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Conserved domains on  [gi|2124907205|ref|WP_227126418|]
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MULTISPECIES: transketolase [Enterocloster]

Protein Classification

transketolase( domain architecture ID 10008162)

transketolase with the TPP di-phosphate residue-binding domain but lacking the TPP pyrimidine-binding domain and the C-terminal domain; transketolase catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
2-275 3.12e-142

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


:

Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 400.61  E-value: 3.12e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205   2 REERKETLQKLCLVFRNKLIDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLA 81
Cdd:COG3959     1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  82 HKGFFPLAELKNLRQTGSMLQGHPCVHKTPGVELSTgplglglsaglgMALGSRLKGYDSYTYVIMGDGEIQEGCVWEAA 161
Cdd:COG3959    81 EKGYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTgslgqglsvavgMALAAKLDGKDYRVYVLLGDGELQEGQVWEAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 162 LSASKFKADHLIGILDNNGVQLDGTLEDIMPMGDIKAKWEAFGWNVIPCDGHDVEDICRAVEEAKMTADKPSLILTKTVK 241
Cdd:COG3959   161 MAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVK 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2124907205 242 GKGVSFMEGKNTWHGKAIGDQEYAQAKAELGGDR 275
Cdd:COG3959   241 GKGVSFMENRPKWHGKAPNDEELEQALAELEAEL 274
 
Name Accession Description Interval E-value
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
2-275 3.12e-142

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 400.61  E-value: 3.12e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205   2 REERKETLQKLCLVFRNKLIDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLA 81
Cdd:COG3959     1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  82 HKGFFPLAELKNLRQTGSMLQGHPCVHKTPGVELSTgplglglsaglgMALGSRLKGYDSYTYVIMGDGEIQEGCVWEAA 161
Cdd:COG3959    81 EKGYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTgslgqglsvavgMALAAKLDGKDYRVYVLLGDGELQEGQVWEAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 162 LSASKFKADHLIGILDNNGVQLDGTLEDIMPMGDIKAKWEAFGWNVIPCDGHDVEDICRAVEEAKMTADKPSLILTKTVK 241
Cdd:COG3959   161 MAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVK 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2124907205 242 GKGVSFMEGKNTWHGKAIGDQEYAQAKAELGGDR 275
Cdd:COG3959   241 GKGVSFMENRPKWHGKAPNDEELEQALAELEAEL 274
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 21-268 4.73e-117

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 336.01  E-value: 4.73e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  21 IDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGFFPLAELKNLRQTGSM 100
Cdd:cd02012     8 IDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKTFRQLGSR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 101 LQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRLKGYDSYTYVIMGDGEIQEGCVWEAALSASKFKADHLIGILDNNG 180
Cdd:cd02012    88 LPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLIAIVDSNR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 181 VQLDGTLEDIMPMGDIKAKWEAFGWNVIPCDGHDVEDICRAVEEAKMTADKPSLILTKTVKGKGVSFMEGKNTWHGKAIG 260
Cdd:cd02012   168 IQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAKWHGKPLG 247


                  ....*...
gi 2124907205 261 DQEYAQAK 268
Cdd:cd02012   248 EEEVELAK 255
PRK05899 PRK05899
transketolase; Reviewed
 30-275 3.70e-93

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 286.26  E-value: 3.70e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  30 GHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGF-FPLAELKNLRQTGSMLQGHPCVH 108
Cdd:PRK05899   29 GHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGYdLSIDDLKNFRQLGSKTPGHPEYG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 109 KTPGVELSTgplglglsaglgMALGSRLKG----------YDSYTYVIMGDGEIQEGCVWEAALSASKFKADHLIGILDN 178
Cdd:PRK05899  109 HTPGVETTTgplgqglanavgMALAEKYLAalfnrpgldiVDHYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 179 NGVQLDGTLEDIMPMgDIKAKWEAFGWNVIPCDGHDVEDICRAVEEAKmTADKPSLILTKTVKGKGVSFMEGKNTWHGKA 258
Cdd:PRK05899  189 NRISIDGPTEGWFTE-DVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAK-ASTKPTLIIAKTIIGKGAPNKEGTHKVHGAP 266

                         250
                  ....*....|....*..
gi 2124907205 259 IGDQEYAQAKAELGGDR 275
Cdd:PRK05899  267 LGAEEIAAAKKELGWDY 283
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
 21-274 3.18e-60

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 194.14  E-value: 3.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  21 IDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGF-FPLAELKNLRQTGS 99
Cdd:pfam00456  14 MDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSMEDLKSFRQLGS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 100 MLQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRLK-------GY---DSYTYVIMGDGEIQEGCVWEAALSASKFKA 169
Cdd:pfam00456  94 KTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLaatynrpGFdivDHYTYVFLGDGCLMEGVSSEASSLAGHLGL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 170 DHLIGILDNNGVQLDGTLeDIMPMGDIKAKWEAFGWNVI-PCDGHDVEDICRAVEEAKMTADKPSLILTKTVKGKGVSFM 248
Cdd:pfam00456 174 GNLIVFYDDNQISIDGET-KISFTEDTAARFEAYGWHVIeVEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNK 252

                         250       260
                  ....*....|....*....|....*.
gi 2124907205 249 EGKNTWHGKAIGDQEYAQAKAELGGD 274
Cdd:pfam00456 253 QGTHDVHGAPLGADEVAALKQKLGWD 278
 
Name Accession Description Interval E-value
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
2-275 3.12e-142

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 400.61  E-value: 3.12e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205   2 REERKETLQKLCLVFRNKLIDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLA 81
Cdd:COG3959     1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  82 HKGFFPLAELKNLRQTGSMLQGHPCVHKTPGVELSTgplglglsaglgMALGSRLKGYDSYTYVIMGDGEIQEGCVWEAA 161
Cdd:COG3959    81 EKGYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTgslgqglsvavgMALAAKLDGKDYRVYVLLGDGELQEGQVWEAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 162 LSASKFKADHLIGILDNNGVQLDGTLEDIMPMGDIKAKWEAFGWNVIPCDGHDVEDICRAVEEAKMTADKPSLILTKTVK 241
Cdd:COG3959   161 MAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVK 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2124907205 242 GKGVSFMEGKNTWHGKAIGDQEYAQAKAELGGDR 275
Cdd:COG3959   241 GKGVSFMENRPKWHGKAPNDEELEQALAELEAEL 274
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 21-268 4.73e-117

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 336.01  E-value: 4.73e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  21 IDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGFFPLAELKNLRQTGSM 100
Cdd:cd02012     8 IDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKTFRQLGSR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 101 LQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRLKGYDSYTYVIMGDGEIQEGCVWEAALSASKFKADHLIGILDNNG 180
Cdd:cd02012    88 LPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLIAIVDSNR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 181 VQLDGTLEDIMPMGDIKAKWEAFGWNVIPCDGHDVEDICRAVEEAKMTADKPSLILTKTVKGKGVSFMEGKNTWHGKAIG 260
Cdd:cd02012   168 IQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAKWHGKPLG 247


                  ....*...
gi 2124907205 261 DQEYAQAK 268
Cdd:cd02012   248 EEEVELAK 255
PRK05899 PRK05899
transketolase; Reviewed
 30-275 3.70e-93

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 286.26  E-value: 3.70e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  30 GHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGF-FPLAELKNLRQTGSMLQGHPCVH 108
Cdd:PRK05899   29 GHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGYdLSIDDLKNFRQLGSKTPGHPEYG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 109 KTPGVELSTgplglglsaglgMALGSRLKG----------YDSYTYVIMGDGEIQEGCVWEAALSASKFKADHLIGILDN 178
Cdd:PRK05899  109 HTPGVETTTgplgqglanavgMALAEKYLAalfnrpgldiVDHYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 179 NGVQLDGTLEDIMPMgDIKAKWEAFGWNVIPCDGHDVEDICRAVEEAKmTADKPSLILTKTVKGKGVSFMEGKNTWHGKA 258
Cdd:PRK05899  189 NRISIDGPTEGWFTE-DVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAK-ASTKPTLIIAKTIIGKGAPNKEGTHKVHGAP 266

                         250
                  ....*....|....*..
gi 2124907205 259 IGDQEYAQAKAELGGDR 275
Cdd:PRK05899  267 LGAEEIAAAKKELGWDY 283
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
 21-274 3.18e-60

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 194.14  E-value: 3.18e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  21 IDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGF-FPLAELKNLRQTGS 99
Cdd:pfam00456  14 MDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSMEDLKSFRQLGS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 100 MLQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRLK-------GY---DSYTYVIMGDGEIQEGCVWEAALSASKFKA 169
Cdd:pfam00456  94 KTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLaatynrpGFdivDHYTYVFLGDGCLMEGVSSEASSLAGHLGL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 170 DHLIGILDNNGVQLDGTLeDIMPMGDIKAKWEAFGWNVI-PCDGHDVEDICRAVEEAKMTADKPSLILTKTVKGKGVSFM 248
Cdd:pfam00456 174 GNLIVFYDDNQISIDGET-KISFTEDTAARFEAYGWHVIeVEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNK 252

                         250       260
                  ....*....|....*....|....*.
gi 2124907205 249 EGKNTWHGKAIGDQEYAQAKAELGGD 274
Cdd:pfam00456 253 QGTHDVHGAPLGADEVAALKQKLGWD 278
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
 30-274 9.83e-59

Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439792 [Multi-domain]  Cd Length: 661  Bit Score: 197.92  E-value: 9.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  30 GHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGF-FPLAELKNLRQTGSMLQGHPCVH 108
Cdd:COG0021    25 GHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYdLSLDDLKNFRQLGSKTPGHPEYG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 109 KTPGVELSTgplglglsaglgMALGSRL-------KGY---DSYTYVIMGDGEIQEGCVWEAALSASKFKADHLIGILDN 178
Cdd:COG0021   105 HTPGVETTTgplgqgianavgMAIAERHlaarfnrPGHdivDHYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDD 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 179 NGVQLDGTLE----DimpmgDIKAKWEAFGWNVIPC-DGHDVEDICRAVEEAKMTADKPSLILTKTVKGKGVSFMEGKNT 253
Cdd:COG0021   185 NGISIDGDTDlafsE-----DVAKRFEAYGWHVIRVeDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQGTAK 259

                         250       260
                  ....*....|....*....|.
gi 2124907205 254 WHGKAIGDQEYAQAKAELGGD 274
Cdd:COG0021   260 AHGAPLGAEEIAATKEALGWP 280
PLN02790 PLN02790
transketolase
 21-275 1.51e-49

transketolase


Pssm-ID: 215424 [Multi-domain]  Cd Length: 654  Bit Score: 172.90  E-value: 1.51e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  21 IDLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGF--FPLAELKNLRQTG 98
Cdd:PLN02790    6 IDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQFRQWG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  99 SMLQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSR----------LKGYDSYTYVIMGDGEIQEGCVWEAALSASKFK 168
Cdd:PLN02790   86 SRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKhlaarfnkpdHKIVDHYTYCILGDGCQMEGISNEAASLAGHWG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 169 ADHLIGILDNNGVQLDGTLEdIMPMGDIKAKWEAFGWNVIPCDG--HDVEDICRAVEEAKMTADKPSLILTKTVKGKGVS 246
Cdd:PLN02790  166 LGKLIVLYDDNHISIDGDTE-IAFTEDVDKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYGSP 244

                         250       260
                  ....*....|....*....|....*....
gi 2124907205 247 FMEGKNTWHGKAIGDQEYAQAKAELGGDR 275
Cdd:PLN02790  245 NKANSYSVHGAALGEKEVDATRKNLGWPY 273
PTZ00089 PTZ00089
transketolase; Provisional
 22-274 8.71e-48

transketolase; Provisional


Pssm-ID: 173383 [Multi-domain]  Cd Length: 661  Bit Score: 168.31  E-value: 8.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  22 DLLYSVQTGHPGGSLSCTEILTALYYELMDVDPMNPEKEDRDHLILSKGHGAPMLYLVLAHKGF-FPLAELKNLRQTGSM 100
Cdd:PTZ00089   19 DLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDLKNFRQLGSR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 101 LQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRL-------KGY---DSYTYVIMGDGEIQEGCVWEAALSASKFKAD 170
Cdd:PTZ00089   99 TPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHlaakfnrPGHpifDNYVYVICGDGCLQEGVSQEALSLAGHLGLE 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 171 HLIGILDNNGVQLDGTLeDIMPMGDIKAKWEAFGWNVIP-CDGH-DVEDICRAVEEAKMTADKPSLILTKTVKGKGVSfM 248
Cdd:PTZ00089  179 KLIVLYDDNKITIDGNT-DLSFTEDVEKKYEAYGWHVIEvDNGNtDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYGSS-K 256

                         250       260
                  ....*....|....*....|....*.
gi 2124907205 249 EGKNTWHGKAIGDQEYAQAKAELGGD 274
Cdd:PTZ00089  257 AGTEKVHGAPLGDEDIAQVKELFGLD 282
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
 130-244 1.00e-12

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 65.26  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 130 MALGSRLKGYDSYTYVIMGDGEIQEGCVWEAALSASKFKADHLIgILDNNGVQLDGTledimpMGDIKAKWEAFGWNVI- 208
Cdd:cd02007    87 MAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIV-ILNDNEMSISPN------VGTPGNLFEELGFRYIg 159

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2124907205 209 PCDGHDVEDICRAVEEAKMTaDKPSLILTKTVKGKG 244
Cdd:cd02007   160 PVDGHNIEALIKVLKEVKDL-KGPVLLHVVTKKGKG 194
TPP_E1_EcPDC_like cd02017
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ...
 30-255 1.80e-11

Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.


Pssm-ID: 238975 [Multi-domain]  Cd Length: 386  Bit Score: 63.48  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  30 GHPGGSLSCTEILTALYYELMDVdpmNPEKEDRDHlILSKGHGAPMLYLVLAHKGFFPLAELKNLRQ--TGSMLQGHPCV 107
Cdd:cd02017    31 GHIATFASAATLYEVGFNHFFRA---RGEGGGGDL-VYFQGHASPGIYARAFLEGRLTEEQLDNFRQevGGGGLSSYPHP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 108 HKTPG-VELSTGPlglglsaglgMALGSRLKGYDS--YTYVI---------------MGDGEIQEGCVWEAALSASKFKA 169
Cdd:cd02017   107 WLMPDfWEFPTVS----------MGLGPIQAIYQArfNRYLEdrglkdtsdqkvwafLGDGEMDEPESLGAIGLAAREKL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 170 DHLIGILDNNGVQLDG-TLEDIMPMGDIKAKWEAFGWNVIP--------------------------CD----------- 211
Cdd:cd02017   177 DNLIFVVNCNLQRLDGpVRGNGKIIQELEGIFRGAGWNVIKviwgskwdellakdgggalrqrmeetVDgdyqtlkakdg 256

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124907205 212 --------------------------------GHDVEDICRAVEEAKMTADKPSLILTKTVKGKGV-SFMEGKNTWH 255
Cdd:cd02017   257 ayvrehffgkypelkalvtdlsdedlwalnrgGHDPRKVYAAYKKAVEHKGKPTVILAKTIKGYGLgAAGEGRNHAH 333
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 22-256 1.18e-10

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 61.65  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  22 DLLYSVQT--GHPGGSLSCTEILTALYYELmdvdpmnpeKEDRDHLILSKGHGAPMLYLVLAHKGffplaELKNLRQTGS 99
Cdd:PLN02234   94 DVIFNVSKtgGHLGSNLGVVELTVALHYIF---------NTPHDKILWDVGHQSYPHKILTGRRG-----KMKTIRQTNG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 100 mLQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRLKGYDSYTYVIMGDGEIQEGCVWEAALSASKFKADHLIGILDNN 179
Cdd:PLN02234  160 -LSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNK 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 180 GV-----QLDGTLEDI---------------MPMGDIKAKWEAFGWNVI-PCDGHDVEDICRAVEEAKMTAD-KPSLILT 237
Cdd:PLN02234  239 QVslptaNLDGPTQPVgalscalsrlqsncgMIRETSSTLFEELGFHYVgPVDGHNIDDLVSILETLKSTKTiGPVLIHV 318

                         250       260
                  ....*....|....*....|
gi 2124907205 238 KTVKGKGVSFME-GKNTWHG 256
Cdd:PLN02234  319 VTEKGRGYPYAErADDKYHG 338
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 6-256 6.08e-09

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 56.24  E-value: 6.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205   6 KETLQKLCLVFRNKLIDLLySVQTGHPGGSLSCTEILTALYYELmdvDPmnpekeDRDHLILSKGHGApmlYlvlAHK-- 83
Cdd:PRK05444   21 EEELPQLADEIREFLIDVV-SKTGGHLGSNLGVVELTVALHYVF---DT------PKDRIIWDVGHQA---Y---PHKil 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  84 -GFFplAELKNLRQTGSmLQGHPC----VHKTPGV-----ELSTGPLglglsaglgMALGSRLKGYDSYTYV-IMGDGEI 152
Cdd:PRK05444   85 tGRR--DRFDTLRQKGG-LSGFPKrsesEYDTFGAghsstSISAALG---------MAKARDLKGGEDRKVVaVIGDGAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 153 QEGCVWEAALSASKFKADHLIgILDNNGvqldgtlediM----PMGDIK---AKW------EAFGWNVI-PCDGHDVEDI 218
Cdd:PRK05444  153 TGGMAFEALNNAGDLKSDLIV-ILNDNE----------MsispNVGALSnylARLrsstlfEELGFNYIgPIDGHDLDAL 221

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2124907205 219 CRAVEEAKmTADKPSLILTKTVKGKGVSFMEG-KNTWHG 256
Cdd:PRK05444  222 IETLKNAK-DLKGPVLLHVVTKKGKGYAPAEAdPIKYHG 259
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 17-256 6.53e-09

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 56.27  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  17 RNKLIDLLySVQTGHPGGSLSCTEILTALYYELmdvdpmnpeKEDRDHLILSKGHGA-PMLYLVLAHKGFfplaelKNLR 95
Cdd:PRK12571   34 RAEVISAV-SETGGHLGSSLGVVELTVALHAVF---------NTPKDKLVWDVGHQCyPHKILTGRRDRF------RTLR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  96 QTGSmLQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRLKGYDSYTYVIMGDGEIQEGCVWEAaLSASKFKADHLIGI 175
Cdd:PRK12571   98 QKGG-LSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMAYEA-LNNAGAADRRLIVI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 176 LDNNGVQLDGT-------LEDIM---PMGDIKAK--------------------------------WEAFGWNVI-PCDG 212
Cdd:PRK12571  176 LNDNEMSIAPPvgalaayLSTLRssdPFARLRAIakgveerlpgplrdgarrarelvtgmigggtlFEELGFTYVgPIDG 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2124907205 213 HDVEDICRAVEEAKMTADKPSLILTKTVKGKGVSFMEG-KNTWHG 256
Cdd:PRK12571  256 HDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEAdEDKYHA 300
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 130-240 8.90e-08

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 52.11  E-value: 8.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 130 MALGSRLKGYDSYTYVIMGDGEIQEGCVWEAALSASKFKADhLIGILDNNGVQLDGTLEDIMPMGDIKAKWEAFGWNVIP 209
Cdd:cd02000   116 AALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLP-VIFVCENNGYAISTPTSRQTAGTSIADRAAAYGIPGIR 194

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2124907205 210 CDGHDVEDICRAVEEAKMTA---DKPSLILTKTV 240
Cdd:cd02000   195 VDGNDVLAVYEAAKEAVERAragGGPTLIEAVTY 228
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 1-270 4.16e-05

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 44.51  E-value: 4.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205   1 MREERKETLQKLCLVFRNKLIdLLYSVQTGHPGGSLSCTEILTALYYELMdvdpmNPEkedrDHLILSKGHGAPMLYLVL 80
Cdd:PLN02582   43 MKNLSVKELKQLADELRSDVI-FNVSKTGGHLGSSLGVVELTVALHYVFN-----APQ----DKILWDVGHQSYPHKILT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205  81 AHKGffplaELKNLRQTGSmLQGHPCVHKTPGVELSTGPLGLGLSAGLGMALGSRLKGYDSYTYVIMGDGEIQEGCVWEA 160
Cdd:PLN02582  113 GRRD-----KMHTMRQTNG-LSGFTKRAESEYDCFGTGHSSTTISAGLGMAVGRDLKGKKNNVVAVIGDGAMTAGQAYEA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 161 ALSASKFKADHLIGILDNNGVQLD-----------GTLEDIM-------------------------PMGDIKAKWEAFG 204
Cdd:PLN02582  187 MNNAGYLDSDMIVILNDNKQVSLPtatldgpappvGALSSALsrlqssrplrelrevakgvtkqiggPMHELAAKVDEYA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 205 WNVI-----------------PCDGHDVEDICRAVEEAKMTADK-PSLILTKTVKGKGVSFME-GKNTWHG-----KAIG 260
Cdd:PLN02582  267 RGMIsgsgstlfeelglyyigPVDGHNIDDLVTILREVKSTKTTgPVLIHVVTEKGRGYPYAErAADKYHGvvkfdPATG 346

                         330
                  ....*....|
gi 2124907205 261 DQEYAQAKAE 270
Cdd:PLN02582  347 KQFKVKAKTQ 356
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 130-239 5.23e-05

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 43.98  E-value: 5.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 130 MALGSRLKGYDSYTYVIMGDGEIQEGCVWEAALSASKFKAdHLIGILDNNGVQLDGTLEDIMPMGDIKAKWEAFGWNVIP 209
Cdd:COG1071   139 AALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKL-PVVFVCENNGYAISTPVERQTAVETIADRAAGYGIPGVR 217

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2124907205 210 CDGHDVEDICRAVEEAKMTA---DKPSLILTKT 239
Cdd:COG1071   218 VDGNDVLAVYAAVKEAVERAragEGPTLIEAKT 250
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
 130-256 8.62e-05

Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440768 [Multi-domain]  Cd Length: 623  Bit Score: 43.46  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 130 MALGSRLKGYDSYTYVIMGDGEIQEGCVWEA---------------------------ALSaskfkaDHLIGILDNNGVQ 182
Cdd:COG1154   127 MAVARDLKGEDRKVVAVIGDGALTGGMAFEAlnnaghlkkdlivilndnemsispnvgALS------NYLARLRTSPTYN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 183 -----LDGTLEDIMPMGDI------KAK------------WEAFGWNVI-PCDGHDVEDICRAVEEAKmTADKPSLILTK 238
Cdd:COG1154   201 klreeVKKLLKKLPGIGPPlyelarRAKeglkglvvpgtlFEELGFKYIgPIDGHDLDALVETLRNAK-DLKGPVLLHVV 279

                         170       180
                  ....*....|....*....|
gi 2124907205 239 TVKGKGVSFMEgKN--TWHG 256
Cdd:COG1154   280 TKKGKGYAPAE-KDpdKFHG 298
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 131-235 1.20e-04

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 41.47  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124907205 131 ALGSRLKGYDSYTYVIMGDGEIQEGcvWEAALSASKFKADHLIGILDNNG---------VQLDGTLEDIMPMG-DIKAKW 200
Cdd:cd00568    55 AIGAALAAPDRPVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGGygtirmhqeAFYGGRVSGTDLSNpDFAALA 132

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2124907205 201 EAFGWNVIPCDghDVEDICRAVEEAkMTADKPSLI 235
Cdd:cd00568   133 EAYGAKGVRVE--DPEDLEAALAEA-LAAGGPALI 164
aceE PRK09405
pyruvate dehydrogenase subunit E1; Reviewed
 212-255 2.60e-04

pyruvate dehydrogenase subunit E1; Reviewed


Pssm-ID: 236500 [Multi-domain]  Cd Length: 891  Bit Score: 42.05  E-value: 2.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2124907205 212 GHDVEDICRAVEEAKMTADKPSLILTKTVKGKGV--SFmEGKNTWH 255
Cdd:PRK09405  366 GHDPRKVYAAYKAAVEHKGQPTVILAKTIKGYGMgeAG-EGKNIAH 410
AceE COG2609
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ...
 212-255 8.66e-04

Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]; Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 442021 [Multi-domain]  Cd Length: 891  Bit Score: 40.44  E-value: 8.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2124907205 212 GHDVEDICRAVEEAKMTADKPSLILTKTVKGKGV-SFMEGKNTWH 255
Cdd:COG2609   367 GHDPRKVYAAYKAAVEHKGQPTVILAKTIKGYGMgEAGEGRNITH 411
PRK13012 PRK13012
2-oxoacid dehydrogenase subunit E1; Provisional
 212-255 1.49e-03

2-oxoacid dehydrogenase subunit E1; Provisional


Pssm-ID: 237267 [Multi-domain]  Cd Length: 896  Bit Score: 39.92  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2124907205 212 GHDVEDICRAVEEAKMTADKPSLILTKTVKGKGV-SFMEGKNTWH 255
Cdd:PRK13012  374 GHDPRKVYAAYAAAVRHKGQPTVILAKTKKGYGMgEAGEGRMTTH 418
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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