|
Name |
Accession |
Description |
Interval |
E-value |
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
9-275 |
3.94e-148 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 415.63 E-value: 3.94e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 9 QQIKEQARLIRRNVITL--NAGSpagGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQA 86
Cdd:COG3959 6 KELEEKARQIRRDILRMiyAAGS---GHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 87 GYIPEAWLPEYQHFNSRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEAAMA 166
Cdd:COG3959 83 GYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKLDGKDYRVYVLLGDGELQEGQVWEAAMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 167 AAKYGLDNLFVIVDKNKLQLAGLTAEIMPLDPLDEKWAAFGFTVSECDGNDVGQLVTALEQMQLRKGAPQVLIAHTIKGK 246
Cdd:COG3959 163 AAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKGK 242
|
250 260
....*....|....*....|....*....
gi 492120632 247 GVSFIEGRSEWHHRVPKGDEVSAALEELN 275
Cdd:COG3959 243 GVSFMENRPKWHGKAPNDEELEQALAELE 271
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
18-271 |
9.00e-120 |
|
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: 342.95 E-value: 9.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 18 IRRNVI--TLNAGSpagGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQAGYIPEAWLP 95
Cdd:cd02012 3 IRRLSIdmVQKAGS---GHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 96 EYQHFNSRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEAAMAAAKYGLDNL 175
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 176 FVIVDKNKLQLAGLTAEIMPLDPLDEKWAAFGFTVSECDGNDVGQLVTALEQMQLRKGAPQVLIAHTIKGKGVSFIEGRS 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 492120632 256 EWHHRVPKGDEVSAAL 271
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
12-275 |
1.64e-72 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 232.72 E-value: 1.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 12 KEQARLIRRNVI--TLNAGSpagGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQAGY- 88
Cdd:PRK05899 9 QLLANAIRVLSIdaVQKANS---GHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGYd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 89 IPEAWLPEYQHFNSRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGST----------KRIYVLTGDGELAEG 158
Cdd:PRK05899 86 LSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALfnrpgldivdHYTYVLCGDGDLMEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 159 SNWEAAMAAAKYGLDNLFVIVDKNKLQLAGLTAEIMPLDpLDEKWAAFGFTVSECDGNDVGQLVTALEQMQlRKGAPQVL 238
Cdd:PRK05899 166 ISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAK-ASTKPTLI 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 492120632 239 IAHTIKGKGVSFIEGRSEWHHRVPKGDEVSAALEELN 275
Cdd:PRK05899 244 IAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELG 280
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
32-274 |
5.92e-37 |
|
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: 133.67 E-value: 5.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 32 GGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQAGY-IPEAWLPEYQHFNSRLPGHPVR 110
Cdd:pfam00456 22 SGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSMEDLKSFRQLGSKTPGHPEF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 111 QKTPGIELNTGALGHGLPVAVGLALAAKM----------SGSTKRIYVLTGDGELAEGSNWEAAMAAAKYGLDNLFVIVD 180
Cdd:pfam00456 102 GHTAGVEVTTGPLGQGIANAVGMAIAERNlaatynrpgfDIVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFYD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 181 KNKLQLAGLTaEIMPLDPLDEKWAAFGFTVSE-CDGNDVGQLVTALEQMQLRKGAPQVLIAHTIKGKGVSFIEGRSEWHH 259
Cdd:pfam00456 182 DNQISIDGET-KISFTEDTAARFEAYGWHVIEvEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNKQGTHDVHG 260
|
250
....*....|....*
gi 492120632 260 RVPKGDEVSAALEEL 274
Cdd:pfam00456 261 APLGADEVAALKQKL 275
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
9-275 |
3.94e-148 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 415.63 E-value: 3.94e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 9 QQIKEQARLIRRNVITL--NAGSpagGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQA 86
Cdd:COG3959 6 KELEEKARQIRRDILRMiyAAGS---GHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 87 GYIPEAWLPEYQHFNSRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEAAMA 166
Cdd:COG3959 83 GYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKLDGKDYRVYVLLGDGELQEGQVWEAAMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 167 AAKYGLDNLFVIVDKNKLQLAGLTAEIMPLDPLDEKWAAFGFTVSECDGNDVGQLVTALEQMQLRKGAPQVLIAHTIKGK 246
Cdd:COG3959 163 AAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKGK 242
|
250 260
....*....|....*....|....*....
gi 492120632 247 GVSFIEGRSEWHHRVPKGDEVSAALEELN 275
Cdd:COG3959 243 GVSFMENRPKWHGKAPNDEELEQALAELE 271
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
18-271 |
9.00e-120 |
|
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: 342.95 E-value: 9.00e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 18 IRRNVI--TLNAGSpagGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQAGYIPEAWLP 95
Cdd:cd02012 3 IRRLSIdmVQKAGS---GHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 96 EYQHFNSRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEAAMAAAKYGLDNL 175
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 176 FVIVDKNKLQLAGLTAEIMPLDPLDEKWAAFGFTVSECDGNDVGQLVTALEQMQLRKGAPQVLIAHTIKGKGVSFIEGRS 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 492120632 256 EWHHRVPKGDEVSAAL 271
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
12-275 |
1.64e-72 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 232.72 E-value: 1.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 12 KEQARLIRRNVI--TLNAGSpagGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQAGY- 88
Cdd:PRK05899 9 QLLANAIRVLSIdaVQKANS---GHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGYd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 89 IPEAWLPEYQHFNSRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGST----------KRIYVLTGDGELAEG 158
Cdd:PRK05899 86 LSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALfnrpgldivdHYTYVLCGDGDLMEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 159 SNWEAAMAAAKYGLDNLFVIVDKNKLQLAGLTAEIMPLDpLDEKWAAFGFTVSECDGNDVGQLVTALEQMQlRKGAPQVL 238
Cdd:PRK05899 166 ISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAK-ASTKPTLI 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 492120632 239 IAHTIKGKGVSFIEGRSEWHHRVPKGDEVSAALEELN 275
Cdd:PRK05899 244 IAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELG 280
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
33-274 |
1.49e-37 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 140.20 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 33 GHTGADLSETDILATLYFRILDISPErieDPA---RDIYIQSKGHGVGGLYCCLAQAGY-IPEAWLPEYQHFNSRLPGHP 108
Cdd:PTZ00089 27 GHPGAPMGMAPIAHILWSEVMKYNPK---DPRwinRDRFVLSNGHASALLYSMLHLTGYdLSMEDLKNFRQLGSRTPGHP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 109 VRQKTPGIELNTGALGHGLPVAVGLALAAKMSGST----------KRIYVLTGDGELAEGSNWEAAMAAAKYGLDNLFVI 178
Cdd:PTZ00089 104 ERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKfnrpghpifdNYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 179 VDKNKLQLAGLTAEIMPLDPLdEKWAAFGFTVSE-CDGN-DVGQLVTALEQMQLRKGAPQVLIAHTIKGKGVSfIEGrSE 256
Cdd:PTZ00089 184 YDDNKITIDGNTDLSFTEDVE-KKYEAYGWHVIEvDNGNtDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYGSS-KAG-TE 260
|
250
....*....|....*...
gi 492120632 257 WHHRVPKGDEVSAALEEL 274
Cdd:PTZ00089 261 KVHGAPLGDEDIAQVKEL 278
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
32-274 |
5.92e-37 |
|
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: 133.67 E-value: 5.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 32 GGHTGADLSETDILATLYFRILDISPERIEDPARDIYIQSKGHGVGGLYCCLAQAGY-IPEAWLPEYQHFNSRLPGHPVR 110
Cdd:pfam00456 22 SGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSMEDLKSFRQLGSKTPGHPEF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 111 QKTPGIELNTGALGHGLPVAVGLALAAKM----------SGSTKRIYVLTGDGELAEGSNWEAAMAAAKYGLDNLFVIVD 180
Cdd:pfam00456 102 GHTAGVEVTTGPLGQGIANAVGMAIAERNlaatynrpgfDIVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFYD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 181 KNKLQLAGLTaEIMPLDPLDEKWAAFGFTVSE-CDGNDVGQLVTALEQMQLRKGAPQVLIAHTIKGKGVSFIEGRSEWHH 259
Cdd:pfam00456 182 DNQISIDGET-KISFTEDTAARFEAYGWHVIEvEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNKQGTHDVHG 260
|
250
....*....|....*
gi 492120632 260 RVPKGDEVSAALEEL 274
Cdd:pfam00456 261 APLGADEVAALKQKL 275
|
|
| PLN02790 |
PLN02790 |
transketolase |
33-275 |
1.12e-30 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 120.51 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 33 GHTGADLSETDILATLYFRILDISPErieDPA---RDIYIQSKGHGVGGLYCCLAQAGY--IPEAWLPEYQHFNSRLPGH 107
Cdd:PLN02790 15 GHPGLPMGCAPMGHVLYDEVMKYNPK---NPYwfnRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQFRQWGSRTPGH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 108 PVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGST----------KRIYVLTGDGELAEGSNWEAAMAAAKYGLDNLFV 177
Cdd:PLN02790 92 PENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARfnkpdhkivdHYTYCILGDGCQMEGISNEAASLAGHWGLGKLIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 178 IVDKNKLQLAGLTaEIMPLDPLDEKWAAFGFTVSECDG--NDVGQLVTALEQMQLRKGAPQVLIAHTIKGKGvSFIEGRS 255
Cdd:PLN02790 172 LYDDNHISIDGDT-EIAFTEDVDKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYG-SPNKANS 249
|
250 260
....*....|....*....|.
gi 492120632 256 EWHHRVPKG-DEVSAALEELN 275
Cdd:PLN02790 250 YSVHGAALGeKEVDATRKNLG 270
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
27-247 |
7.64e-27 |
|
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: 109.33 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 27 AGSpagGHTGADLSETDILATLYFRILDISPErieDPA---RDIYIQSKGHGVGGLYCCLAQAGY-IPeawLPEYQHF-- 100
Cdd:COG0021 22 ANS---GHPGLPMGMAPIAYVLWTKFLKHNPA---NPKwpnRDRFVLSAGHGSMLLYSLLHLTGYdLS---LDDLKNFrq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 101 -NSRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGST----------KRIYVLTGDGELAEGSNWEAAMAAAK 169
Cdd:COG0021 93 lGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARfnrpghdivdHYTYVIAGDGDLMEGISHEAASLAGH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 170 YGLDNLFVIVDKNKLQLAGLTaeimpldpldEKW---------AAFGFTVSEC-DGNDVGQLVTALEQMQLRKGAPQVLI 239
Cdd:COG0021 173 LKLGKLIVLYDDNGISIDGDT----------DLAfsedvakrfEAYGWHVIRVeDGHDLEAIDAAIEAAKAETDKPTLII 242
|
....*...
gi 492120632 240 AHTIKGKG 247
Cdd:COG0021 243 CKTIIGYG 250
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
112-252 |
2.36e-12 |
|
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: 65.59 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 112 KTPGIELNTGALGHGLPVAVGLALAAKMSGsTKRI-YVLTGDGELAEGSNWEAAMAAAKYGLDNLFVIVDkNKLQLAGLT 190
Cdd:cd02000 95 KEKNFFGGNGIVGGQVPLAAGAALALKYRG-EDRVaVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPT 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492120632 191 AEIMPLDPLDEKWAAFGFTVSECDGNDVGQLVTALEQmqlrkgapqvLIAHTIKGKGVSFIE 252
Cdd:cd02000 173 SRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKE----------AVERARAGGGPTLIE 224
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
124-247 |
2.81e-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: 64.10 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 124 GHG---LPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEaAMAAAKYGLDNLFVIVDKNKlqlagltaeiMPLDPLD 200
Cdd:cd02007 75 GHSstsISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFE-ALNNAGYLKSNMIVILNDNE----------MSISPNV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 492120632 201 EK----WAAFGFT-VSECDGNDVGQLVTALEQMQLRKGaPQVLIAHTIKGKG 247
Cdd:cd02007 144 GTpgnlFEELGFRyIGPVDGHNIEALIKVLKEVKDLKG-PVLLHVVTKKGKG 194
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
107-242 |
5.14e-10 |
|
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: 57.27 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 107 HPVRQKTPGIELNTGALGHGLPVAVGLALAAKmsgsTKRIYVLTGDGELAEgsNWEAAMAAAKYGLDNLFVIVD------ 180
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP----DRPVVCIAGDGGFMM--TGQELATAVRYGLPVIVVVFNnggygt 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492120632 181 -----KNKLQLAGLTAEIMPLDpLDEKWAAFGFTVSECDgnDVGQLVTALEQMQLRKGaPQVLIAHT 242
Cdd:cd00568 106 irmhqEAFYGGRVSGTDLSNPD-FAALAEAYGAKGVRVE--DPEDLEAALAEALAAGG-PALIEVKT 168
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
120-252 |
9.02e-10 |
|
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: 58.23 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 120 TGALGHGLPVAVGLALAAKMSGsTKRI-YVLTGDGELAEGSNWEAAMAAAKYGLDNLFVIVDkNKLQLAGLTAEIMPLDP 198
Cdd:COG1071 126 SGIVGGQLPHAVGAALAAKLRG-EDEVaVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAISTPVERQTAVET 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 492120632 199 LDEKWAAFGFTVSECDGNDVGQLVTALEQmqlrkgapqvLIAHTIKGKGVSFIE 252
Cdd:COG1071 204 IADRAAGYGIPGVRVDGNDVLAVYAAVKE----------AVERARAGEGPTLIE 247
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-262 |
1.69e-09 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 58.09 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 122 ALGH---GLPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEAAMAAAKYGlDNLFVIVDKNKLQLA----GLTAEIM 194
Cdd:PRK12315 111 TVGHtstSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAenhgGLYKNLK 189
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492120632 195 PLDPLDEKWA-----AFGFT---VSecDGNDVGQLVTALEQMQLRKgAPQVLIAHTIKGKGVSF-IEGRSEWHHRVP 262
Cdd:PRK12315 190 ELRDTNGQSEnnlfkAMGLDyryVE--DGNDIESLIEAFKEVKDID-HPIVLHIHTLKGKGYQPaEENKEAFHWHMP 263
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
130-265 |
2.01e-09 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 57.78 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 130 AVGLALAAKMSGSTKR--IYVLtGDGELAEGSNWEAaMAAAKYGLDNLFVIVDKNKL-----------QLAGLTAEIMpl 196
Cdd:PRK05444 126 ALGMAKARDLKGGEDRkvVAVI-GDGALTGGMAFEA-LNNAGDLKSDLIVILNDNEMsispnvgalsnYLARLRSSTL-- 201
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 197 dpldekWAAFGFT-VSECDGNDVGQLVTALEQMQLRKGaPQVLIAHTIKGKGVSFIEGRSEWHHRVPKGD 265
Cdd:PRK05444 202 ------FEELGFNyIGPIDGHDLDALIETLKNAKDLKG-PVLLHVVTKKGKGYAPAEADPIKYHGVGKFD 264
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
9-188 |
4.62e-07 |
|
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: 50.38 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 9 QQIKEQAR-LIRRNVITLN--AGSPA---GGHTGADLSETDILATLYFRILdiSPERIEDPARDIYIQskGHGVGGLYcc 82
Cdd:cd02017 1 LEIERRIRsLIRWNAMAMVhrANKKDlgiGGHIATFASAATLYEVGFNHFF--RARGEGGGGDLVYFQ--GHASPGIY-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 83 lAQA---GYIPEAWLPEYQHF--NSRLPGHPVRQKTPGI-ELNTGALGHGLPVAVGLALAAK-------MSGSTKRIYVL 149
Cdd:cd02017 75 -ARAfleGRLTEEQLDNFRQEvgGGGLSSYPHPWLMPDFwEFPTVSMGLGPIQAIYQARFNRyledrglKDTSDQKVWAF 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 492120632 150 TGDGELAEGSNWEAAMAAAKYGLDNLFVIVDKNKLQLAG 188
Cdd:cd02017 154 LGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDG 192
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-268 |
7.17e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 50.11 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 5 RYDAQQIKEQARLIRRNVItlNAGSPAGGHTGADLSETDilatlyfriLDISPERIEDPARDIYIQSKGH---------G 75
Cdd:PRK12571 20 ALSDAELEQLADELRAEVI--SAVSETGGHLGSSLGVVE---------LTVALHAVFNTPKDKLVWDVGHqcyphkiltG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 76 VGGLYCCLAQAGyipeawlpeyqhfnsRLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGSTKRIYVLTGDGEL 155
Cdd:PRK12571 89 RRDRFRTLRQKG---------------GLSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 156 AEGSNWEaAMAAAKYGLDNLFVIVDKNKLQLA----GLTAEIMPL---DPLDEKWAA----------------------- 205
Cdd:PRK12571 154 TAGMAYE-ALNNAGAADRRLIVILNDNEMSIAppvgALAAYLSTLrssDPFARLRAIakgveerlpgplrdgarrarelv 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492120632 206 ------------FGFT-VSECDGNDVGQLVTALEQMQLRKGAPQVLIAHTIKGKGVSFIEGRSEWHHRVPKGDEVS 268
Cdd:PRK12571 233 tgmigggtlfeeLGFTyVGPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADEDKYHAVGKFDVVT 308
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
104-265 |
1.45e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 49.33 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 104 LPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEaAMAAAKYGLDNLFVIVDKNK 183
Cdd:PLN02234 160 LSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKGMNNSVVSVIGDGAMTAGQAYE-AMNNAGYLHSNMIVILNDNK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 184 lQLAGLTAEI-MPLDPLDEKWAAFGFTVSEC----------------------DGNDVGQLVTALEQMQLRKGAPQVLI- 239
Cdd:PLN02234 239 -QVSLPTANLdGPTQPVGALSCALSRLQSNCgmiretsstlfeelgfhyvgpvDGHNIDDLVSILETLKSTKTIGPVLIh 317
|
170 180
....*....|....*....|....*.
gi 492120632 240 AHTIKGKGVSFIEGRSEWHHRVPKGD 265
Cdd:PLN02234 318 VVTEKGRGYPYAERADDKYHGVLKFD 343
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
98-252 |
2.33e-04 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 40.65 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 98 QHFNSRLPGHPVrqkTPGIelnTGALGHGLPVAVGlalaAKMSGSTKRIYVLTGDGELaeGSNWEAAMAAAKYGLDNLFV 177
Cdd:pfam02775 11 QYYRFRPPRRYL---TSGG---LGTMGYGLPAAIG----AKLARPDRPVVAIAGDGGF--QMNLQELATAVRYNLPITVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 178 IVD-------KNKLQLAGL----TAEIMPLDPLD-EKWA-AFGFTVseCDGNDVGQLVTALEQMqlrkgapqvliahtIK 244
Cdd:pfam02775 79 VLNnggygmtRGQQTPFGGgrysGPSGKILPPVDfAKLAeAYGAKG--ARVESPEELEEALKEA--------------LE 142
|
....*...
gi 492120632 245 GKGVSFIE 252
Cdd:pfam02775 143 HDGPALID 150
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
121-208 |
5.41e-04 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 39.89 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492120632 121 GALGHGLPVAVGLALAAkmsgSTKRIYVLTGDGelaeGSNW--EAAMAAAKYGLDNLFVIVDkNK--LQLAGLTAEIMPL 196
Cdd:cd02002 49 GGLGWGLPAAVGAALAN----PDRKVVAIIGDG----SFMYtiQALWTAARYGLPVTVVILN-NRgyGALRSFLKRVGPE 119
|
90
....*....|..
gi 492120632 197 DPLDEKWAAFGF 208
Cdd:cd02002 120 GPGENAPDGLDL 131
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
109-182 |
1.02e-03 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 39.05 E-value: 1.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492120632 109 VRQKTPGIELNTGALGHgLPVAVGLALAAKMSGSTKRIYVLTGDGelAEGSNweaAM---AAAKYGLDNLFVIVDKN 182
Cdd:cd02004 33 LRPRKPRHRLDAGTFGT-LGVGLGYAIAAALARPDKRVVLVEGDG--AFGFS---GMeleTAVRYNLPIVVVVGNNG 103
|
|
| PRK06457 |
PRK06457 |
pyruvate dehydrogenase; Provisional |
121-194 |
1.24e-03 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180570 [Multi-domain] Cd Length: 549 Bit Score: 40.20 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492120632 121 GALGHGLPVAVGLALAakmSGSTKRIYVLTGDGELAEGSnwEAAMAAAKYGLDNLFVIVDKNKLQLAGLTAEIM 194
Cdd:PRK06457 396 GSMGIGVPGSVGASFA---VENKRQVISFVGDGGFTMTM--MELITAKKYDLPVKIIIYNNSKLGMIKFEQEVM 464
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
121-182 |
1.43e-03 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 39.94 E-value: 1.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492120632 121 GALGHGLPVAVGLALAAkmsgSTKRIYVLTGDGElaegSNW--EAAMAAAKYGLDNLFVIVdKN 182
Cdd:PRK07092 407 GGLGYGLPAAVGVALAQ----PGRRVIGLIGDGS----AMYsiQALWSAAQLKLPVTFVIL-NN 461
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
121-179 |
1.66e-03 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 39.23 E-value: 1.66e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 492120632 121 GALGHGLPVAVGLALAAKMSGSTKRIYVLTGDGELAEGSNWEAAMAAAKYGLDNLFVIV 179
Cdd:pfam00676 101 GILGAQVPLGAGIALAAKYRGKKEVAITLYGDGAANQGDFFEGLNFAALWKLPVIFVCE 159
|
|
| |
