAASFKTPRQALDclLAGCESITLPLD 189
Cdd:cd00957 168 AGVTLISPFVGRIlDwykKHSGDkaytaeedpGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILA--LAGCDYLTISPA 245
|
....
gi 1317696659 190 VAQQ 193
Cdd:cd00957 246 LLEE 249
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
65-187 |
2.85e-09 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 55.90 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 65 AEGMVEDARKLRAIIND-------LVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSALAGAEYVAPYVNRV-- 135
Cdd:PTZ00411 115 KQAMVDKARKIIKMYEEagiskdrILIKLASTWEGIQAAKALEKEGIHCNLTLLFSFAQAVACAQAGVTLISPFVGRIld 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317696659 136 ---DAQGGD--------GIQTVIELQQLLALHAPQSKVLAASFKTPRQALDclLAGCESITLP 187
Cdd:PTZ00411 195 wykKPEKAEsyvgaqdpGVISVTKIYNYYKKHGYKTIVMGASFRNTGEILE--LAGCDKLTIS 255
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
6-186 |
1.18e-08 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 54.35 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 6 DTSDVAAVKKlariFPLAGVTTNPS-IVAAGKTP-----LDELLPALHDALG--------------------GK------ 53
Cdd:PRK12309 18 DTGDIQAIEK----FTPRDATTNPSlITAAAQMPqyqsiVDETLRQARKELGsdapvedvvalafdrlavafGLkilkiv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 54 -GRLFAQVMATTA---EGMVEDARKLRAIIND-------LVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSAL 122
Cdd:PRK12309 94 pGRVSTEVDARLSydtEATIAKARKLISLYEDagisrdrVLIKIASTWEGIKAAEVLEKEGIHCNLTLLFGFHQAIACAE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317696659 123 AGAEYVAPYVNRV----------DAQGG---DGIQTVIELQQLLALHAPQSKVLAASFKTPRQAldCLLAGCESITL 186
Cdd:PRK12309 174 AGVTLISPFVGRIldwykketgrDSYPGaedPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEI--IELAGCDLLTI 248
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
14-105 |
2.19e-06 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 47.51 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 14 KKLARIFPLAGVTTNPSI------------------VAAGKTPLD--------------ELLPALHDALGGK-GRLFAQV 60
Cdd:PRK03343 31 ARLIDEKGVVGVTSNPAIfqkaiaggdaydaqiaelAAAGADVEEayeelttadvrnacDVLRPVYEATGGVdGRVSIEV 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1317696659 61 ---MATTAEGMVEDARKLRAIIN--DLVVKVPVTAEGLAAIKMLKAEGIP 105
Cdd:PRK03343 111 sprLAHDTEATIAEARRLWAAVDrpNLMIKIPATPEGLPAIEALIAEGIS 160
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
6-186 |
2.70e-06 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 47.02 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 6 DTSDVAAVKKlariFPLAGVTTNPSIV--AAGktpLDELLPALHDAL-------GGK----------------------- 53
Cdd:PRK12346 16 DSGDIESIRH----YHPQDATTNPSLLlkAAG---LPQYQHLIDDAIawgkkqgGTQeqqvvaacdklavnfgaeilksv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 54 -GRLFAQVMATTA---EGMVEDARKLRAIIND-------LVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSAL 122
Cdd:PRK12346 89 pGRVSTEVDARLSfdrEKSIEKARHLVDLYQQqgidksrILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317696659 123 AGAEYVAPYVNRV-------------DAQGGDGIQTVIELQQLLALHAPQSKVLAASFKTPRQALDclLAGCESITL 186
Cdd:PRK12346 169 AGVFLISPFVGRIydwyqarkpmdpyVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILA--LAGCDRLTI 243
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
24-116 |
7.03e-06 |
|
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: 45.78 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 24 GVTTNPSI------------------VAAGKTPLD--------------ELLPALHDALGGK-GRLFAQV---MATTAEG 67
Cdd:cd00955 28 GVTSNPAIfekaiagsaayddqiralKGQGLDAEAiyealaiediqdacDLLAPVYEQTGGNdGYVSLEVsprLADDTQG 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1317696659 68 MVEDARKLRAIIN--DLVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQ 116
Cdd:cd00955 108 TIAEAKRLWKAVGrpNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQ 158
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
61-104 |
1.18e-04 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 42.65 E-value: 1.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1317696659 61 MATTAEGMVEDARKLRAIIN--DLVVKVPVTAEGLAAIKMLKAEGI 104
Cdd:PRK09533 114 LALDTEGTIAEARRLWAAVDrpNLMIKVPATPEGLPAIRQLIAEGI 159
|
|
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
6-185 |
6.77e-04 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 39.76 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 6 DTSDVAAVKKLArifPLaGVTTNPS-IVAAGKTP-----LDEllpALHDALGGKGRLFAQVMATT--------------- 64
Cdd:PRK05269 17 DTGDIEAIKKYQ---PQ-DATTNPSlILKAAQIPeyaplIDD---AVAWAKQQSGDRAQQIDDAIdklavnfgleilkli 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 65 ---------------AEGMVEDARKLRA------IINDLV-VKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGMLSAL 122
Cdd:PRK05269 90 pgrvstevdarlsfdTEATIAKARKLIAlyeeagISKDRIlIKIASTWEGIRAAEQLEKEGINCNLTLLFSFAQARACAE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317696659 123 AGAEYVAPYVNRV-D----AQGGD--------GIQTVIELQQLLALHAPQSKVLAASFKTPRQALDclLAGCESIT 185
Cdd:PRK05269 170 AGVFLISPFVGRIlDwykkNTGKKeyapaedpGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILE--LAGCDRLT 243
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
4-184 |
8.03e-04 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 39.23 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 4 YLDTSDVAAVKKLARIFPLAGVTTNPSIVaagktpldellPALHDALGG-KGRLFAQVMATTAEGM-------VEDARKL 75
Cdd:cd00945 9 DATLEDIAKLCDEAIEYGFAAVCVNPGYV-----------RLAADALAGsDVPVIVVVGFPTGLTTtevkvaeVEEAIDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317696659 76 RAIINDLVVKVPVTAEG-----LAAIKMLKAE---GIPT--------LGTAVYGAAQGMLSALAGAEYVAPYVNRVDAQG 139
Cdd:cd00945 78 GADEIDVVINIGSLKEGdweevLEEIAAVVEAadgGLPLkviletrgLKTADEIAKAARIAAEAGADFIKTSTGFGGGGA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1317696659 140 gdgiqTVIELQQLLALHAPQSKVLAASF-KTPRQALDCLLAGCESI 184
Cdd:cd00945 158 -----TVEDVKLMKEAVGGRVGVKAAGGiKTLEDALAAIEAGADGI 198
|
|
| |
