NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2428127549|ref|WP_270875636|]
View 

transaldolase [Campylobacter sp. JMF_09 ED2]

Protein Classification

transaldolase( domain architecture ID 10012088)

transaldolase transfers a C3 ketol fragment from a ketose donor to an aldose acceptor as part of the non-oxidative branch of the pentose phosphate pathway

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK03903 PRK03903
transaldolase; Provisional
52-332 1.53e-141

transaldolase; Provisional


:

Pssm-ID: 235171  Cd Length: 274  Bit Score: 401.28  E-value: 1.53e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  52 AYGAQKAKFAHKNTKKLYEILAITDIKNAANALLANYAKGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKV 131
Cdd:PRK03903    1 AYKDEIAKLKGKKAKEIYEELAIKDIKKAADKLLPLYEKPDDGFISIEIDPFLEDDAAGSIEEGKRLYKTIGRPNVMIKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 132 PATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEAIKEGTSefaakfEGTKLPQSVISIFVSRFDRALDEDMKKSGLe 211
Cdd:PRK03903   81 PATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEALNEGLK------KNTKDPKAVISVFVSRFDRLLDPKLAPKNL- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 212 PAKIGIMNATKCYNIIAKENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFIGAK-CEPKTPFSDEE 290
Cdd:PRK03903  154 QAKSGIMNATKCYNQIEQHANKNIRTLFASTGVKGDDLPKDYYIKELLFKNSINTAPLDTIEAFLKDGnTEPKKPLKIEE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2428127549 291 IDKFFADVaQKAGIDMDKIYKKLLKDGLVAFEQAFDEIMTTL 332
Cdd:PRK03903  234 IEAFFKEL-KSHNIDLENTYQKLLKDGLEAFKQAFEDILKSL 274
 
Name Accession Description Interval E-value
PRK03903 PRK03903
transaldolase; Provisional
52-332 1.53e-141

transaldolase; Provisional


Pssm-ID: 235171  Cd Length: 274  Bit Score: 401.28  E-value: 1.53e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  52 AYGAQKAKFAHKNTKKLYEILAITDIKNAANALLANYAKGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKV 131
Cdd:PRK03903    1 AYKDEIAKLKGKKAKEIYEELAIKDIKKAADKLLPLYEKPDDGFISIEIDPFLEDDAAGSIEEGKRLYKTIGRPNVMIKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 132 PATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEAIKEGTSefaakfEGTKLPQSVISIFVSRFDRALDEDMKKSGLe 211
Cdd:PRK03903   81 PATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEALNEGLK------KNTKDPKAVISVFVSRFDRLLDPKLAPKNL- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 212 PAKIGIMNATKCYNIIAKENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFIGAK-CEPKTPFSDEE 290
Cdd:PRK03903  154 QAKSGIMNATKCYNQIEQHANKNIRTLFASTGVKGDDLPKDYYIKELLFKNSINTAPLDTIEAFLKDGnTEPKKPLKIEE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2428127549 291 IDKFFADVaQKAGIDMDKIYKKLLKDGLVAFEQAFDEIMTTL 332
Cdd:PRK03903  234 IEAFFKEL-KSHNIDLENTYQKLLKDGLEAFKQAFEDILKSL 274
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
9-327 2.81e-103

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: 306.56  E-value: 2.81e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   9 SLWCDFIERDFIAKEF-SDFLAKGTFNGATSNPSIFKNAITTSQAYGAQ--KAKFAHKNTKKLYEILAITDIKNAANALL 85
Cdd:cd00955     1 SLWLDNLSRSFIDNGFlKRLIEEQGVVGVTSNPAIFEKAIAGSAAYDDQirALKGQGLDAEAIYEALAIEDIQDACDLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  86 AN--YAKGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTA 163
Cdd:cd00955    81 PVyeQTGGNDGYVSLEVSPRLADDTQGTIAEAKRLWKAVGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 164 KCLEAIKEGTSEFAAKFEGTKLPQSVISIFVSRFDRALDEDMKKSGLEPA--KIGIMNATKCYN------------IIAK 229
Cdd:cd00955   161 AVAEAYLRGLERRVEGGGDLSQVASVASFFVSRVDTLIDKKLDAPEAKALqgKVAIANAKLAYQeyqekfsgprwaALAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 230 ENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFI-GAKCEPKTPFSDEEIDKFFADVAqKAGIDMDK 308
Cdd:cd00955   241 AGAKPQRLLWASTGVKNPAYPDVLYVEELIGPDTVNTMPDATLKAFAdHGEVRPTLEEGLEEAERVLAELE-RLGIDLDA 319
                         330
                  ....*....|....*....
gi 2428127549 309 IYKKLLKDGLVAFEQAFDE 327
Cdd:cd00955   320 VTEKLLKEGVKKFKDSFEK 338
tal_mycobact TIGR00876
transaldolase, mycobacterial type; This model describes one of three related but easily ...
8-331 8.29e-78

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: 241.95  E-value: 8.29e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   8 FSLWCDFIERDFI-AKEFSDFLAKGTFNGATSNPSIFKNAITTSQAYGAQKAKFAHK--NTKKLYEILAITDIKNAANAL 84
Cdd:TIGR00876   3 FSLWCDDIERDFLeNGDFLELIDKGAICGATSNPSIFCEAISEGAFYDAEIAELAAKgaDADAIIETLALDDILQACDAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  85 LANYAKGD--DGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQT 162
Cdd:TIGR00876  83 MPLWEDSDgnDGRISIEIDPFLADDAAKSIDEAIELFKILDRPNLFIKIPASEAGIEAISALLAAGIPVNVTLIFSPKIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 163 AKCLEAIKEGTSEFAAKFEGTKLPQSVISIFVSRFDRALDEDMKKSGLEPA-----KIGIMNA-------------TKCY 224
Cdd:TIGR00876 163 GEIADALAKEAEKARQAGHSLSKIHAVASFFVSRFDKEIDKLLDKIGSRQAlelqaQAGIANArlayatyrevfedSDCY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 225 NIIAKENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFI-GAKCEPKTPF-SDEEIDKFFaDVAQKA 302
Cdd:TIGR00876 243 RQIKQDAAKLQRPLFASTGVKNNDLADDLYIKALCAKHSINTAPEEAIDAVAdDGNIECDTPLgTASDAEAFF-DELGAH 321
                         330       340
                  ....*....|....*....|....*....
gi 2428127549 303 GIDMDKIYKKLLKDGLVAFEQAFDEIMTT 331
Cdd:TIGR00876 322 GIDLEDTAAKLEEEGLIAFEASFEELLQE 350
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
10-297 8.39e-68

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: 212.01  E-value: 8.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  10 LWCDFIERDFIAKefsdFLAKGTFNGATSNPSIFKNAITTSQAYGAQkakfahkntkklyeilaITDIKnaanallanya 89
Cdd:pfam00923   1 IWLDTADRDLIKK----LIEEGGIDGVTTNPSIFLKAIEYSALYDEA-----------------IAEIK----------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  90 KGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEAI 169
Cdd:pfam00923  49 EIGDGPVSLEVDPRLADDTEGTIEEARRLIALYGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAG 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 170 KegtsefaakfegtklpqSVISIFVSRFDRALDEDMKKSGLEpaKIGIMNATKCYNIIAKENLpfvralfaSTGVKGGEI 249
Cdd:pfam00923 129 A-----------------SVISPFVGRIDDWGDKRLGAALRG--DDGIANAKEIYQIYKKYGW--------STGVLAASF 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2428127549 250 PADYYIKELLYPLSVnTAPLDTIKAFigakcepktpFSDEEIDKFFAD 297
Cdd:pfam00923 182 RNVLYVLALAGCDTI-TIPPDTLEAL----------AKDEGVRKFAKD 218
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
9-300 1.80e-46

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: 156.77  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   9 SLWCDFIERDFIAKefsdFLAKGTFNGATSNPSIFKNAittsqaygaqkakfAHKNTKKLY-EILAITDiknaanallan 87
Cdd:COG0176     2 KLWLDTADREEIKE----LIDLGGVDGVTTNPSLIAKA--------------GIKDFVEDIrEICDIVD----------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  88 yakgddGFISIEVdpsISDDAEAMIKEGKRLYAQIAmPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLE 167
Cdd:COG0176    53 ------GPVSAEV---LATDTEGMIAEARRLAALYR-PNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAE 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 168 AIKegtsefaakfegtklpqSVISIFVSRFDRAlDEDmkksglepakiGIMNATKCYNIIAKENLPfVRALFASTGvkgg 247
Cdd:COG0176   123 AGA-----------------SYVSPFVGRIDDI-GID-----------GIALVREIYQIYKNYGAR-TRILAASFR---- 168
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2428127549 248 eipADYYIKE--LLYPLSVnTAPLDTIKAFIgakcepKTPFSDEEIDKFFADVAQ 300
Cdd:COG0176   169 ---NPLQVLEaaLAGADTV-TIPPAVLEALA------DHPLTDEGIEKFLADWEK 213
 
Name Accession Description Interval E-value
PRK03903 PRK03903
transaldolase; Provisional
52-332 1.53e-141

transaldolase; Provisional


Pssm-ID: 235171  Cd Length: 274  Bit Score: 401.28  E-value: 1.53e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  52 AYGAQKAKFAHKNTKKLYEILAITDIKNAANALLANYAKGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKV 131
Cdd:PRK03903    1 AYKDEIAKLKGKKAKEIYEELAIKDIKKAADKLLPLYEKPDDGFISIEIDPFLEDDAAGSIEEGKRLYKTIGRPNVMIKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 132 PATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEAIKEGTSefaakfEGTKLPQSVISIFVSRFDRALDEDMKKSGLe 211
Cdd:PRK03903   81 PATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEALNEGLK------KNTKDPKAVISVFVSRFDRLLDPKLAPKNL- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 212 PAKIGIMNATKCYNIIAKENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFIGAK-CEPKTPFSDEE 290
Cdd:PRK03903  154 QAKSGIMNATKCYNQIEQHANKNIRTLFASTGVKGDDLPKDYYIKELLFKNSINTAPLDTIEAFLKDGnTEPKKPLKIEE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2428127549 291 IDKFFADVaQKAGIDMDKIYKKLLKDGLVAFEQAFDEIMTTL 332
Cdd:PRK03903  234 IEAFFKEL-KSHNIDLENTYQKLLKDGLEAFKQAFEDILKSL 274
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
9-327 2.81e-103

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: 306.56  E-value: 2.81e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   9 SLWCDFIERDFIAKEF-SDFLAKGTFNGATSNPSIFKNAITTSQAYGAQ--KAKFAHKNTKKLYEILAITDIKNAANALL 85
Cdd:cd00955     1 SLWLDNLSRSFIDNGFlKRLIEEQGVVGVTSNPAIFEKAIAGSAAYDDQirALKGQGLDAEAIYEALAIEDIQDACDLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  86 AN--YAKGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTA 163
Cdd:cd00955    81 PVyeQTGGNDGYVSLEVSPRLADDTQGTIAEAKRLWKAVGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 164 KCLEAIKEGTSEFAAKFEGTKLPQSVISIFVSRFDRALDEDMKKSGLEPA--KIGIMNATKCYN------------IIAK 229
Cdd:cd00955   161 AVAEAYLRGLERRVEGGGDLSQVASVASFFVSRVDTLIDKKLDAPEAKALqgKVAIANAKLAYQeyqekfsgprwaALAA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 230 ENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFI-GAKCEPKTPFSDEEIDKFFADVAqKAGIDMDK 308
Cdd:cd00955   241 AGAKPQRLLWASTGVKNPAYPDVLYVEELIGPDTVNTMPDATLKAFAdHGEVRPTLEEGLEEAERVLAELE-RLGIDLDA 319
                         330
                  ....*....|....*....
gi 2428127549 309 IYKKLLKDGLVAFEQAFDE 327
Cdd:cd00955   320 VTEKLLKEGVKKFKDSFEK 338
tal_mycobact TIGR00876
transaldolase, mycobacterial type; This model describes one of three related but easily ...
8-331 8.29e-78

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: 241.95  E-value: 8.29e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   8 FSLWCDFIERDFI-AKEFSDFLAKGTFNGATSNPSIFKNAITTSQAYGAQKAKFAHK--NTKKLYEILAITDIKNAANAL 84
Cdd:TIGR00876   3 FSLWCDDIERDFLeNGDFLELIDKGAICGATSNPSIFCEAISEGAFYDAEIAELAAKgaDADAIIETLALDDILQACDAL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  85 LANYAKGD--DGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQT 162
Cdd:TIGR00876  83 MPLWEDSDgnDGRISIEIDPFLADDAAKSIDEAIELFKILDRPNLFIKIPASEAGIEAISALLAAGIPVNVTLIFSPKIA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 163 AKCLEAIKEGTSEFAAKFEGTKLPQSVISIFVSRFDRALDEDMKKSGLEPA-----KIGIMNA-------------TKCY 224
Cdd:TIGR00876 163 GEIADALAKEAEKARQAGHSLSKIHAVASFFVSRFDKEIDKLLDKIGSRQAlelqaQAGIANArlayatyrevfedSDCY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 225 NIIAKENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFI-GAKCEPKTPF-SDEEIDKFFaDVAQKA 302
Cdd:TIGR00876 243 RQIKQDAAKLQRPLFASTGVKNNDLADDLYIKALCAKHSINTAPEEAIDAVAdDGNIECDTPLgTASDAEAFF-DELGAH 321
                         330       340
                  ....*....|....*....|....*....
gi 2428127549 303 GIDMDKIYKKLLKDGLVAFEQAFDEIMTT 331
Cdd:TIGR00876 322 GIDLEDTAAKLEEEGLIAFEASFEELLQE 350
PRK03343 PRK03343
transaldolase; Validated
9-335 6.54e-68

transaldolase; Validated


Pssm-ID: 235117  Cd Length: 368  Bit Score: 216.99  E-value: 6.54e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   9 SLWCDFIERDFIAK-EFSDFLAKGTFNGATSNPSIFKNAITTSQAYGAQ--KAKFAHKNTKKLYEILAITDIKNA--ANA 83
Cdd:PRK03343   14 SIWLDDLSRDRLTSgNLARLIDEKGVVGVTSNPAIFQKAIAGGDAYDAQiaELAAAGADVEEAYEELTTADVRNAcdVLR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  84 LLANYAKGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTA 163
Cdd:PRK03343   94 PVYEATGGVDGRVSIEVSPRLAHDTEATIAEARRLWAAVDRPNLMIKIPATPEGLPAIEALIAEGISVNVTLIFSVERYR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 164 KCLEAIKEGTSEFAAKFEGTKLPQSVISIFVSRFDRALDEDMKKSGLEPA-----KIGIMNATKCYNI------------ 226
Cdd:PRK03343  174 AVADAYLRGLEKRLAAGHDLSKIHSVASFFVSRVDTEVDKRLEAIGTDEAlalrgKAAIANARLAYQAyeevfasprwaa 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 227 IAKENLPFVRALFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAFIgAKCEPKTPFSD--EEIDKFFADVAqKAGI 304
Cdd:PRK03343  254 LAAAGARPQRPLWASTGTKNPAYSDTLYVDELVAPDTVNTMPEATLDAFA-DHGEVADTLTGdyEEAQAVLAALA-ALGI 331
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2428127549 305 DMDKIYKKLLKDGLVAFEQAFDEIMTTLEKE 335
Cdd:PRK03343  332 DLDDVTAVLEEEGVDKFEASWNELLASLEAK 362
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
10-297 8.39e-68

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: 212.01  E-value: 8.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  10 LWCDFIERDFIAKefsdFLAKGTFNGATSNPSIFKNAITTSQAYGAQkakfahkntkklyeilaITDIKnaanallanya 89
Cdd:pfam00923   1 IWLDTADRDLIKK----LIEEGGIDGVTTNPSIFLKAIEYSALYDEA-----------------IAEIK----------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  90 KGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEAI 169
Cdd:pfam00923  49 EIGDGPVSLEVDPRLADDTEGTIEEARRLIALYGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAG 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 170 KegtsefaakfegtklpqSVISIFVSRFDRALDEDMKKSGLEpaKIGIMNATKCYNIIAKENLpfvralfaSTGVKGGEI 249
Cdd:pfam00923 129 A-----------------SVISPFVGRIDDWGDKRLGAALRG--DDGIANAKEIYQIYKKYGW--------STGVLAASF 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2428127549 250 PADYYIKELLYPLSVnTAPLDTIKAFigakcepktpFSDEEIDKFFAD 297
Cdd:pfam00923 182 RNVLYVLALAGCDTI-TIPPDTLEAL----------AKDEGVRKFAKD 218
PRK09533 PRK09533
bifunctional transaldolase/phosoglucose isomerase; Validated
9-333 3.22e-62

bifunctional transaldolase/phosoglucose isomerase; Validated


Pssm-ID: 236551 [Multi-domain]  Cd Length: 948  Bit Score: 213.29  E-value: 3.22e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   9 SLWCDFIERDFIAK-EFSDFLAKGTFNGATSNPSIFKNAITTSQAYGAQKAKFAHKNTK---KLYEILAITDIKNAANAL 84
Cdd:PRK09533   13 SVWLDFLARGFIAKgELKRLVEEDGLRGVTSNPAIFEKAIGSSDEYDDAIKAALAEGDRsviELYETLAIEDIQAAADVL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  85 LAN--YAKGDDGFISIEVDPSISDDAEAMIKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQT 162
Cdd:PRK09533   93 RPVydATDGADGFVSLEVSPYLALDTEGTIAEARRLWAAVDRPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFSQDVY 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 163 AKCLEAIKEGTSEFAAKFEGTKLPQSVISIFVSRFDRALD---EDMKKSGLEPA----------KIGIMNATKCYN---- 225
Cdd:PRK09533  173 EEVAEAYISGLEARAAKGGDPSHVASVASFFVSRIDSAVDkrlDEKIAAANDPAekaalealkgKVAIANAKLAYQrykr 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 226 IIAKENLPFVRA--------LFASTGVKGGEIPADYYIKELLYPLSVNTAPLDTIKAF-----IGAKCEPKTpfsdEEID 292
Cdd:PRK09533  253 LFAGPRWEALAAkgakpqrlLWASTGTKNKAYSDVLYVEELIGPDTVNTMPPATLDAFrdhgkVRATLEEDV----DEAR 328
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2428127549 293 KFFADVAQkAGIDMDKIYKKLLKDGLVAFEQAFDEIMTTLE 333
Cdd:PRK09533  329 AVLADLAE-AGISLDAVTDKLVAEGVQLFADAFDKLLGAVA 368
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
9-300 1.80e-46

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: 156.77  E-value: 1.80e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549   9 SLWCDFIERDFIAKefsdFLAKGTFNGATSNPSIFKNAittsqaygaqkakfAHKNTKKLY-EILAITDiknaanallan 87
Cdd:COG0176     2 KLWLDTADREEIKE----LIDLGGVDGVTTNPSLIAKA--------------GIKDFVEDIrEICDIVD----------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  88 yakgddGFISIEVdpsISDDAEAMIKEGKRLYAQIAmPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLE 167
Cdd:COG0176    53 ------GPVSAEV---LATDTEGMIAEARRLAALYR-PNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAE 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 168 AIKegtsefaakfegtklpqSVISIFVSRFDRAlDEDmkksglepakiGIMNATKCYNIIAKENLPfVRALFASTGvkgg 247
Cdd:COG0176   123 AGA-----------------SYVSPFVGRIDDI-GID-----------GIALVREIYQIYKNYGAR-TRILAASFR---- 168
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2428127549 248 eipADYYIKE--LLYPLSVnTAPLDTIKAFIgakcepKTPFSDEEIDKFFADVAQ 300
Cdd:COG0176   169 ---NPLQVLEaaLAGADTV-TIPPAVLEALA------DHPLTDEGIEKFLADWEK 213
Transaldolase cd00439
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
35-268 9.10e-27

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: 106.28  E-value: 9.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  35 GATSNPSIFKNAITTSQAYGAQKAKFAH--KNTKKLYEILAITDIKNAANALLANYAK-GDDGFISIEVDPSISDDAEAM 111
Cdd:cd00439    23 GVTTNPSIIQAAISTSNAYNDQFRTLVEsgKDIESAYWELVVKDIQDACKLFEPIYDQtEADGRVSVEVSARLADDTQGM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 112 IKEGKRLYAQIAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEAikeGTsefaakfegtklpqSVIS 191
Cdd:cd00439   103 VEAAKYLSKVVNRRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVADA---GT--------------SVAS 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2428127549 192 IFVSRFDRALDEDMKKSGLEP-AKIGIMNATKCYNIIaKENLPFVRALFASTGVKGgeipadyYIKELLYPLSVNTAP 268
Cdd:cd00439   166 PFVSRIDTLMDKMLEQIGLDLrGKAGVAQVTLAYKLY-KQKFKKQRVLWASFSDTL-------YVAPLIGCDTVTTMP 235
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
22-199 5.19e-19

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: 83.78  E-value: 5.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  22 KEFSDFlakGTFNGATSNPSIFknaittsqaygaqkAKFAHKNTKKLY-EILAITDiknaanallanyakgddGFISIEV 100
Cdd:cd00956    13 KKASET---GLLDGVTTNPSLI--------------AKSGRIDFEAVLkEICEIID-----------------GPVSAQV 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549 101 dpsISDDAEAMIKEGKRLYAQIamPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTakcLEAIKEGtsefaAKF 180
Cdd:cd00956    59 ---VSTDAEGMVAEARKLASLG--GNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQA---LLAAKAG-----ATY 125
                         170
                  ....*....|....*....
gi 2428127549 181 egtklpqsvISIFVSRFDR 199
Cdd:cd00956   126 ---------VSPFVGRIDD 135
Transaldolase_TalAB cd00957
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ...
26-231 2.77e-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: 66.49  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  26 DFLAKGTFNGATSNPSI---------FKNAITTSQAYGAQKAKFAHKNTKKLYEILAI---TDIknaanallanyAKGDD 93
Cdd:cd00957    20 EAIKKFKPQDATTNPSLilaaaklpeYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVnfgTEI-----------LKLIP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  94 GFISIEVDPSISDDAEAMIKEGKR---LYAQIAMPN--VMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEA 168
Cdd:cd00957    89 GRVSTEVDARLSFDTNATIAKARKlikLYEEAGIDKerILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQAVACAEA 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2428127549 169 ikegtsefaakfegtklPQSVISIFVSRFdraLDEDMKKSGLEPAKI----GIMNATKCYNIIAKEN 231
Cdd:cd00957   169 -----------------GVTLISPFVGRI---LDWYKKHSGDKAYTAeedpGVASVKKIYNYYKKFG 215
PTZ00411 PTZ00411
transaldolase-like protein; Provisional
93-231 1.01e-10

transaldolase-like protein; Provisional


Pssm-ID: 240406  Cd Length: 333  Bit Score: 62.06  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  93 DGFISIEVDPSISDDAEAMIKEGKR---LYAQ--IAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLE 167
Cdd:PTZ00411  100 PGRVSTEVDARLSFDKQAMVDKARKiikMYEEagISKDRILIKLASTWEGIQAAKALEKEGIHCNLTLLFSFAQAVACAQ 179
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2428127549 168 AikegtsefaakfeGTKLpqsvISIFVSRFDRALDEDMKKSGLEPAK-IGIMNATKCYNIIAKEN 231
Cdd:PTZ00411  180 A-------------GVTL----ISPFVGRILDWYKKPEKAESYVGAQdPGVISVTKIYNYYKKHG 227
PRK05269 PRK05269
transaldolase B; Provisional
36-168 1.51e-09

transaldolase B; Provisional


Pssm-ID: 235381 [Multi-domain]  Cd Length: 318  Bit Score: 58.25  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  36 ATSNPSIFKNAITT-------SQAYGAQKAKFAHKNTK------KLY-----EILAITDiknaanallanyakgddGFIS 97
Cdd:PRK05269   32 ATTNPSLILKAAQIpeyapliDDAVAWAKQQSGDRAQQiddaidKLAvnfglEILKLIP-----------------GRVS 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2428127549  98 IEVDPSISDDAEAMIKEGKRL---YAQIAMPN--VMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEA 168
Cdd:PRK05269   95 TEVDARLSFDTEATIAKARKLialYEEAGISKdrILIKIASTWEGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 170
PRK12309 PRK12309
transaldolase;
94-225 8.27e-09

transaldolase;


Pssm-ID: 183426 [Multi-domain]  Cd Length: 391  Bit Score: 56.28  E-value: 8.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  94 GFISIEVDPSISDDAEAMIKEGKRLYAQ-----IAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEA 168
Cdd:PRK12309   95 GRVSTEVDARLSYDTEATIAKARKLISLyedagISRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTLLFGFHQAIACAEA 174
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2428127549 169 ikegtsefaakfeGTKLpqsvISIFVSRFdraLDEDMKKSGLE----PAKIGIMNATKCYN 225
Cdd:PRK12309  175 -------------GVTL----ISPFVGRI---LDWYKKETGRDsypgAEDPGVQSVTQIYN 215
PRK12346 PRK12346
transaldolase A; Provisional
94-196 1.22e-06

transaldolase A; Provisional


Pssm-ID: 183458  Cd Length: 316  Bit Score: 49.33  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428127549  94 GFISIEVDPSISDDAEAMIKEGKRL---YAQ--IAMPNVMIKVPATQAGYETMRALTRRGINVNATLIFSPEQTAKCLEA 168
Cdd:PRK12346   90 GRVSTEVDARLSFDREKSIEKARHLvdlYQQqgIDKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEA 169
                          90       100
                  ....*....|....*....|....*...
gi 2428127549 169 ikegtsefaakfeGTKLpqsvISIFVSR 196
Cdd:PRK12346  170 -------------GVFL----ISPFVGR 180
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH