|
Name |
Accession |
Description |
Interval |
E-value |
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
1-213 |
6.91e-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: 6.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 1 MELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKT-RKSRENSIRDILKYSKGMVYVQTVSEKYEDIMSEVQSLLEFDNK 79
Cdd:COG0176 1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAgIKDFVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAALYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 80 RIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNNIET 159
Cdd:COG0176 81 NVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGART 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2570555655 160 KILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDWDEL 213
Cdd:COG0176 161 RILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
2-210 |
3.82e-79 |
|
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: 235.93 E-value: 3.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 2 ELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKT-RKSRENSIRDILKYSKGMVYVQTVSEKYEDIMSEVQSLLEFDNkR 80
Cdd:cd00956 1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSgRIDFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEARKLASLGG-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 81 IGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNNIETK 160
Cdd:cd00956 80 VVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDTK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570555655 161 ILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDW 210
Cdd:cd00956 160 ILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDW 209
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
1-212 |
6.24e-61 |
|
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: 189.69 E-value: 6.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 1 MELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRKSRENSIRDILKYSKGMVYVQTVSEKYEDIMSEVQSLLEF-DNk 79
Cdd:TIGR00875 1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKLaPN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 80 rIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNNIET 159
Cdd:TIGR00875 80 -IVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2570555655 160 KILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDWDE 212
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNA 211
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
3-217 |
2.19e-56 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 178.50 E-value: 2.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 3 LYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRKSREN---SIRDILKYSKGMVYVQTV---SEKYEDIMSEVQSLL-E 75
Cdd:pfam00923 1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKAIEYSALydeAIAEIKEIGDGPVSLEVDprlADDTEGTIEEARRLIaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 76 FDNKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRM----------EQNEIDAINII 145
Cdd:pfam00923 81 YGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIddwgdkrlgaALRGDDGIANA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570555655 146 KEIRNIYEMNNIETKILAASFRNMEQImrVIKAGAHAVTISYELFCEMFNNylteKSINKFKEDWDELNDKL 217
Cdd:pfam00923 161 KEIYQIYKKYGWSTGVLAASFRNVLYV--LALAGCDTITIPPDTLEALAKD----EGVRKFAKDWEKLLGSI 226
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
1-213 |
1.80e-54 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 173.77 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 1 MELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRK----SRENSIRDILKySKGMVYVQTVSEKYEDIMSEVQSLLEF 76
Cdd:PRK12656 1 MEFMLDTLNLEAIKKWHEILPLAGVTSNPSIAKKEGDidffERIREVREIIG-DEASIHVQVVAQDYEGILKDAHEIRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 77 DNKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNN 156
Cdd:PRK12656 80 CGDDVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENLNIDSNAVIGQLAEAIDREN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570555655 157 IETKILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDWDEL 213
Cdd:PRK12656 160 SDSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFADDWEAI 216
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
1-213 |
6.91e-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: 6.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 1 MELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKT-RKSRENSIRDILKYSKGMVYVQTVSEKYEDIMSEVQSLLEFDNK 79
Cdd:COG0176 1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAgIKDFVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAALYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 80 RIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNNIET 159
Cdd:COG0176 81 NVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGART 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2570555655 160 KILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDWDEL 213
Cdd:COG0176 161 RILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
2-210 |
3.82e-79 |
|
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: 235.93 E-value: 3.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 2 ELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKT-RKSRENSIRDILKYSKGMVYVQTVSEKYEDIMSEVQSLLEFDNkR 80
Cdd:cd00956 1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSgRIDFEAVLKEICEIIDGPVSAQVVSTDAEGMVAEARKLASLGG-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 81 IGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNNIETK 160
Cdd:cd00956 80 VVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDTK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2570555655 161 ILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDW 210
Cdd:cd00956 160 ILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDW 209
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
1-212 |
6.24e-61 |
|
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: 189.69 E-value: 6.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 1 MELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRKSRENSIRDILKYSKGMVYVQTVSEKYEDIMSEVQSLLEF-DNk 79
Cdd:TIGR00875 1 MKFFLDTANVEEIKKAAELGILAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKLaPN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 80 rIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNNIET 159
Cdd:TIGR00875 80 -IVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2570555655 160 KILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDWDE 212
Cdd:TIGR00875 159 EVIAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNA 211
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
3-217 |
2.19e-56 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 178.50 E-value: 2.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 3 LYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRKSREN---SIRDILKYSKGMVYVQTV---SEKYEDIMSEVQSLL-E 75
Cdd:pfam00923 1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKAIEYSALydeAIAEIKEIGDGPVSLEVDprlADDTEGTIEEARRLIaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 76 FDNKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRM----------EQNEIDAINII 145
Cdd:pfam00923 81 YGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRIddwgdkrlgaALRGDDGIANA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2570555655 146 KEIRNIYEMNNIETKILAASFRNMEQImrVIKAGAHAVTISYELFCEMFNNylteKSINKFKEDWDELNDKL 217
Cdd:pfam00923 161 KEIYQIYKKYGWSTGVLAASFRNVLYV--LALAGCDTITIPPDTLEALAKD----EGVRKFAKDWEKLLGSI 226
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
1-213 |
1.80e-54 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 173.77 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 1 MELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRK----SRENSIRDILKySKGMVYVQTVSEKYEDIMSEVQSLLEF 76
Cdd:PRK12656 1 MEFMLDTLNLEAIKKWHEILPLAGVTSNPSIAKKEGDidffERIREVREIIG-DEASIHVQVVAQDYEGILKDAHEIRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 77 DNKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNN 156
Cdd:PRK12656 80 CGDDVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRMENLNIDSNAVIGQLAEAIDREN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2570555655 157 IETKILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDWDEL 213
Cdd:PRK12656 160 SDSKILAASFKNVAQVNKAFALGAQAVTAGPDVFEAAFAMPSIQKAVDDFADDWEAI 216
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
1-210 |
3.25e-51 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 165.34 E-value: 3.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 1 MELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRKSREN---SIRDILKySKGMVYVQTVSEKYEDIMSEVQSLLEFD 77
Cdd:PRK12653 1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVvlpQLHEAMG-GQGRLFAQVMATTAEGMVNDARKLRSII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 78 NKrIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRMEQNEIDAINIIKEIRNIYEMNNI 157
Cdd:PRK12653 80 AD-IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2570555655 158 ETKILAASFRNMEQIMRVIKAGAHAVTISYELFCEMFNNYLTEKSINKFKEDW 210
Cdd:PRK12653 159 QAKVLAASFKTPRQALDCLLAGCESITLPLDVAQQMISYPAVDAAVAKFEQDW 211
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
2-210 |
1.13e-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: 100.12 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 2 ELYLDTADIDEIKSAFNIGIVKGVTTNPTILLKTRK--SRENSIRDILKYSKGMVYVQTVSEKYEDIM------------ 67
Cdd:cd00439 1 SPWYDTLDRPATDLLPLIRGVRGVTTNPSIIQAAIStsNAYNDQFRTLVESGKDIESAYWELVVKDIQdacklfepiydq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 68 --------SEVQSLLEFD----------------NKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAG 123
Cdd:cd00439 81 teadgrvsVEVSARLADDtqgmveaakylskvvnRRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 124 ADYIAPYINRM-------------EQNEIDAINIIKEIRNIYEMNNIETKILAASFRNMEQIMRVIkaGAHAVTISYELF 190
Cdd:cd00439 161 TSVASPFVSRIdtlmdkmleqiglDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLI--GCDTVTTMPDQA 238
|
250 260
....*....|....*....|
gi 2570555655 191 CEMfnnyltekSINKFKEDW 210
Cdd:cd00439 239 LEA--------GVDKFKKDF 250
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
6-196 |
4.31e-18 |
|
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: 80.74 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 6 DTADIDEIKsAFNIgivKGVTTNPTILLKTRKSRE--------------------------------NSIRDILKYSKGM 53
Cdd:cd00957 15 DTGDFEAIK-KFKP---QDATTNPSLILAAAKLPEynklvdeaiayakkkggsdedqisnaldkllvNFGTEILKLIPGR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 54 VYVQT---VSEKYEDIMSEVQSLLEF------DNKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGA 124
Cdd:cd00957 91 VSTEVdarLSFDTNATIAKARKLIKLyeeagiDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAVACAEAGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 125 DYIAPYINRM-------------EQNEIDAINIIKEIRNIYEMNNIETKILAASFRNMEQIMRVikAGAHAVTISYELFC 191
Cdd:cd00957 171 TLISPFVGRIldwykkhsgdkayTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILAL--AGCDYLTISPALLE 248
|
....*
gi 2570555655 192 EMFNN 196
Cdd:cd00957 249 ELKNS 253
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
6-193 |
2.84e-14 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 70.13 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 6 DTADIDEIKSaFNigiVKGVTTNPTILLK--TRKSRENSIRDILKYSK---------------------GMVYVQTVSEK 62
Cdd:PRK12346 16 DSGDIESIRH-YH---PQDATTNPSLLLKaaGLPQYQHLIDDAIAWGKkqggtqeqqvvaacdklavnfGAEILKSVPGR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 63 yedIMSEVQSLLEFDN---------------------KRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSAL 121
Cdd:PRK12346 92 ---VSTEVDARLSFDReksiekarhlvdlyqqqgidkSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 122 AGADYIAPYINR----------MEQNEIDAINIIKEIRNIYE---MNNIETKILAASFRNMEQIMRVikAGAHAVTISYE 188
Cdd:PRK12346 169 AGVFLISPFVGRiydwyqarkpMDPYVVEEDPGVKSVRNIYDyykQHRYETIVMGASFRRTEQILAL--AGCDRLTISPN 246
|
....*
gi 2570555655 189 LFCEM 193
Cdd:PRK12346 247 LLKEL 251
|
|
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
6-189 |
4.25e-12 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 64.03 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 6 DTADIDEIKS-----AfnigivkgvTTNPTILLKTRKSRENS--IRDILKYSK--GMVYVQTVSEKYED----------- 65
Cdd:PRK05269 17 DTGDIEAIKKyqpqdA---------TTNPSLILKAAQIPEYAplIDDAVAWAKqqSGDRAQQIDDAIDKlavnfgleilk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 66 -----IMSEVQSLLEFD---------------------NKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVS 119
Cdd:PRK05269 88 lipgrVSTEVDARLSFDteatiakarklialyeeagisKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFSFAQARAC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 120 ALAGADYIAPYINR-----MEQNEIDAINI--------IKEIRNIYEMNNIETKILAASFRNMEQIMRVikAGAHAVTIS 186
Cdd:PRK05269 168 AEAGVFLISPFVGRildwyKKNTGKKEYAPaedpgvvsVTKIYNYYKKHGYKTVVMGASFRNTGQILEL--AGCDRLTIS 245
|
...
gi 2570555655 187 YEL 189
Cdd:PRK05269 246 PAL 248
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
77-217 |
1.55e-10 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 59.75 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 77 DNKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRM----EQNEIDA---------IN 143
Cdd:PTZ00411 135 SKDRILIKLASTWEGIQAAKALEKEGIHCNLTLLFSFAQAVACAQAGVTLISPFVGRIldwyKKPEKAEsyvgaqdpgVI 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2570555655 144 IIKEIRNIYEMNNIETKILAASFRNMEQIMRVikAGAHAVTISYELFCEMFNNYLTEKSINKFKEDWDELNDKL 217
Cdd:PTZ00411 215 SVTKIYNYYKKHGYKTIVMGASFRNTGEILEL--AGCDKLTISPKLLEELANTEDGPVERKLDPEKLTEDTEKL 286
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
77-193 |
3.53e-10 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 58.59 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2570555655 77 DNKRIGIKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQAVVSALAGADYIAPYINRM-------------EQNEIDAIN 143
Cdd:PRK12309 129 SRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTLLFGFHQAIACAEAGVTLISPFVGRIldwykketgrdsyPGAEDPGVQ 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2570555655 144 IIKEIRNIYEMNNIETKILAASFRNMEQIMRVikAGAHAVTISYELFCEM 193
Cdd:PRK12309 209 SVTQIYNYYKKFGYKTEVMGASFRNIGEIIEL--AGCDLLTISPKLLEQL 256
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
83-116 |
5.19e-03 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 36.88 E-value: 5.19e-03
10 20 30
....*....|....*....|....*....|....
gi 2570555655 83 IKIPVTPDGIKAIKELSDKSIKTIATAVFTTSQA 116
Cdd:PRK03903 78 IKVPATKAGYEAMSALMKKGISVNATLIFSPEQA 111
|
|
| |
