|
Name |
Accession |
Description |
Interval |
E-value |
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
1-211 |
1.86e-63 |
|
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: 195.68 E-value: 1.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 1 MKYLIDSANLDEIQKCLKYG-FKGITANPSMYLKEKV-NFHEFIETCANLNPEILTAEVIGNNLYELINSCDKILNIN-K 77
Cdd:COG0176 1 MKLWLDTADREEIKELIDLGgVDGVTTNPSLIAKAGIkDFVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAALYrP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 78 NTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDENGNDGIKNLTEICNLISINGYNT 157
Cdd:COG0176 81 NVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGART 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489535279 158 KVVAASIKNVFHLTQASLCGCDYAAVTYDLFKKASFNQLTIDGANTFERDWSKV 211
Cdd:COG0176 161 RILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
2-210 |
5.79e-57 |
|
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: 179.31 E-value: 5.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 2 KYLIDSANLDEIQKCLKYGF-KGITANPSMYLKE-KVNFHEFI-ETCANLNPEIlTAEVIGNNLYELINSCDKILNINKN 78
Cdd:cd00956 1 KIFLDTADLEEIKKASETGLlDGVTTNPSLIAKSgRIDFEAVLkEICEIIDGPV-SAQVVSTDAEGMVAEARKLASLGGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 79 TIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDENGNDGIKNLTEICNLISINGYNTK 158
Cdd:cd00956 80 VVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDTK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489535279 159 VVAASIKNVFHLTQASLCGCDYAAVTYDLFKKASFNQLTIDGANTFERDWSK 210
Cdd:cd00956 160 ILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
1-211 |
4.71e-47 |
|
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: 154.25 E-value: 4.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 1 MKYLIDSANLDEIQKCLKYG-FKGITANPSMYLKEKVNFHEFIETCANLNPEILTAEVIGNNLYELINSCDKILNINKNT 79
Cdd:TIGR00875 1 MKFFLDTANVEEIKKAAELGiLAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKLAPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 80 IIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDENGNDGIKNLTEICNLISINGYNTKV 159
Cdd:TIGR00875 81 VVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDTEV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489535279 160 VAASIKNVFHLTQASLCGCDYAAVTYDLFKKASFNQLTIDGANTFERDWSKV 211
Cdd:TIGR00875 161 IAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAA 212
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
5-210 |
1.89e-36 |
|
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: 127.27 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 5 IDSANLDEIQKCLK-YGFKGITANPSMYLKE---KVNFHEFIETCANLNPEILTAEVIGNNLY----------ELINSCD 70
Cdd:pfam00923 3 LDTADRDLIKKLIEeGGIDGVTTNPSIFLKAieySALYDEAIAEIKEIGDGPVSLEVDPRLADdtegtieearRLIALYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 71 KilninKNTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGR----------NDENGNDGI 140
Cdd:pfam00923 83 R-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRiddwgdkrlgAALRGDDGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 141 KNLTEICNLISINGYNTKVVAASIKNVFHLTqaSLCGCDYAAVTYDLFKKasFNQLtiDGANTFERDWSK 210
Cdd:pfam00923 158 ANAKEIYQIYKKYGWSTGVLAASFRNVLYVL--ALAGCDTITIPPDTLEA--LAKD--EGVRKFAKDWEK 221
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
1-211 |
8.63e-28 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 104.82 E-value: 8.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 1 MKYLIDSANLDEIQK-CLKYGFKGITANPSMYLKE-KVNFHEFIETCANL---NPEIlTAEVIGNNLYELINSCDKIL-N 74
Cdd:PRK12656 1 MEFMLDTLNLEAIKKwHEILPLAGVTSNPSIAKKEgDIDFFERIREVREIigdEASI-HVQVVAQDYEGILKDAHEIRrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 75 INKNTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNdENGN-DGIKNLTEICNLISIN 153
Cdd:PRK12656 80 CGDDVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRM-ENLNiDSNAVIGQLAEAIDRE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489535279 154 GYNTKVVAASIKNVFHLTQASLCGCDYAAVTYDLFkKASFNQLTIDGA-NTFERDWSKV 211
Cdd:PRK12656 159 NSDSKILAASFKNVAQVNKAFALGAQAVTAGPDVF-EAAFAMPSIQKAvDDFADDWEAI 216
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
1-211 |
1.86e-63 |
|
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: 195.68 E-value: 1.86e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 1 MKYLIDSANLDEIQKCLKYG-FKGITANPSMYLKEKV-NFHEFIETCANLNPEILTAEVIGNNLYELINSCDKILNIN-K 77
Cdd:COG0176 1 MKLWLDTADREEIKELIDLGgVDGVTTNPSLIAKAGIkDFVEDIREICDIVDGPVSAEVLATDTEGMIAEARRLAALYrP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 78 NTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDENGNDGIKNLTEICNLISINGYNT 157
Cdd:COG0176 81 NVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGASYVSPFVGRIDDIGIDGIALVREIYQIYKNYGART 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489535279 158 KVVAASIKNVFHLTQASLCGCDYAAVTYDLFKKASFNQLTIDGANTFERDWSKV 211
Cdd:COG0176 161 RILAASFRNPLQVLEAALAGADTVTIPPAVLEALADHPLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
2-210 |
5.79e-57 |
|
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: 179.31 E-value: 5.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 2 KYLIDSANLDEIQKCLKYGF-KGITANPSMYLKE-KVNFHEFI-ETCANLNPEIlTAEVIGNNLYELINSCDKILNINKN 78
Cdd:cd00956 1 KIFLDTADLEEIKKASETGLlDGVTTNPSLIAKSgRIDFEAVLkEICEIIDGPV-SAQVVSTDAEGMVAEARKLASLGGN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 79 TIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDENGNDGIKNLTEICNLISINGYNTK 158
Cdd:cd00956 80 VVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIFDNYGFDTK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489535279 159 VVAASIKNVFHLTQASLCGCDYAAVTYDLFKKASFNQLTIDGANTFERDWSK 210
Cdd:cd00956 160 ILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKHPLTDKGVEKFLEDWQS 211
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
1-211 |
4.71e-47 |
|
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: 154.25 E-value: 4.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 1 MKYLIDSANLDEIQKCLKYG-FKGITANPSMYLKEKVNFHEFIETCANLNPEILTAEVIGNNLYELINSCDKILNINKNT 79
Cdd:TIGR00875 1 MKFFLDTANVEEIKKAAELGiLAGVTTNPSLIAKEGRSFWEVLKEIQEAVEGPVSAETISLDAEGMVEEAKELAKLAPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 80 IIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDENGNDGIKNLTEICNLISINGYNTKV 159
Cdd:TIGR00875 81 VVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVGRLDDIGGDGMKLIEEVKTIFENHAPDTEV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489535279 160 VAASIKNVFHLTQASLCGCDYAAVTYDLFKKASFNQLTIDGANTFERDWSKV 211
Cdd:TIGR00875 161 IAASVRHPRHVLEAALIGADIATMPLDVMQQLFNHPLTDIGLERFLKDWNAA 212
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
5-210 |
1.89e-36 |
|
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: 127.27 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 5 IDSANLDEIQKCLK-YGFKGITANPSMYLKE---KVNFHEFIETCANLNPEILTAEVIGNNLY----------ELINSCD 70
Cdd:pfam00923 3 LDTADRDLIKKLIEeGGIDGVTTNPSIFLKAieySALYDEAIAEIKEIGDGPVSLEVDPRLADdtegtieearRLIALYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 71 KilninKNTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGR----------NDENGNDGI 140
Cdd:pfam00923 83 R-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASVISPFVGRiddwgdkrlgAALRGDDGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 141 KNLTEICNLISINGYNTKVVAASIKNVFHLTqaSLCGCDYAAVTYDLFKKasFNQLtiDGANTFERDWSK 210
Cdd:pfam00923 158 ANAKEIYQIYKKYGWSTGVLAASFRNVLYVL--ALAGCDTITIPPDTLEA--LAKD--EGVRKFAKDWEK 221
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
1-211 |
8.63e-28 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 104.82 E-value: 8.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 1 MKYLIDSANLDEIQK-CLKYGFKGITANPSMYLKE-KVNFHEFIETCANL---NPEIlTAEVIGNNLYELINSCDKIL-N 74
Cdd:PRK12656 1 MEFMLDTLNLEAIKKwHEILPLAGVTSNPSIAKKEgDIDFFERIREVREIigdEASI-HVQVVAQDYEGILKDAHEIRrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 75 INKNTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNdENGN-DGIKNLTEICNLISIN 153
Cdd:PRK12656 80 CGDDVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRM-ENLNiDSNAVIGQLAEAIDRE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489535279 154 GYNTKVVAASIKNVFHLTQASLCGCDYAAVTYDLFkKASFNQLTIDGA-NTFERDWSKV 211
Cdd:PRK12656 159 NSDSKILAASFKNVAQVNKAFALGAQAVTAGPDVF-EAAFAMPSIQKAvDDFADDWEAI 216
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
1-208 |
5.21e-23 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 92.15 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 1 MKYLIDSANLDEIQKCLK-YGFKGITANPSMYLKEKVNFHEFI-ETCANLNPE-ILTAEVIGNNLYELINSCDKILNINK 77
Cdd:PRK12653 1 MELYLDTSDVVAVKALSRiFPLAGVTTNPSIIAAGKKPLEVVLpQLHEAMGGQgRLFAQVMATTAEGMVNDARKLRSIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 78 NTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDENGNDGIKNLTEICNLISINGYNT 157
Cdd:PRK12653 81 DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVNRIDAQGGSGIQTVTDLQQLLKMHAPQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489535279 158 KVVAASIKNVFHLTQASLCGCDYAAVTYDLFKKAsFNQLTIDGANT-FERDW 208
Cdd:PRK12653 161 KVLAASFKTPRQALDCLLAGCESITLPLDVAQQM-ISYPAVDAAVAkFEQDW 211
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
77-210 |
8.19e-13 |
|
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: 65.45 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 77 KNTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGRNDE-------------NGNDGIKNL 143
Cdd:cd00439 116 RNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADAGTSVASPFVSRIDTlmdkmleqigldlRGKAGVAQV 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489535279 144 TEICNLISINGYNTKVVAASIKNVFHLtqASLCGCDYAAVTYDLFKKAsfnqltidGANTFERDWSK 210
Cdd:cd00439 196 TLAYKLYKQKFKKQRVLWASFSDTLYV--APLIGCDTVTTMPDQALEA--------GVDKFKKDFES 252
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
63-190 |
5.40e-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: 63.41 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 63 YELINSCDKIlNINKNTI-IKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGR---------- 131
Cdd:cd00957 111 RKLIKLYEEA-GIDKERIlIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAVACAEAGVTLISPFVGRildwykkhsg 189
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489535279 132 --NDENGND-GIKNLTEICNLISINGYNTKVVAASIKNVFHLTqaSLCGCDYAAVTYDLFKK 190
Cdd:cd00957 190 dkAYTAEEDpGVASVKKIYNYYKKFGYKTKVMGASFRNIGQIL--ALAGCDYLTISPALLEE 249
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
75-179 |
3.46e-09 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 55.51 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 75 INKNTI-IKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGR------NDENGND-------GI 140
Cdd:PTZ00411 134 ISKDRIlIKLASTWEGIQAAKALEKEGIHCNLTLLFSFAQAVACAQAGVTLISPFVGRildwykKPEKAESyvgaqdpGV 213
|
90 100 110
....*....|....*....|....*....|....*....
gi 489535279 141 KNLTEICNLISINGYNTKVVAASIKNVFHLTQasLCGCD 179
Cdd:PTZ00411 214 ISVTKIYNYYKKHGYKTIVMGASFRNTGEILE--LAGCD 250
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
76-179 |
1.12e-08 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 53.97 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 76 NKNTIIKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGR-----NDENGND--------GIKN 142
Cdd:PRK12309 130 RDRVLIKIASTWEGIKAAEVLEKEGIHCNLTLLFGFHQAIACAEAGVTLISPFVGRildwyKKETGRDsypgaedpGVQS 209
|
90 100 110
....*....|....*....|....*....|....*..
gi 489535279 143 LTEICNLISINGYNTKVVAASIKNVFHLTQasLCGCD 179
Cdd:PRK12309 210 VTQIYNYYKKFGYKTEVMGASFRNIGEIIE--LAGCD 244
|
|
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
95-180 |
8.46e-07 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 48.23 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 95 ILNSKGVKTACTLIFNVNQASLAINAGAdYLF-PFIGR------NDENGND-------GIKNLTEICNLISINGYNTKVV 160
Cdd:PRK05269 145 QLEKEGINCNLTLLFSFAQARACAEAGV-FLIsPFVGRildwykKNTGKKEyapaedpGVVSVTKIYNYYKKHGYKTVVM 223
|
90 100
....*....|....*....|
gi 489535279 161 AASIKNVFHLTQasLCGCDY 180
Cdd:PRK05269 224 GASFRNTGQILE--LAGCDR 241
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
75-190 |
3.02e-04 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 40.86 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489535279 75 INKNTI-IKINFSEVGLELINILNSKGVKTACTLIFNVNQASLAINAGADYLFPFIGR-----NDENGND--------GI 140
Cdd:PRK12346 123 IDKSRIlIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRiydwyQARKPMDpyvveedpGV 202
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489535279 141 KNLTEICNLISINGYNTKVVAASIKNVFHLTqaSLCGCDYAAVTYDLFKK 190
Cdd:PRK12346 203 KSVRNIYDYYKQHRYETIVMGASFRRTEQIL--ALAGCDRLTISPNLLKE 250
|
|
| |
