|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-624 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 558.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 8 AKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAE 87
Cdd:PRK05899 2 MMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 88 AGL-FPIADLNNLRKIDSDLEGHPTPR-LNFIDVGTGSLGQGVAVGAGMA----YVGKNFDKA-----DYRTYVVVGDGE 156
Cdd:PRK05899 82 AGYdLSIDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGLANAVGMAlaekYLAALFNRPgldivDHYTYVLCGDGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 157 SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLqHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFhCAAITKNK 236
Cdd:PRK05899 162 LMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEG-WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAI-EEAKASTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 237 PTAIIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEVVKHLEGLivnknvkltpkpvpktgaapdvDINNiklssppayklg 316
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLG--AEEIAAAKKEL----------------------GWDY------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 317 dsiatRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDK------LKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFV 390
Cdd:PRK05899 284 -----RKASGKALNALAKALPELVGGSADLAGSNNTKIkgskdfAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 391 STFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA-NTK 469
Cdd:PRK05899 359 GTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 470 GVCFIRTSRPNTCVIYD--NEEPFTIGrGKVVRqkSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAE 547
Cdd:PRK05899 439 GPSALVLTRQNLPVLERtaQEEGVAKG-GYVLR--DDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 548 liiehgkqcggrvvvvEDHYQQGGLGEAVLSALAGE-------RNFV---VKHLYVPTVPRSGPPSVLIDMFGISARHVV 617
Cdd:PRK05899 516 ----------------DAAYKESVLPAAVTARVAVEagvadgwYKYVgldGKVLGIDTFGASAPADELFKEFGFTVENIV 579
|
....*..
gi 45550715 618 NAVNEIL 624
Cdd:PRK05899 580 AAAKELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
19-270 |
1.04e-130 |
|
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: 383.78 E-value: 1.04e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 19 QKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNN 98
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 99 LRKIDSDLEGHPTPRLN-FIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNL 177
Cdd:cd02012 81 FRQLGSRLPGHPEYGLTpGVEVTTGSLGQGLSVAVGMALAEK-LLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 178 CVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLD 257
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|...
gi 45550715 258 NWHGKPLGDKAAE 270
Cdd:cd02012 240 KWHGKPLGEEEVE 252
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
317-624 |
2.83e-107 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 325.89 E-value: 2.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRtvAFVSTFAT 395
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGlALAGKI--PFVSTFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 396 FFT-RAFDQIRM-GAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCF 473
Cdd:COG3958 80 FLTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 474 IRTSRPNTCVIYDNEEPFTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHG 553
Cdd:COG3958 160 LRLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550715 554 KQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVP-TVPRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:COG3958 238 RKT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
15-536 |
2.89e-75 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 253.10 E-value: 2.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 15 KDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPI 93
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 94 ADLNNLRKIDSDLEGHPT-PRLNFIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIW 163
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPEyGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatfnkpgFEIVDHYTYVFVGDGCLQEGISY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 164 ESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIA 242
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTDKPTLIEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 243 KTFKGRDFPNIEDLDNWHGKPLGDkaaEVVKHLeglivNKNVKLTPKP--VPKT------------GAAPDVDINNI--- 305
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGD---EEVALT-----KKNLGWNYNPfeIPQEvydhfkktvkerGAKAEQEWNELfaa 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 306 -KLSSP----------------------PAYKL-GDSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFS----DKLKN 357
Cdd:TIGR00232 312 yKKKYPelaaeftrrlsgelpadwdkqlPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTkwkgSGDLH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 358 LDP-QRYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLE 436
Cdd:TIGR00232 392 ENPlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 437 DIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPNTCVIyDNEEPFTIGRGKVVRQKSSD-EVLLIGAGI 514
Cdd:TIGR00232 472 QLASLRAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQL-EESSLEKVLKGGYVLKDSKGpDLILIATGS 550
|
570 580
....*....|....*....|..
gi 45550715 515 TLYECLAAADQLEKNCITVRVI 536
Cdd:TIGR00232 551 EVQLAVEAAKKLAAENIKVRVV 572
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
317-483 |
3.73e-52 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 176.97 E-value: 3.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQ---RYIECFIAEQNLVGVAVGAACR-RRTVAFVST 392
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHgPLLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 393 FATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKG- 470
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|....
gi 45550715 471 -VCFIRTSRPNTCV 483
Cdd:pfam02779 161 kPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
364-480 |
1.06e-32 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 122.59 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 364 IECFIAEQNLVGVAVGAACRRRtVAFVSTFATFFTRAFDQIRMGAISQtNVNFVGSHCGC-SIGEDGPSQMGLEDIAMFR 442
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGGgGVGEDGPTHHSIEDEALLR 95
|
90 100 110
....*....|....*....|....*....|....*...
gi 45550715 443 TIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPN 480
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKS 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-624 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 558.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 8 AKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAE 87
Cdd:PRK05899 2 MMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 88 AGL-FPIADLNNLRKIDSDLEGHPTPR-LNFIDVGTGSLGQGVAVGAGMA----YVGKNFDKA-----DYRTYVVVGDGE 156
Cdd:PRK05899 82 AGYdLSIDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGLANAVGMAlaekYLAALFNRPgldivDHYTYVLCGDGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 157 SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLqHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFhCAAITKNK 236
Cdd:PRK05899 162 LMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEG-WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAI-EEAKASTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 237 PTAIIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEVVKHLEGLivnknvkltpkpvpktgaapdvDINNiklssppayklg 316
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLG--AEEIAAAKKEL----------------------GWDY------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 317 dsiatRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDK------LKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFV 390
Cdd:PRK05899 284 -----RKASGKALNALAKALPELVGGSADLAGSNNTKIkgskdfAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 391 STFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA-NTK 469
Cdd:PRK05899 359 GTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 470 GVCFIRTSRPNTCVIYD--NEEPFTIGrGKVVRqkSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAE 547
Cdd:PRK05899 439 GPSALVLTRQNLPVLERtaQEEGVAKG-GYVLR--DDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 548 liiehgkqcggrvvvvEDHYQQGGLGEAVLSALAGE-------RNFV---VKHLYVPTVPRSGPPSVLIDMFGISARHVV 617
Cdd:PRK05899 516 ----------------DAAYKESVLPAAVTARVAVEagvadgwYKYVgldGKVLGIDTFGASAPADELFKEFGFTVENIV 579
|
....*..
gi 45550715 618 NAVNEIL 624
Cdd:PRK05899 580 AAAKELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
19-270 |
1.04e-130 |
|
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: 383.78 E-value: 1.04e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 19 QKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNN 98
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 99 LRKIDSDLEGHPTPRLN-FIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNL 177
Cdd:cd02012 81 FRQLGSRLPGHPEYGLTpGVEVTTGSLGQGLSVAVGMALAEK-LLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 178 CVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLD 257
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|...
gi 45550715 258 NWHGKPLGDKAAE 270
Cdd:cd02012 240 KWHGKPLGEEEVE 252
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
317-624 |
2.83e-107 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 325.89 E-value: 2.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRtvAFVSTFAT 395
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGlALAGKI--PFVSTFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 396 FFT-RAFDQIRM-GAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCF 473
Cdd:COG3958 80 FLTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 474 IRTSRPNTCVIYDNEEPFTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHG 553
Cdd:COG3958 160 LRLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550715 554 KQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVP-TVPRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:COG3958 238 RKT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
7-277 |
2.49e-106 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 322.03 E-value: 2.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 7 EAKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWA 86
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 87 EAGLFPIADLNNLRKIDSDLEGHPTP-RLNFIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWES 165
Cdd:COG3959 81 EKGYFPKEELATFRKLGSRLQGHPDMkKTPGVEMSTGSLGQGLSVAVGMALAAK-LDGKDYRVYVLLGDGELQEGQVWEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 166 LHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTF 245
Cdd:COG3959 160 AMAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTV 239
|
250 260 270
....*....|....*....|....*....|...
gi 45550715 246 KGRDFPNIEDLDNWHGKPL-GDKAAEVVKHLEG 277
Cdd:COG3959 240 KGKGVSFMENRPKWHGKAPnDEELEQALAELEA 272
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
15-536 |
2.89e-75 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 253.10 E-value: 2.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 15 KDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPI 93
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 94 ADLNNLRKIDSDLEGHPT-PRLNFIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIW 163
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPEyGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatfnkpgFEIVDHYTYVFVGDGCLQEGISY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 164 ESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIA 242
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTDKPTLIEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 243 KTFKGRDFPNIEDLDNWHGKPLGDkaaEVVKHLeglivNKNVKLTPKP--VPKT------------GAAPDVDINNI--- 305
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGD---EEVALT-----KKNLGWNYNPfeIPQEvydhfkktvkerGAKAEQEWNELfaa 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 306 -KLSSP----------------------PAYKL-GDSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFS----DKLKN 357
Cdd:TIGR00232 312 yKKKYPelaaeftrrlsgelpadwdkqlPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTkwkgSGDLH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 358 LDP-QRYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLE 436
Cdd:TIGR00232 392 ENPlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 437 DIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPNTCVIyDNEEPFTIGRGKVVRQKSSD-EVLLIGAGI 514
Cdd:TIGR00232 472 QLASLRAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQL-EESSLEKVLKGGYVLKDSKGpDLILIATGS 550
|
570 580
....*....|....*....|..
gi 45550715 515 TLYECLAAADQLEKNCITVRVI 536
Cdd:TIGR00232 551 EVQLAVEAAKKLAAENIKVRVV 572
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
324-478 |
2.20e-64 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. 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. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 208.84 E-value: 2.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 324 AYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQ 403
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45550715 404 IR-MGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSR 478
Cdd:cd07033 81 IRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
18-625 |
5.46e-61 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 214.92 E-value: 5.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 18 AQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPIADL 96
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 97 NNLRKIDSDLEGHP----TPRlnfIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIW 163
Cdd:PTZ00089 90 KNFRQLGSRTPGHPerhiTPG---VEVTTGPLGQGIANAVGLAIAEKHlaakfnrpgHPIFDNYVYVICGDGCLQEGVSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 164 ESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRdRLEAFGFNAVVVD--GHDVEELSKAFHCAAITKNKPTAII 241
Cdd:PTZ00089 167 EALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEK-KYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLII 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 242 AKTFKGRDfPNIEDLDNWHGKPLGDKAAEVVKHLEGL--------------IVNKNVKLTPKPVPK--------TGAAPD 299
Cdd:PTZ00089 246 VKTTIGYG-SSKAGTEKVHGAPLGDEDIAQVKELFGLdpekkfhvseevrqFFEQHVEKKKENYEAwkkrfakyTAAFPK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 300 V----------DINNIKLSSPPAYKLGDS-IATRLAYGTALAKIGQNNLRVVALDGD------TKNSTFSDKLKNLDPQR 362
Cdd:PTZ00089 325 EaqaierrfkgELPPGWEKKLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADltpsnlTRPKEANDFTKASPEGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 363 YIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFR 442
Cdd:PTZ00089 405 YIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 443 TIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPNTCVIyDNEEPFTIGRGK--VVRQKSSDEVLLIGAGITLYEC 519
Cdd:PTZ00089 485 ATPNLLVIRPADGTETSGAYALAlANAKTPTILCLSRQNTPPL-PGSSIEGVLKGAyiVVDFTNSPQLILVASGSEVSLC 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 520 LAAADQLEKNcITVRVID-P----FTVKPLDaeliiehgkqcggrvvvvedhYQQGGL---GEAVLSALAGERNFVVK-- 589
Cdd:PTZ00089 564 VEAAKALSKE-LNVRVVSmPcwelFDQQSEE---------------------YQQSVLpsgGVPVLSVEAYVSFGWEKys 621
|
650 660 670
....*....|....*....|....*....|....*...
gi 45550715 590 HLYV--PTVPRSGPPSVLIDMFGISARHVVNAVNEILK 625
Cdd:PTZ00089 622 HVHVgiSGFGASAPANALYKHFGFTVENVVEKARALAA 659
|
|
| PLN02790 |
PLN02790 |
transketolase |
22-624 |
5.08e-59 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 209.11 E-value: 5.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 22 RIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL--FPIADLNNL 99
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 100 RKIDSDLEGHPTprlNF----IDVGTGSLGQGVAVGAGMAYVGKN----FDKADY-----RTYVVVGDGESAEGSIWESL 166
Cdd:PLN02790 82 RQWGSRTPGHPE---NFetpgIEVTTGPLGQGIANAVGLALAEKHlaarFNKPDHkivdhYTYCILGDGCQMEGISNEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 167 HFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRdRLEAFGFNAVVVDG--HDVEELSKAFHCAAITKNKPTAIIAKT 244
Cdd:PLN02790 159 SLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDK-RYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 245 FKGRDFPNIEDLDNWHGKPLGDKAAEVVK-----HLEGLIVNKNVKLTPKPVPKTGAAPDVDIN---------------N 304
Cdd:PLN02790 238 TIGYGSPNKANSYSVHGAALGEKEVDATRknlgwPYEPFHVPEDVKSHWSKHTKEGAALEAEWNakfaeykkkypeeaaE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 305 IK-----------LSSPPAYKLGDSI-ATRLAYGT---ALAK-----IG------QNNLRVVALDGDTKNSTFSdklknl 358
Cdd:PLN02790 318 LKslisgelpsgwEKALPTFTPEDPAdATRNLSQKclnALAKvlpglIGgsadlaSSNMTLLKDFGDFQKDTPE------ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 359 dpQRYIECFIAEQNLVGVAVGAACRRRT-VAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLED 437
Cdd:PLN02790 392 --ERNVRFGVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 438 IAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKG---VCFIRTSRPNTCVIYDNEepftIGRGK-VVRQKSSD---EVLL 509
Cdd:PLN02790 470 LASLRAMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPNLPGTSIEG----VEKGGyVISDNSSGnkpDLIL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 510 IGAGITLYECLAAADQLEKNCITVRVidpftVKPLDAELIIEHgkqcggrvvvvEDHYQQGGLGEAVLSALA-------G 582
Cdd:PLN02790 546 IGTGSELEIAAKAAKELRKEGKKVRV-----VSMVCWELFEEQ-----------SDEYKESVLPSSVTARVSveagstfG 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 45550715 583 ERNFVV---KHLYVPTVPRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:PLN02790 610 WEKYVGskgKVIGVDRFGASAPAGILYKEFGFTVENVVAAAKSLL 654
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
12-536 |
3.55e-56 |
|
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: 201.39 E-value: 3.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 12 QDLKDLAQKLRIHSINATQASKSGHP---TSCASIAEimsVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEA 88
Cdd:COG0021 2 PLDQLAANAIRALAMDAVQKANSGHPglpMGMAPIAY---VLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 89 GL-FPIADLNNLRKIDSDLEGHP----TPrlnFIDVGTGSLGQGVAVGAGMAYVGK----NFDKA-----DYRTYVVVGD 154
Cdd:COG0021 79 GYdLSLDDLKNFRQLGSKTPGHPeyghTP---GVETTTGPLGQGIANAVGMAIAERhlaaRFNRPghdivDHYTYVIAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 155 GESAEGSIWESLHFAGHYKLDNLCVIFDVNR--------LGQSEatslqhklDVyRDRLEAFGFNAV-VVDGHDVEELSK 225
Cdd:COG0021 156 GDLMEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdLAFSE--------DV-AKRFEAYGWHVIrVEDGHDLEAIDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 226 AFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGDKAAEVVKhleglivnKNVKLTPKP--VP----------- 292
Cdd:COG0021 227 AIEAAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATK--------EALGWPPEPfeVPdevyahwraag 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 293 KTGAA----------------PD-----VDINNIKL-----SSPPAYKLGD-SIATRLAYGTALAKIGQN--NLrVVA-- 341
Cdd:COG0021 299 ERGAAaeaewnerfaayaaayPElaaelERRLAGELpedwdAALPAFEADAkGVATRKASGKVLNALAPVlpEL-IGGsa 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 342 -LDGDTKnsTFSDKLKNLDPQ----RYIECFIAEQnlvgvAVGAAC-----RRRTVAFVSTFATF--FTRAfdQIRMGAI 409
Cdd:COG0021 378 dLAGSNK--TTIKGAGSFSPEdpsgRNIHFGVREH-----AMGAIMngialHGGLRPYGGTFLVFsdYMRP--AIRLAAL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 410 SQTNVNFVGSHcgCSI--GEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKG-VCFIrTSRPNTCVIY 485
Cdd:COG0021 449 MKLPVIYVFTH--DSIglGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLAlERKDGpTALI-LSRQNLPTLD 525
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 45550715 486 DNEEPFT-IGRGKVVRQKSSD--EVLLIGAG--ITLyeCLAAADQLEKNCITVRVI 536
Cdd:COG0021 526 RTAAAAEgVAKGAYVLADAEGtpDVILIATGseVSL--AVEAAELLAAEGIKVRVV 579
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
123-624 |
1.40e-54 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 195.30 E-value: 1.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 123 SLGQGVAVGAGMAyvgknfDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVIFDVNRLGQSEAT-SLQHKLDvy 201
Cdd:PRK05444 124 SAALGMAKARDLK------GGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDNEMSISPNVgALSNYLA-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 202 rdRL------EAFGFNAV-VVDGHDVEELSKAFHcAAITKNKPTAIIAKTFKGRDFPNIE-DLDNWHGkplgdkaaevvk 273
Cdd:PRK05444 195 --RLrsstlfEELGFNYIgPIDGHDLDALIETLK-NAKDLKGPVLLHVVTKKGKGYAPAEaDPIKYHG------------ 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 274 hleglivnknvklTPKPVPKTGAAPdvdinniKLSSPPAYKLGDsiatrlAYGTALAKIGQNNLRVVAL-----DGdTKN 348
Cdd:PRK05444 260 -------------VGKFDPETGEQP-------KSSKPGKPSYTK------VFGETLCELAEKDPKIVAItaampEG-TGL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 349 STFSDKLknldPQRYIECFIAEQNLVGVAVGAACRRRTVaFVSTFATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSiGE 427
Cdd:PRK05444 313 VKFSKRF----PDRYFDVGIAEQHAVTFAAGLATEGLKP-VVAIYSTFLQRAYDQVIHDvALQNLPVTFAIDRAGLV-GA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 428 DGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPN-TCVIYDNEEPFTIGRGKVVRQksSD 505
Cdd:PRK05444 387 DGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRGNgVGVELPELEPLPIGKGEVLRE--GE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 506 EVLLIGAGITLYECLAAADQLEKncitVRVIDPFTVKPLDAELIIEHGKQcGGRVVVVEDHYQQGGLGEAVLSALAGERN 585
Cdd:PRK05444 465 DVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAK-HDLVVTVEEGAIMGGFGSAVLEFLADHGL 539
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 45550715 586 FV-VKHLYVPT--VPRsGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:PRK05444 540 DVpVLNLGLPDefIDH-GSREELLAELGLDAEGIARRILELL 580
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
317-483 |
3.73e-52 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 176.97 E-value: 3.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQ---RYIECFIAEQNLVGVAVGAACR-RRTVAFVST 392
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHgPLLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 393 FATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKG- 470
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|....
gi 45550715 471 -VCFIRTSRPNTCV 483
Cdd:pfam02779 161 kPVVLRLPRQLLRP 174
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
206-625 |
1.93e-50 |
|
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: 184.83 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 206 EAFGFNAV-VVDGHDVEELSKAFHcAAITKNKPTAIIAKTFKGRDF-PNIEDLDNWHGkplgdkaaevvkhlegliVNKN 283
Cdd:COG1154 242 EELGFKYIgPIDGHDLDALVETLR-NAKDLKGPVLLHVVTKKGKGYaPAEKDPDKFHG------------------VGPF 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 284 VKLTPKPVPKTgaapdvdinniklSSPPAYklgdsiaTRlAYGTALAKIGQNNLRVVA-----LDGdTKNSTFSDKLknl 358
Cdd:COG1154 303 DPETGEPKKSK-------------SSAPSY-------TD-VFGDTLVELAEKDPRIVAitaamPEG-TGLDKFAERF--- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 359 dPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQIRMG-AISQTNVNFVgshcgcsI------GEDGPS 431
Cdd:COG1154 358 -PDRFFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHDvALQNLPVTFA-------IdraglvGADGPT 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 432 QMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPNTC-VIYDNE-EPFTIGRGKVVRQksSDEVLL 509
Cdd:COG1154 429 HHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGPgVELPAElEPLPIGKGEVLRE--GKDVAI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 510 IGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFV-V 588
Cdd:COG1154 507 LAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREH-DLVVTVEEGVLAGGFGSAVLEFLADAGLDVpV 585
|
410 420 430
....*....|....*....|....*....|....*....
gi 45550715 589 KHLYVPT--VPRsGPPSVLIDMFGISARHVVNAVNEILK 625
Cdd:COG1154 586 LRLGLPDrfIEH-GSRAELLAELGLDAEGIARAILELLG 623
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
15-271 |
4.84e-49 |
|
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: 174.11 E-value: 4.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 15 KDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPI 93
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 94 ADLNNLRKIDSDLEGHP----TPRlnfIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEG 160
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPefghTAG---VEVTTGPLGQGIANAVGMAIAERNlaatynrpgFDIVDHYTYVFLGDGCLMEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 161 SIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTA 239
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDT-AARFEAYGWHVIeVEDGHDVEAIAAAIEEAKAEKDKPTL 238
|
250 260 270
....*....|....*....|....*....|..
gi 45550715 240 IIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEV 271
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAPLG--ADEV 268
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
496-616 |
1.61e-37 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 135.42 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 496 GKVVRQKSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEhGKQCGGRVVVVEDHYQQGGLGEA 575
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILE-SVKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 45550715 576 VLSALAGE----RNFVVKHLYVPTVPRSGPPSVLIDMFGISARHV 616
Cdd:pfam02780 80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
124-625 |
6.70e-34 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 137.16 E-value: 6.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 124 LGQGvAVGAGMAYVG-KNFDKADYRTYVVVGDGE-------SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQ 195
Cdd:PRK12571 148 IGDG-SLTAGMAYEAlNNAGAADRRLIVILNDNEmsiappvGALAAYLSTLRSSDPFARLRAIAKGVEERLPGPLRDGAR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 196 HKLDVYRDR------LEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIE-DLDNWHGkplgdk 267
Cdd:PRK12571 227 RARELVTGMigggtlFEELGFTYVgPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEaDEDKYHA------ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 268 aaevvkhlegliVNKNVKLTPKPvpkTGAAPdvdinniklsSPPAYklgdsiaTRLaYGTALAKIGQNNLRVVALDGDTK 347
Cdd:PRK12571 301 ------------VGKFDVVTGLQ---KKSAP----------SAPSY-------TSV-FGEELTKEAAEDSDIVAITAAMP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 348 NSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQIRMG-AISQTNVNFVGSHCGCsIG 426
Cdd:PRK12571 348 LGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLHDvALQNLPVRFVLDRAGL-VG 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 427 EDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAV-ELAANTKGVCFIRTSRPNTC--VIYDNEEPFTIGRGKVVRQKS 503
Cdd:PRK12571 426 ADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEGVgvEIPAEGTILGIGKGRVPREGP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 504 sdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELI---IEHGKqcggrVVVVEDHYQQGGLGEAVLSAL 580
Cdd:PRK12571 506 --DVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTdllVRHHI-----VVIVEEQGAMGGFGAHVLHHL 578
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 45550715 581 A--GERNFVVKhLYVPTVPR-----SGPPSVLIDMfGISARHVVNAVNEILK 625
Cdd:PRK12571 579 AdtGLLDGGLK-LRTLGLPDrfidhASREEMYAEA-GLTAPDIAAAVTGALA 628
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
364-480 |
1.06e-32 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 122.59 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 364 IECFIAEQNLVGVAVGAACRRRtVAFVSTFATFFTRAFDQIRMGAISQtNVNFVGSHCGC-SIGEDGPSQMGLEDIAMFR 442
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGGgGVGEDGPTHHSIEDEALLR 95
|
90 100 110
....*....|....*....|....*....|....*...
gi 45550715 443 TIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPN 480
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKS 133
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
368-625 |
1.12e-24 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 105.10 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 368 IAEQNLVGVAVGAACR-RRTVAFVsTFATFFTRAFDQI-----RMGAIS--QTNVNFV-----GSHcgcsIGEdGP--SQ 432
Cdd:COG0022 58 ISEAGIVGAAIGAALAgLRPVVEI-QFADFIYPAFDQIvnqaaKLRYMSggQFKVPMVirtpyGGG----IGA-GAqhSQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 433 MgLEdiAMFRTIPGSTIFYPSDAvstERAVEL--AAntkgvcfIRTSRPntcVIY--------------DNEEPFTIGRG 496
Cdd:COG0022 132 S-LE--AWFAHIPGLKVVAPSTP---YDAKGLlkAA-------IRDDDP---VIFlehkrlyrlkgevpEEDYTVPLGKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 497 KVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGEAV 576
Cdd:COG0022 196 RVVRE--GTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEI 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45550715 577 LSALAgERNFvvKHLYVPTVPRSGP------PSVLIDMFGISARHVVNAVNEILK 625
Cdd:COG0022 273 AARIA-EEAF--DYLDAPVKRVTGPdtpipyAPALEKAYLPSADRIVAAVRELLA 324
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
22-247 |
4.14e-24 |
|
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: 104.69 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 22 RIHSI---NATQ----ASK-----SGHPTSCASIAEIMSVLFFQQLRlnlKHPRDPSSDRfILSKGHAAPILYA-AWAEa 88
Cdd:cd02017 6 RIRSLirwNAMAmvhrANKkdlgiGGHIATFASAATLYEVGFNHFFR---ARGEGGGGDL-VYFQGHASPGIYArAFLE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 89 GLFPIADLNNLRKIDSD--LEGHPTPRL--NFIDVGTGSLGQGVAVGAGMA----YV---GKNfDKADYRTYVVVGDGES 157
Cdd:cd02017 81 GRLTEEQLDNFRQEVGGggLSSYPHPWLmpDFWEFPTVSMGLGPIQAIYQArfnrYLedrGLK-DTSDQKVWAFLGDGEM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 158 AEGSIWESLHFAGHYKLDNLCVIFDVNR-------------LGQSEAT--------------SLQHKL------DVYRDR 204
Cdd:cd02017 160 DEPESLGAIGLAAREKLDNLIFVVNCNLqrldgpvrgngkiIQELEGIfrgagwnvikviwgSKWDELlakdggGALRQR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 205 LEA---------------------FG----FNAVVVD------------GHDVEELSKAFHCAAITKNKPTAIIAKTFKG 247
Cdd:cd02017 240 MEEtvdgdyqtlkakdgayvrehfFGkypeLKALVTDlsdedlwalnrgGHDPRKVYAAYKKAVEHKGKPTVILAKTIKG 319
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
120-581 |
8.52e-24 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 106.34 E-value: 8.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 120 GTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEA-------- 191
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTAnldgptqp 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 192 --------TSLQHKLDVYRDR----LEAFGFNAV-VVDGHDVEELSKAFHCAAITKN-KPTAIIAKTFKGRDFPNIEDLD 257
Cdd:PLN02234 254 vgalscalSRLQSNCGMIRETsstlFEELGFHYVgPVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERAD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 258 nwhgkplgDKAAEVVKHleglivnknvkltpkpVPKTGAapdvDINNIklSSPPAYKLgdsiatrlAYGTALAKIGQNNL 337
Cdd:PLN02234 334 --------DKYHGVLKF----------------DPETGK----QFKNI--SKTQSYTS--------CFVEALIAEAEADK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 338 RVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGA-ISQTNVNF 416
Cdd:PLN02234 376 DIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQVVHDVdLQKLPVRF 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 417 VGSHCGCsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVCFiRTSRPNTCVIY----DNEEP 490
Cdd:PLN02234 455 AIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSlppgNKGVP 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 491 FTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQG 570
Cdd:PLN02234 533 LQIGRGRILRD--GERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKS--HEVLITVEEGSIG 608
|
490
....*....|.
gi 45550715 571 GLGEAVLSALA 581
Cdd:PLN02234 609 GFGSHVVQFLA 619
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
10-624 |
2.12e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 92.27 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 10 TVQDLKDLAQKLR---IHSINATqaskSGHPTSCASIAEimsvlffqqLRLNLKHPRDPSSDRFILSKGHAA---PILYA 83
Cdd:PLN02582 47 SVKELKQLADELRsdvIFNVSKT----GGHLGSSLGVVE---------LTVALHYVFNAPQDKILWDVGHQSyphKILTG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 84 AWAEaglfpiadLNNLRKIDSdLEGHPTPRLNFID-VGTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSI 162
Cdd:PLN02582 114 RRDK--------MHTMRQTNG-LSGFTKRAESEYDcFGTGHSSTTISAGLGMA-VGRDLKGKKNNVVAVIGDGAMTAGQA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 163 WESLHFAGHYKLDNLCVIFDVNRLGQSEAT-------------------------------------------SLQHKLD 199
Cdd:PLN02582 184 YEAMNNAGYLDSDMIVILNDNKQVSLPTATldgpappvgalssalsrlqssrplrelrevakgvtkqiggpmhELAAKVD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 200 VYRDRL---------EAFGFNAV-VVDGHDVEELSKAFHCAAITKNK-PTAIIAKTFKGRDFPNIEDL-DNWHGkplgdk 267
Cdd:PLN02582 264 EYARGMisgsgstlfEELGLYYIgPVDGHNIDDLVTILREVKSTKTTgPVLIHVVTEKGRGYPYAERAaDKYHG------ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 268 aaeVVKHleglivnknvkltpkpVPKTGaapdvdinniklssppayKLGDSIATRLAYGT----ALAKIGQNNLRVVALD 343
Cdd:PLN02582 338 ---VVKF----------------DPATG------------------KQFKVKAKTQSYTTyfaeALIAEAEVDKDVVAIH 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 344 GDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGA-ISQTNVNFVGSHCG 422
Cdd:PLN02582 381 AAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQVVHDVdLQKLPVRFAMDRAG 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 423 CsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVCFiRTSRPNTCVIYDNEE----PFTIGRG 496
Cdd:PLN02582 460 L-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNnkgiPIEVGKG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 497 KVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQGGLGEAV 576
Cdd:PLN02582 538 RILLE--GERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKS--HEVLITVEEGSIGGFGSHV 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 45550715 577 LSALAGE---------RNFVVKHLYVptvpRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:PLN02582 614 AQFMALDglldgklkwRPLVLPDRYI----DHGAPADQLAEAGLTPSHIAATVLNVL 666
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
360-624 |
2.31e-19 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 90.04 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 360 PQRYIECFIAEQNLVGVAVGAACR-RRTVAFVsTFATFFTRAFDQIrmgaisqtnVNFV-------GSHCGCSIGEDGPS 431
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNgLRPIAEF-MFADFIFPAFDQI---------VNEAakyrymsGGQFDCPIVIRGPN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 432 ----QMGLEDI----AMFRTIPGSTIFYPSDAVSTeRAVELAAntkgvcfIRTsrPNTCVIYDNE------------EPF 491
Cdd:PTZ00182 151 gavgHGGAYHSqsfeAYFAHVPGLKVVAPSDPEDA-KGLLKAA-------IRD--PNPVVFFEPKllyresvevvpeADY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 492 T--IGRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQ 569
Cdd:PTZ00182 221 TlpLGKAKVVREGK--DVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPT 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45550715 570 GGLGeAVLSALAGERNFvvKHLYVPTVPRSG-----PPSVLIDMFGI-SARHVVNAVNEIL 624
Cdd:PTZ00182 298 CGIG-AEIAAQIMEDCF--LYLEAPIKRVCGadtpfPYAKNLEPAYLpDKEKVVEAAKRVL 355
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
355-586 |
4.80e-17 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 82.46 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 355 LKNLDPQRYIECFIAEQNLVGVAVGAA-CRRRTVAFVSTFaTFFTRAFDQIRMGAiSQTNVnFVGSHCGCSIGEDGP--- 430
Cdd:PRK09212 45 LEQFGPKRVIDTPITEHGFAGLAVGAAfAGLRPIVEFMTF-NFSMQAIDQIVNSA-AKTNY-MSGGQLKCPIVFRGPnga 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 431 -----SQMGLEDIAMFRTIPGSTIFYPSdavsteraveLAANTKGVCFIRTSRPNTCVIYDNE-------------EPFT 492
Cdd:PRK09212 122 aarvaAQHSQCYAAWYSHIPGLKVVAPY----------FAADCKGLLKTAIRDPNPVIFLENEilyghshevpeeeESIP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 493 IGRGKVVRQKSSdeVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGL 572
Cdd:PRK09212 192 IGKAAILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGV 268
|
250
....*....|....
gi 45550715 573 GeAVLSALAGERNF 586
Cdd:PRK09212 269 G-AEIAALIMKEAF 281
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
104-625 |
1.32e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 83.13 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 104 SDLEGHPTPRLN---FIDVGTGSlgQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVI 180
Cdd:PRK12315 94 DDVTGYTNPEESehdFFTVGHTS--TSIALATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIII 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 181 FDVNRLGQSEATS-LQHKLDVYRDR--------LEAFGFNAVVV-DGHDVEELSKAFHCAAITkNKPTAIIAKTFKGRDF 250
Cdd:PRK12315 170 VNDNQMSIAENHGgLYKNLKELRDTngqsennlFKAMGLDYRYVeDGNDIESLIEAFKEVKDI-DHPIVLHIHTLKGKGY 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 251 -PNIEDLDNWH-GKPLgdkaaevvkHLEglivnknvklTPKP-VPKTGAapdvDINNIKLSSppaykLGDSIAtrlaygt 327
Cdd:PRK12315 249 qPAEENKEAFHwHMPF---------DLE----------TGQSkVPASGE----SYSSVTLDY-----LLKKIK------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 328 alakigqNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRTVAFVstFATFFTRAFDQIRM 406
Cdd:PRK12315 294 -------EGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGiAANGARPVIFV--NSTFLQRAYDQLSH 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 407 G-AISQTNVNFVGShcGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAAN-TKGVCFIRTsrPNTCVI 484
Cdd:PRK12315 365 DlAINNNPAVMIVF--GGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTqHEHPVAIRV--PEHGVE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 485 YDNEEP--FTIGRGKVVRQKSsdEVLLIGAGiTLYEC-LAAADQL-EKNCITVRVIDPFTVKPLDAELiIEHGKQCGGRV 560
Cdd:PRK12315 441 SGPTVDtdYSTLKYEVTKAGE--KVAILALG-DFYELgEKVAKKLkEELGIDATLINPKFITGLDEEL-LEKLKEDHELV 516
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45550715 561 VVVEDHYQQGGLGEAVLSALAGER----NFVVKHLYVPTVprsgPPSVLIDMFGISARHVVNAVNEILK 625
Cdd:PRK12315 517 VTLEDGILDGGFGEKIARYYGNSDmkvlNYGAKKEFNDRV----PVEELYKRNHLTPEQIVEDILSVLK 581
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
120-245 |
1.86e-15 |
|
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: 77.15 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 120 GTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDvNRLGQSEATSLQHKLD 199
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALK-YRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPTSRQTAGT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45550715 200 VYRDRLEAFGFNAVVVDGHDVEELSKAFHCA---AITKNKPTAIIAKTF 245
Cdd:cd02000 180 SIADRAAAYGIPGIRVDGNDVLAVYEAAKEAverARAGGGPTLIEAVTY 228
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
360-586 |
2.97e-14 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 75.34 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 360 PQRYIECFIAEQNLVGVAVGAACR--RRTVAFVsTFaTFFTRAFDQIRMGAiSQTNVnFVGSHCGCSIGEDGPS------ 431
Cdd:PRK11892 188 ARRVIDTPITEHGFAGIGVGAAFAglKPIVEFM-TF-NFAMQAIDQIINSA-AKTLY-MSGGQMGCPIVFRGPNgaaarv 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 432 --QMGLEDIAMFRTIPGSTIFYPSDAvsteravelaANTKGV--CFIRTsrPNTCVIYDNE------------EPFT--I 493
Cdd:PRK11892 264 aaQHSQDYAAWYSHIPGLKVVAPYSA----------ADAKGLlkAAIRD--PNPVIFLENEilygqsfdvpklDDFVlpI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 494 GRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLG 573
Cdd:PRK11892 332 GKARIHREGK--DVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVG 408
|
250
....*....|...
gi 45550715 574 eAVLSALAGERNF 586
Cdd:PRK11892 409 -AEIAARVMEQAF 420
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
341-616 |
3.83e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 72.44 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 341 ALDGDTKNSTFSDKLknldPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGAISQTN-VNFVGS 419
Cdd:PLN02225 407 GMEMDASLITFQERF----PDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVIT 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 420 HCGCsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVC--FIRTSRPNTCVIYDNEEPFTIGR 495
Cdd:PLN02225 482 SAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEIGR 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 496 GKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQGGLGEA 575
Cdd:PLN02225 561 GRVLVE--GQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQN--HKFLITVEEGCVGGFGSH 636
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 45550715 576 VLS--ALAGERNFVVKhlYVPTVPRSG-----PPSVLIDMFGISARHV 616
Cdd:PLN02225 637 VAQfiALDGQLDGNIK--WRPIVLPDGyieeaSPREQLALAGLTGHHI 682
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
108-246 |
9.78e-11 |
|
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: 63.11 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 108 GHPTPRLNFIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAghyKLDNLCVIFDV--NR 185
Cdd:pfam00676 87 GYYGAKGNRFYGGNGILGAQVPLGAGIALAAK-YRGKKEVAITLYGDGAANQGDFFEGLNFA---ALWKLPVIFVCenNQ 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45550715 186 LGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCA---AITKNKPTAIIAKTFK 246
Cdd:pfam00676 163 YGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAaerARTGKGPFLIELVTYR 226
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
120-250 |
1.71e-10 |
|
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: 60.64 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 120 GTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVIFDVNRLGQSEATSLQHKLd 199
Cdd:cd02007 73 GTGHSSTSISAALGMA-VARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSISPNVGTPGNL- 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 45550715 200 vyrdrLEAFGFNAV-VVDGHDVEELSKAFHCAAITKnKPTAIIAKTFKGRDF 250
Cdd:cd02007 150 -----FEELGFRYIgPVDGHNIEALIKVLKEVKDLK-GPVLLHVVTKKGKGY 195
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
355-586 |
1.82e-09 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 59.83 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 355 LKNLDPQRYIECFIAEQNLVGVAVGAACR--RRTVAFVsTFaTFFTRAFDQIRMGAISQTNVNfvGSHCGCSIGEDGP-- 430
Cdd:PLN02683 68 LQKYGPDRVLDTPITEAGFTGIGVGAAYAglKPVVEFM-TF-NFSMQAIDHIINSAAKTNYMS--AGQISVPIVFRGPng 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 431 ------SQMGLEDIAMFRTIPGSTIFYPSDAvSTERAVELAAntkgvcfIRTsrPNTCVIYDNE----EPFT-------- 492
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYSS-EDARGLLKAA-------IRD--PDPVVFLENEllygESFPvsaevlds 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 493 -----IGRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHY 567
Cdd:PLN02683 214 sfvlpIGKAKIEREGK--DVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|....*....
gi 45550715 568 QQGGLGeAVLSALAGERNF 586
Cdd:PLN02683 291 PQHGVG-AEICASVVEESF 308
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
116-244 |
3.92e-08 |
|
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: 53.03 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 116 FIDVGTGSLGQGV--AVGAGMAYvgknfdkADYRTYVVVGDGESAEGsiWESLHFAGHYKLDNLCVIFD----------- 182
Cdd:cd00568 40 LTSTGFGAMGYGLpaAIGAALAA-------PDRPVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNnggygtirmhq 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550715 183 VNRLGQSEATSLQHKLDvYRDRLEAFGFNAVVVDghDVEELSKAFHcAAITKNKPTAIIAKT 244
Cdd:cd00568 111 EAFYGGRVSGTDLSNPD-FAALAEAYGAKGVRVE--DPEDLEAALA-EALAAGGPALIEVKT 168
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
22-247 |
1.57e-06 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 51.30 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 22 RIHSI---NA----TQASKS-----GHPTSCASIAEIMSVLF--FQQLRlNLKHPRDpssdrFILSKGHAAPILYA-AWA 86
Cdd:PRK09405 83 RIRSYirwNAaamvLRANKKdlglgGHISSFASSATLYEVGFnhFFRAP-NEPHGGD-----LVFFQGHASPGIYArAFL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 87 EaGLFPIADLNNLRK-IDSD-LEGHPTPRL--NFIDVGTGSLGQGvAVGA-------------GMAyvgknfDKADYRTY 149
Cdd:PRK09405 157 E-GRLTEEQLDNFRQeVDGKgLSSYPHPWLmpDFWQFPTVSMGLG-PIMAiyqarflkylenrGLK------DTSDQKVW 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 150 VVVGDGESAEGsiwESL---HFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRLEAF----GFNAV- 213
Cdd:PRK09405 229 AFLGDGEMDEP---ESLgaiSLAAREKLDNL--IFVIN-------CNLQ-RLDgpV-RgngkiiQELEGIfrgaGWNVIk 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 214 -------------------------VVDG-------------------------------------------HDVEELSK 225
Cdd:PRK09405 295 viwgsrwdpllakdtsgklvqlmneTVDGdyqtykakdgayvrehffgkypetkalvadmsdddiwalnrggHDPRKVYA 374
|
330 340
....*....|....*....|..
gi 45550715 226 AFHCAAITKNKPTAIIAKTFKG 247
Cdd:PRK09405 375 AYKAAVEHKGQPTVILAKTIKG 396
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
16-247 |
1.64e-06 |
|
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: 51.23 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 16 DLAQKLRIHSI---NA----TQASKS-----GHPTSCASIAEIMSVLF--FQQLRlNLKHPRDpssdrFILSKGHAAPIL 81
Cdd:COG2609 78 DEELERRIRSIirwNAmamvVRANRKggglgGHISSFASAATLYEVGFnhFFRGP-DHPGGGD-----LVYFQGHASPGI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 82 YA-AWAEaGLFPIADLNNLRKidsDLEGH-----PTPRL--NFIDVGTGSLGQGvAVGA-------------GMAyvgkn 140
Cdd:COG2609 152 YArAFLE-GRLTEEQLDNFRQ---EVDGKglssyPHPWLmpDFWQFPTVSMGLG-PINAiyqarfmkylhnrGLK----- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 141 fDKADYRTYVVVGDGESAEGsiwESL---HFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRLEAF- 208
Cdd:COG2609 222 -DTSDRKVWAFLGDGEMDEP---ESLgaiSLAAREKLDNL--IFVIN-------CNLQ-RLDgpV-RgngkiiQELEGVf 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 209 ---GFNAV--------------------------VVDG------------------------------------------ 217
Cdd:COG2609 287 rgaGWNVIkviwgsewdpllakdtdgalvkrmneTVDGdyqtykakdgayvrehffgkypelkalvadmsdediwrlnrg 366
|
330 340 350
....*....|....*....|....*....|.
gi 45550715 218 -HDVEELSKAFHCAAITKNKPTAIIAKTFKG 247
Cdd:COG2609 367 gHDPRKVYAAYKAAVEHKGQPTVILAKTIKG 397
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
16-247 |
3.03e-06 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 50.32 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 16 DLAQKLRIHSI---NA----TQASKS-----GHPTSCASIAEIMSV---LFFqqlrlnlKHPRDPSSDRFILSKGHAAPI 80
Cdd:PRK13012 85 DLALEERLAAIirwNAlamvVRANRAygelgGHIASYASAADLFEVgfnHFF-------RGRDDAGGGDLVYFQPHSAPG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 81 LYA-AWAEaGLFPIADLNNLRK-IDSD-LEGHPTPRL--NFIDVGTGSLGQGVAVGA----GMAYVGKN--FDKADYRTY 149
Cdd:PRK13012 158 IYArAFLE-GRLSEEQLDHFRQeIGGPgLSSYPHPWLmpDFWQFPTGSMGIGPINAIyqarFMRYLQHRglKDTSGRKVW 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 150 VVVGDGESAEGSIWESLHFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRLEAF----GFN------ 211
Cdd:PRK13012 237 GFFGDGEMDEPESIAALSLAAREGLDNL--VFVIN-------CNLQ-RLDgpV-RgngriiQELEALfrgaGWNvikvlw 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 212 --------------------AVVVD-------------------------------------------GHDVEELSKAFH 228
Cdd:PRK13012 306 gsdwdalfardttgalvrrfAETVDgqfqtfkandgaynrehffgqdpelaalvahlsdedidrlkrgGHDPRKVYAAYA 385
|
330
....*....|....*....
gi 45550715 229 CAAITKNKPTAIIAKTFKG 247
Cdd:PRK13012 386 AAVRHKGQPTVILAKTKKG 404
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
346-455 |
4.18e-06 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 46.95 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 346 TKNSTFSDKLKNLDPQRYIECfIAEQNLVGVAVGAA-CRRRTVAFVsTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCS 424
Cdd:cd06586 21 DEISSLLDALREGDKRIIDTV-IHELGAAGAAAGYArAGGPPVVIV-TSGTGLLNAINGLADAAAEHLPVVFLIGARGIS 98
|
90 100 110
....*....|....*....|....*....|.
gi 45550715 425 iGEDGPSQMGLEDIAMFRTIPGSTIFYPSDA 455
Cdd:cd06586 99 -AQAKQTFQSMFDLGMYRSIPEANISSPSPA 128
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
362-625 |
1.06e-05 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 47.81 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 362 RYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQI--RMGAISQTNvnfvGSHCGCSIGEDGPS----QMGL 435
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLGA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 436 EDI----AMFRTIPGSTIFypsdAVSTeravelAANTKGV--CFIRTSRPntcVIY--------------DNEEPFTIGR 495
Cdd:CHL00144 128 EHSqrleSYFQSVPGLQIV----ACST------PYNAKGLlkSAIRSNNP---VIFfehvllynlkeeipDNEYLLPLEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 496 GKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGeA 575
Cdd:CHL00144 195 AEVVRPGN--DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKT-HKVLIVEECMKTGGIG-A 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45550715 576 VLSALagernfVVKHLY--------------VPTvPRSGPpsvLIDMFGISARHVVNAVNEILK 625
Cdd:CHL00144 271 ELIAQ------INEHLFdeldapivrlssqdVPT-PYNGP---LEEATVIQPAQIIEAVEQIIT 324
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
120-248 |
1.99e-03 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 41.08 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45550715 120 GTGSLGQGVAVGAGMAYVGK------NFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDnlcVIFDV-NRL---GQS 189
Cdd:PLN02374 192 GFAFIGEGIPVATGAAFSSKyrrevlKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLP---IVFVVeNNLwaiGMS 268
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550715 190 EATSLQHKlDVYRdRLEAFGFNAVVVDGHD---VEELSKAFHCAAITKNKPTAIIAKTFKGR 248
Cdd:PLN02374 269 HLRATSDP-EIWK-KGPAFGMPGVHVDGMDvlkVREVAKEAIERARRGEGPTLVECETYRFR 328
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
120-181 |
3.21e-03 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 40.08 E-value: 3.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45550715 120 GTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGhykLDNLCVIF 181
Cdd:PLN02269 136 GHGIVGAQVPLGAGLAFAQK-YNKEENVAFALYGDGAANQGQLFEALNIAA---LWDLPVIF 193
|
|
| |
