|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-620 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 572.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 88 EAGF-LPEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCMLGDG 156
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 157 EVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDiYQKRCEAFGWHTIIVDGHSVEELCKAFGQAKH--Q 234
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 235 PTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQiiqeiysqvqsKKKILATPPqedapsvdianirmptppsykvgdk 314
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 315 iatRKAYGLALAKLGHASDRIIALDGDTKNSTFSELF------KKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCST 388
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 389 FAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA-NTKGI 467
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 468 CFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKlild 547
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 548 saratkgriltvEDHYYEGGIGEAVSAAVVGEPGVT----------VTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVK 617
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 6678359 618 GLV 620
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-271 |
2.62e-134 |
|
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: 393.02 E-value: 2.62e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLN 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 100 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNL 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 179 VAIFDINRLGQSDPAPLQHQVDIYQKRCEAFGWHTIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGITGIEDKE 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 6678359 256 AWHGKPLPKNMAEQII 271
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
313-620 |
7.95e-117 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 350.16 E-value: 7.95e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 313 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAF 392
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 393 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFI 470
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 471 RTSRPENAIIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSAR 550
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678359 551 ATkGRILTVEDHYYEGGIGEAVSAAVVGEPGVTVTRLAVSQVP-RSGKPAELLKMFGIDKDAIVQAVKGLV 620
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-619 |
1.20e-77 |
|
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: 259.65 E-value: 1.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRykaLDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLK---FNPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 92 LPEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCMLGDGEVSEG 161
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 162 SVWEAMAFAGIYKLDNLVAIFDINRLgQSDPAPLQHQVDIYQKRCEAFGWHTI-IVDGHSVEELCKAFGQAK---HQPTA 237
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 238 IIAKTFKGRGITGIEDKEAWHGKPLPK------------NMAEQII-QEIY------------SQVQSKKKILAT----P 288
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAykkkY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 289 PQEDAPSVDIANIRMP-----TPPSYKVGDK-IATRKAYGLALAKLGHASDRIIALDGDTKNSTFSEL-----FKKEHPD 357
Cdd:TIGR00232 317 PELAAEFTRRLSGELPadwdkQLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHENPLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 358 RFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMF 437
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 438 RSVPMSTVFYPSDGVATEKAVELAantkgicfIRTSRPENAIIYS-----NNEDFQVGQAK----VVLKSKDDQVTVIGA 508
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSrqnlpQLEESSLEKVLkggyVLKDSKGPDLILIAT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 509 GVTLHEALAAAESLKKDKISIRVLDPFTIKPLD------RKLILDSARAtkgrILTVED------HYYEGGIGEAVSAAV 576
Cdd:TIGR00232 549 GSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDkqdeeyRESVLPANVT----RLAIEAgaadewYKYAGLVGAILGMDS 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 6678359 577 VGEpgvtvtrlavsqvprSGKPAELLKMFGIDKDAIVQAVKGL 619
Cdd:TIGR00232 625 FGE---------------SAPGDKLFEEFGFTVENVVAKAKKL 652
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
313-476 |
2.56e-50 |
|
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: 171.96 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 313 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPD---RFIECYIAEQNMVSIAVGCATRDR-TVPFCST 388
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 389 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGI 467
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 6678359 468 --CFIRTSRPE 476
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-474 |
1.28e-31 |
|
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: 119.51 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 314 KIATRKAYGLALAKLGhasdriialdgdtknstfselfkkehpdrfIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAFF 393
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 394 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTS 473
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 6678359 474 R 474
Cdd:smart00861 131 R 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-620 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 572.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 88 EAGF-LPEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCMLGDG 156
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 157 EVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDiYQKRCEAFGWHTIIVDGHSVEELCKAFGQAKH--Q 234
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 235 PTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQiiqeiysqvqsKKKILATPPqedapsvdianirmptppsykvgdk 314
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 315 iatRKAYGLALAKLGHASDRIIALDGDTKNSTFSELF------KKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCST 388
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 389 FAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA-NTKGI 467
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 468 CFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKlild 547
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 548 saratkgriltvEDHYYEGGIGEAVSAAVVGEPGVT----------VTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVK 617
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 6678359 618 GLV 620
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-271 |
2.62e-134 |
|
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: 393.02 E-value: 2.62e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLN 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 100 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNL 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 179 VAIFDINRLGQSDPAPLQHQVDIYQKRCEAFGWHTIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGITGIEDKE 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 6678359 256 AWHGKPLPKNMAEQII 271
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
313-620 |
7.95e-117 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 350.16 E-value: 7.95e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 313 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAF 392
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 393 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFI 470
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 471 RTSRPENAIIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSAR 550
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678359 551 ATkGRILTVEDHYYEGGIGEAVSAAVVGEPGVTVTRLAVSQVP-RSGKPAELLKMFGIDKDAIVQAVKGLV 620
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
8-281 |
1.35e-111 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 335.51 E-value: 1.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 88 EAGFLPEAELLNLRKISSDLDGHPVPKQafT---DVATGSLGQGLGAACGMAYTGKYfDKASYRVYCMLGDGEVSEGSVW 164
Cdd:COG3959 81 EKGYFPKEELATFRKLGSRLQGHPDMKK--TpgvEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 165 EAMAFAGIYKLDNLVAIFDINRLgQSD--------PAPLqhqvdiyQKRCEAFGWHTIIVDGHSVEELCKAFGQAKH--- 233
Cdd:COG3959 158 EAAMAAAHYKLDNLIAIVDRNGL-QIDgptedvmsLEPL-------AEKWEAFGWHVIEVDGHDIEALLAALDEAKAvkg 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6678359 234 QPTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQIIQEIYSQVQSK 281
Cdd:COG3959 230 KPTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELGDY 277
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-619 |
1.20e-77 |
|
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: 259.65 E-value: 1.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRykaLDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLK---FNPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 92 LPEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCMLGDGEVSEG 161
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 162 SVWEAMAFAGIYKLDNLVAIFDINRLgQSDPAPLQHQVDIYQKRCEAFGWHTI-IVDGHSVEELCKAFGQAK---HQPTA 237
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 238 IIAKTFKGRGITGIEDKEAWHGKPLPK------------NMAEQII-QEIY------------SQVQSKKKILAT----P 288
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAykkkY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 289 PQEDAPSVDIANIRMP-----TPPSYKVGDK-IATRKAYGLALAKLGHASDRIIALDGDTKNSTFSEL-----FKKEHPD 357
Cdd:TIGR00232 317 PELAAEFTRRLSGELPadwdkQLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHENPLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 358 RFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMF 437
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 438 RSVPMSTVFYPSDGVATEKAVELAantkgicfIRTSRPENAIIYS-----NNEDFQVGQAK----VVLKSKDDQVTVIGA 508
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSrqnlpQLEESSLEKVLkggyVLKDSKGPDLILIAT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 509 GVTLHEALAAAESLKKDKISIRVLDPFTIKPLD------RKLILDSARAtkgrILTVED------HYYEGGIGEAVSAAV 576
Cdd:TIGR00232 549 GSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDkqdeeyRESVLPANVT----RLAIEAgaadewYKYAGLVGAILGMDS 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 6678359 577 VGEpgvtvtrlavsqvprSGKPAELLKMFGIDKDAIVQAVKGL 619
Cdd:TIGR00232 625 FGE---------------SAPGDKLFEEFGFTVENVVAKAKKL 652
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
19-531 |
9.90e-69 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 235.72 E-value: 9.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 19 ANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPEAEL 97
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 98 LNLRKISSDLDGHPvpKQAFT---DVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCMLGDGEVSEGSVWE 165
Cdd:PTZ00089 90 KNFRQLGSRTPGHP--ERHITpgvEVTTGPLGQGIANAVGLAiaekhlaakFNRPGHPIFDNYVYVICGDGCLQEGVSQE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 166 AMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDIyQKRCEAFGWHTIIVD-GHS-VEELCKAFGQAKH---QPTAIIA 240
Cdd:PTZ00089 168 ALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDV-EKKYEAYGWHVIEVDnGNTdFDGLRKAIEEAKKskgKPKLIIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 241 KTFKGRGiTGIEDKEAWHGKPLP----KNMAEQI-------------IQEIYSQVQSKKKILATPPQE-------DAPSV 296
Cdd:PTZ00089 247 KTTIGYG-SSKAGTEKVHGAPLGdediAQVKELFgldpekkfhvseeVRQFFEQHVEKKKENYEAWKKrfakytaAFPKE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 297 DIANIR----------MPTPPSYKVGDK-IATRKAYGLALAKLGHASDRIIALDGDTKNSTFS-----ELFKKEHPD-RF 359
Cdd:PTZ00089 326 AQAIERrfkgelppgwEKKLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTrpkeaNDFTKASPEgRY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 360 IECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRS 439
Cdd:PTZ00089 406 IRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 440 VPMSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRpENAIIYSNNEDFQVGQAKVVLKSKDD--QVTVIGAGVTLHEAL 516
Cdd:PTZ00089 486 TPNLLVIRPADGTETSGAYALAlANAKTPTILCLSR-QNTPPLPGSSIEGVLKGAYIVVDFTNspQLILVASGSEVSLCV 564
|
570
....*....|....*
gi 6678359 517 AAAESLKKDkISIRV 531
Cdd:PTZ00089 565 EAAKALSKE-LNVRV 578
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
319-474 |
2.67e-66 |
|
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: 213.84 E-value: 2.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 319 KAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDrTVPFCSTFAAFFTRAFD 398
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678359 399 QIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSR 474
Cdd:cd07033 80 QIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
16-620 |
2.75e-61 |
|
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: 215.26 E-value: 2.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYkalDPRNPH--N-DRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKH---NPANPKwpNrDRFVLSAGHGSMLLYSLLHLTGYd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 92 LPEAELLNLRKISSDLDGHP-------VpkqaftDVATGSLGQGLGAACGMAYTGKY----FDKASY-----RVYCMLGD 155
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPeyghtpgV------ETTTGPLGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 156 GEVSEGSVWEAMAFAGIYKLDNLVAIFDINR--------LGQSDpaplqhqvDIyQKRCEAFGWHTI-IVDGHSVEELCK 226
Cdd:COG0021 156 GDLMEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdLAFSE--------DV-AKRFEAYGWHVIrVEDGHDLEAIDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 227 AFGQAKH---QPTAIIAKTFKGRGITGIEDKEAWHGKPL-PKNMAE------------QIIQEIYSQVQSKKKILATP-- 288
Cdd:COG0021 227 AIEAAKAetdKPTLIICKTIIGYGSPNKQGTAKAHGAPLgAEEIAAtkealgwppepfEVPDEVYAHWRAAGERGAAAea 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 289 -------------PQEDAPSVDIANIRMP-----TPPSYKVGDK-IATRKAYGLALAKLGhasDRIIALDG---DTKNST 346
Cdd:COG0021 307 ewnerfaayaaayPELAAELERRLAGELPedwdaALPAFEADAKgVATRKASGKVLNALA---PVLPELIGgsaDLAGSN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 347 FSEL-----FKKEHPD-RFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAF--FTRAfdQIRMAAIsesninlcgSHCG 418
Cdd:COG0021 384 KTTIkgagsFSPEDPSgRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFsdYMRP--AIRLAAL---------MKLP 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 419 V-------SI--GEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANtkgicfiRTSRPeNAIIYS------- 482
Cdd:COG0021 453 ViyvfthdSIglGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLALE-------RKDGP-TALILSrqnlptl 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 483 NNEDFQVGQAK----VVLKSKDD-QVTVIGAGVTLHEALAAAESLKKDKISIRV-----LDPFTIKPLD-RKLILDSarA 551
Cdd:COG0021 525 DRTAAAAEGVAkgayVLADAEGTpDVILIATGSEVSLAVEAAELLAAEGIKVRVvsmpsWELFEAQDAAyRESVLPP--A 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678359 552 TKGRIltvedhyyeggigeAVSAAV-------VGEPGVTVTrlavsqVPR---SGKPAELLKMFGIDKDAIVQAVKGLV 620
Cdd:COG0021 603 VRARV--------------AVEAGVtdgwykyVGLDGAVIG------IDTfgaSAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PLN02790 |
PLN02790 |
transketolase |
23-620 |
4.66e-59 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 209.11 E-value: 4.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 23 RISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYkalDPRNP---HNDRFVLSKGHAAPILYAVWAEAGF--LPEAEL 97
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKY---NPKNPywfNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 98 LNLRKISSDLDGHPvpkQAFT----DVATGSLGQGLGAACGMAYTGKY----FDKA-----SYRVYCMLGDGEVSEGSVW 164
Cdd:PLN02790 79 KQFRQWGSRTPGHP---ENFEtpgiEVTTGPLGQGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 165 EAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDIyQKRCEAFGWHTIIVDG--HSVEELCKAFGQAK---HQPTAII 239
Cdd:PLN02790 156 EAASLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDV-DKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKavtDKPTLIK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 240 AKTFKGRGITGIEDKEAWHGKPL-PKNMAE------------QIIQEIYSQVQSKKKILATP---------------PQE 291
Cdd:PLN02790 235 VTTTIGYGSPNKANSYSVHGAALgEKEVDAtrknlgwpyepfHVPEDVKSHWSKHTKEGAALeaewnakfaeykkkyPEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 292 DAPSVDIANIRMPTP-----PSYKVGDKI-ATRKAYGLALAKLGHASDRIIALDGDTKNSTFSEL-----FKKEHP-DRF 359
Cdd:PLN02790 315 AAELKSLISGELPSGwekalPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPeERN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 360 IECYIAEQNMVSIAVGCAT-RDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFR 438
Cdd:PLN02790 395 VRFGVREHGMGAICNGIALhSSGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 439 SVPMSTVFYPSDGVATEKAVELA-ANTKG---ICFIRTSRP-----------ENAIIYSNNEDfqvgqakvvlKSKDDqV 503
Cdd:PLN02790 475 AMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPnlpgtsiegveKGGYVISDNSS----------GNKPD-L 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 504 TVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKlildsaratkgriltvEDHYYEGGIGEAVSAAVVGEPGVT 583
Cdd:PLN02790 544 ILIGTGSELEIAAKAAKELRKEGKKVRVVSMVCWELFEEQ----------------SDEYKESVLPSSVTARVSVEAGST 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 6678359 584 V----------TRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVKGLV 620
Cdd:PLN02790 608 FgwekyvgskgKVIGVDRFGASAPAGILYKEFGFTVENVVAAAKSLL 654
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
313-476 |
2.56e-50 |
|
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: 171.96 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 313 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPD---RFIECYIAEQNMVSIAVGCATRDR-TVPFCST 388
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 389 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGI 467
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 6678359 468 --CFIRTSRPE 476
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-620 |
6.58e-48 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 176.81 E-value: 6.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 129 LGAACGMAYTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKlDNLVAIFDINRLGQSDP--------APLQHQVD 200
Cdd:PRK05444 123 ISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDNEMSISPNvgalsnylARLRSSTL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 201 IyqkrcEAFGWHTI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGITGIE-DKEAWHGkpLPKnmaeqiiqeiyS 276
Cdd:PRK05444 202 F-----EELGFNYIgPIDGHDLDALIETLKNAKdlKGPVLLHVVTKKGKGYAPAEaDPIKYHG--VGK-----------F 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 277 QVQSKKKILATPPQedapsvdianirmptPPSYKvgdkiatrKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHP 356
Cdd:PRK05444 264 DPETGEQPKSSKPG---------------KPSYT--------KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 357 DRFIECYIAEQNMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQIRM-AAISESNINLCGSHCGVSiGEDGPSQMALEDLA 435
Cdd:PRK05444 321 DRYFDVGIAEQHAVTFAAGLAT-EGLKPVVAIYSTFLQRAYDQVIHdVALQNLPVTFAIDRAGLV-GADGPTHQGAFDLS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 436 MFRSVPMSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENA-IIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLH 513
Cdd:PRK05444 399 YLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRGNGVgVELPELEPLPIGKGEVLREGED--VAILAFGTMLA 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 514 EALAAAESLKkdkiSIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVSAAVVGE-PGVTVTRLAVSQ- 591
Cdd:PRK05444 477 EALKAAERLA----SATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLEFLADHgLDVPVLNLGLPDe 551
|
490 500 510
....*....|....*....|....*....|
gi 6678359 592 -VPRsGKPAELLKMFGIDKDAIVQAVKGLV 620
Cdd:PRK05444 552 fIDH-GSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
216-620 |
1.48e-44 |
|
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: 167.88 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 216 VDGHSVEELCKAFGQAKHQPTAII--AKTFKGRGIT-GIEDKEAWHGkPLPKNMAeqiiqeiySQVQSKKKilatppqed 292
Cdd:COG1154 252 IDGHDLDALVETLRNAKDLKGPVLlhVVTKKGKGYApAEKDPDKFHG-VGPFDPE--------TGEPKKSK--------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 293 apsvdianirmPTPPSYkvgdkiaTrKAYGLALAKLGHASDRIIA-----LDGdtknsTFSELFKKEHPDRFIECYIAEQ 367
Cdd:COG1154 314 -----------SSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERFPDRFFDVGIAEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 368 NMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQIRM-AAISesniNLcgshcGVSI--------GEDGPSQMALEDLAMFR 438
Cdd:COG1154 370 HAVTFAAGLAT-EGLKPVVAIYSTFLQRAYDQVIHdVALQ----NL-----PVTFaidraglvGADGPTHHGVFDLSYLR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 439 SVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSR--PENAIIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEAL 516
Cdd:COG1154 440 CIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgnGPGVELPAELEPLPIGKGEVLREGKD--VAILAFGTMVAEAL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 517 AAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVSAAVVGEpGVT--VTRLAVSQ--V 592
Cdd:COG1154 518 EAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEFLADA-GLDvpVLRLGLPDrfI 595
|
410 420
....*....|....*....|....*...
gi 6678359 593 PRsGKPAELLKMFGIDKDAIVQAVKGLV 620
Cdd:COG1154 596 EH-GSRAELLAELGLDAEGIARAILELL 622
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
16-262 |
1.59e-43 |
|
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: 159.09 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPE 94
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 95 AELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCMLGDGEVSEGSVW 164
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPeFGHTAGVEVTTGPLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 165 EAMAFAGIYKLDNLVAIFDINRLGqsdpapLQHQVDIY-----QKRCEAFGWHTI-IVDGHSVEELCKAFGQAK---HQP 235
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQIS------IDGETKISftedtAARFEAYGWHVIeVEDGHDVEAIAAAIEEAKaekDKP 236
|
250 260
....*....|....*....|....*..
gi 6678359 236 TAIIAKTFKGRGITGIEDKEAWHGKPL 262
Cdd:pfam00456 237 TLIKCRTVIGYGSPNKQGTHDVHGAPL 263
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
492-612 |
5.97e-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: 133.88 E-value: 5.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 492 AKVVLKSKDDQVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEA 571
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 6678359 572 VSAAVVGE----PGVTVTRLAVSQVPRSGKPAELLKMFGIDKDAI 612
Cdd:pfam02780 80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-622 |
8.24e-32 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 131.00 E-value: 8.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 129 LGAACGMAyTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFD---------------INRLGQSD-- 191
Cdd:PRK12571 125 ISAALGFA-KARALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDnemsiappvgalaayLSTLRSSDpf 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 192 --------------PAPLQ---HQVDIYQKRC-------EAFGWHTI-IVDGHSVEELCKAFGQAKHQ---PTAIIAKTF 243
Cdd:PRK12571 204 arlraiakgveerlPGPLRdgaRRARELVTGMigggtlfEELGFTYVgPIDGHDMEALLSVLRAARARadgPVLVHVVTE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 244 KGRGITGIE-DKEAWHGkplpknmaeqiiqeiYSQVQskkkiLATPPQEDAPsvdianirmPTPPSYKvgdkiatrKAYG 322
Cdd:PRK12571 284 KGRGYAPAEaDEDKYHA---------------VGKFD-----VVTGLQKKSA---------PSAPSYT--------SVFG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 323 LALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDrTVPFCSTFAAFFTRAFDQIRM 402
Cdd:PRK12571 327 EELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLH 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 403 -AAISESNINLCGSHCGVsIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAV-ELAANTKGICFIRTSRPE--NA 478
Cdd:PRK12571 406 dVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEgvGV 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 479 IIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLIldsARATKGRI-L 557
Cdd:PRK12571 485 EIPAEGTILGIGKGRVPREGPD--VAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALT---DLLVRHHIvV 559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678359 558 TVEDHYYEGGIGEAVSAAvVGEPGVTVTRLAVSQV---PR---SGKPAELLKMFGIDKDAIVQAVKGLVTK 622
Cdd:PRK12571 560 IVEEQGAMGGFGAHVLHH-LADTGLLDGGLKLRTLglpDRfidHASREEMYAEAGLTAPDIAAAVTGALAR 629
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-474 |
1.28e-31 |
|
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: 119.51 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 314 KIATRKAYGLALAKLGhasdriialdgdtknstfselfkkehpdrfIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAFF 393
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 394 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTS 473
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 6678359 474 R 474
Cdd:smart00861 131 R 131
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
36-269 |
6.28e-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: 104.31 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 36 GHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHndrfVLSKGHAAPILYAVWAEAGFLPEAELLNLRKISSD--LDGHPVP 113
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEGGGGDL----VYFQGHASPGIYARAFLEGRLTEEQLDNFRQEVGGggLSSYPHP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 114 KQ--AFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDIN 185
Cdd:cd02017 107 WLmpDFWEFPTVSMGLGPIQAIYQARFNRYLedrglkDTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 186 RlgQSDPAPLQHQVDIYQkRCEAF----GWHTIIV--------------------------------------------- 216
Cdd:cd02017 187 L--QRLDGPVRGNGKIIQ-ELEGIfrgaGWNVIKViwgskwdellakdgggalrqrmeetvdgdyqtlkakdgayvrehf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 217 ---------------D---------GHSVEELCKAFGQA---KHQPTAIIAKTFKGRGItgiedKEAWHGkplpKNMAEQ 269
Cdd:cd02017 264 fgkypelkalvtdlsDedlwalnrgGHDPRKVYAAYKKAvehKGKPTVILAKTIKGYGL-----GAAGEG----RNHAHQ 334
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
350-577 |
7.64e-20 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 91.58 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 350 LFKKEHPDRFIECYIAEQNMVSIAVGCATRDRTvPFCS-TFAAFFTRAFDQIrmaaisesnIN-------LCGS--HCGV 419
Cdd:PTZ00182 75 LLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLR-PIAEfMFADFIFPAFDQI---------VNeaakyryMSGGqfDCPI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 420 SI-GEDGPS-QMALEDL----AMFRSVPMSTVFYPSDgvatekavelAANTKGICF--IRTSRP----ENAIIY------ 481
Cdd:PTZ00182 145 VIrGPNGAVgHGGAYHSqsfeAYFAHVPGLKVVAPSD----------PEDAKGLLKaaIRDPNPvvffEPKLLYresvev 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 482 SNNEDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATkGRILTV 559
Cdd:PTZ00182 215 VPEADYTLplGKAKVVREGKD--VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIV 291
|
250
....*....|....*...
gi 6678359 560 EDHYYEGGIGEAVSAAVV 577
Cdd:PTZ00182 292 HEAPPTCGIGAEIAAQIM 309
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
132-620 |
2.25e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 91.99 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 132 ACGMAyTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKlDNLVAIFDINRLGQSDpaplqHQVDIYQK------- 204
Cdd:PRK12315 122 ATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAE-----NHGGLYKNlkelrdt 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 205 --RCE-----AFGWHTIIV-DGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGIT-GIEDKEAWH---------GKPLPK 264
Cdd:PRK12315 195 ngQSEnnlfkAMGLDYRYVeDGNDIESLIEAFKEVKdiDHPIVLHIHTLKGKGYQpAEENKEAFHwhmpfdletGQSKVP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 265 NMAEQ----IIQEIYSQVQSKKKILAtppqedapsvdianIRMPTPPSYKVGDkiatrkayglalaklghasdriialdg 340
Cdd:PRK12315 275 ASGESyssvTLDYLLKKIKEGKPVVA--------------INAAIPGVFGLKE--------------------------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 341 dtknstfselFKKEHPDRFIECYIAEQNMVSIAVGCAtRDRTVPFCSTFAAFFTRAFDQIR--MAAISESNINLCGshcG 418
Cdd:PRK12315 314 ----------FRKKYPDQYVDVGIAEQESVAFASGIA-ANGARPVIFVNSTFLQRAYDQLShdLAINNNPAVMIVF---G 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 419 VSIGEDGPSQMALEDLAMFRSVPMSTVFYPsdgvaTEKAVELA------ANTKGICFIRTsrPENAIIYSNNEDFQVGQA 492
Cdd:PRK12315 380 GSISGNDVTHLGIFDIPMISNIPNLVYLAP-----TTKEELIAmlewalTQHEHPVAIRV--PEHGVESGPTVDTDYSTL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 493 KVVLKSKDDQVTVIGAGVTLHEALAAAESLKKD-KISIRVLDPFTIKPLDRKLiLDSARATKGRILTVEDHYYEGGIGEA 571
Cdd:PRK12315 453 KYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVVTLEDGILDGGFGEK 531
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 6678359 572 VsAAVVGEPGVTV-----TRLAVSQVPrsgkPAELLKMFGIDKDAIVQAVKGLV 620
Cdd:PRK12315 532 I-ARYYGNSDMKVlnygaKKEFNDRVP----VEELYKRNHLTPEQIVEDILSVL 580
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
121-569 |
2.69e-18 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 89.00 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 121 ATGSLGQGLGAACGMAyTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGiYKLDNLVAIFDINRL---------GQSD 191
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG-YLHSNMIVILNDNKQvslptanldGPTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 192 P-APLQHQVDIYQKRC-----------EAFGWHTI-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTFKGRGITGIED- 253
Cdd:PLN02234 253 PvGALSCALSRLQSNCgmiretsstlfEELGFHYVgPVDGHNIDDLVSILETLKSTktigPVLIHVVTEKGRGYPYAERa 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 254 KEAWHGkplpknmaeqiiqeiysqvqskkkILATPPQEDAPSVDIANIRMPTppsykvgdkiatrKAYGLALAKLGHASD 333
Cdd:PLN02234 333 DDKYHG------------------------VLKFDPETGKQFKNISKTQSYT-------------SCFVEALIAEAEADK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 334 RIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQ-IRMAAISESNINL 412
Cdd:PLN02234 376 DIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLAC-EGLKPFCTIYSSFMQRAYDQvVHDVDLQKLPVRF 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 413 CGSHCGVsIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA--NTKGICF-------IRTSRPENaiiySN 483
Cdd:PLN02234 455 AIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCFryhrgngIGVSLPPG----NK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 484 NEDFQVGQAKVVlkSKDDQVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKgRILTVEdhy 563
Cdd:PLN02234 530 GVPLQIGRGRIL--RDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE-VLITVE--- 603
|
....*.
gi 6678359 564 yEGGIG 569
Cdd:PLN02234 604 -EGSIG 608
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
12-569 |
3.02e-17 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 85.72 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 12 LQALKDTANRLRISSIQATTAAGsGHPTSCCSAAEIMAVLFFhtmrykaldPRNPHNDRFVLSKGHAA------------ 79
Cdd:PLN02582 48 VKELKQLADELRSDVIFNVSKTG-GHLGSSLGVVELTVALHY---------VFNAPQDKILWDVGHQSyphkiltgrrdk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 80 -PILYAVWAEAGFLPEAEllnlrkisSDLD----GHpvpkqaftdvATGSLGQGLGAACGMAYTGKyfdkaSYRVYCMLG 154
Cdd:PLN02582 118 mHTMRQTNGLSGFTKRAE--------SEYDcfgtGH----------SSTTISAGLGMAVGRDLKGK-----KNNVVAVIG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 155 DGEVSEGSVWEAMAFAGIYKLDNLVAIFD------------------------INRLGQSDPA----------------- 193
Cdd:PLN02582 175 DGAMTAGQAYEAMNNAGYLDSDMIVILNDnkqvslptatldgpappvgalssaLSRLQSSRPLrelrevakgvtkqiggp 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 194 --PLQHQVDIYQKRC---------EAFGWHTI-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTFKGRGITGIE---DK 254
Cdd:PLN02582 255 mhELAAKVDEYARGMisgsgstlfEELGLYYIgPVDGHNIDDLVTILREVKSTkttgPVLIHVVTEKGRGYPYAEraaDK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 255 eaWHGkplpknmaeqiiqeiysqvqskkkilatppqedapsvdIANIRMPTPPSYKVGDKIATRKAY-GLALAKLGHASD 333
Cdd:PLN02582 335 --YHG--------------------------------------VVKFDPATGKQFKVKAKTQSYTTYfAEALIAEAEVDK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 334 RIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQ-IRMAAISESNINL 412
Cdd:PLN02582 375 DVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLAC-EGLKPFCAIYSSFLQRGYDQvVHDVDLQKLPVRF 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 413 CGSHCGVsIGEDGPSQMALEDLAMFRSVPMSTVFYPSDG------VATEKAVElaanTKGICFiRTSRPeNAI---IYSN 483
Cdd:PLN02582 454 AMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEaelfhmVATAAAID----DRPSCF-RYPRG-NGIgvqLPPN 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 484 NED--FQVGQAKVVLKSkdDQVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKgRILTVEd 561
Cdd:PLN02582 527 NKGipIEVGKGRILLEG--ERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVE- 602
|
....*...
gi 6678359 562 hyyEGGIG 569
Cdd:PLN02582 603 ---EGSIG 607
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
121-243 |
3.53e-16 |
|
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: 79.46 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 121 ATGSLGQGLGAACGMAYTGKYFDKASYrVYCMLGDGEVSEGSVWEAMAFAGIYKLDnlvAIFDI--NRLGQSDPAPLQHQ 198
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFAALWKLP---VIFVCenNGYAISTPTSRQTA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 6678359 199 VDIYQKRCEAFGWHTIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 243
Cdd:cd02000 178 GTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAveraraGGGPTLIEAVTY 228
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
351-573 |
5.28e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 78.60 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 351 FKKEHPDRFIECYIAEQNMVSIAVGCATRDRTvPFCSTFAAFFTRAFDQIRMAAISESN-INLCGSHCGVsIGEDGPSQM 429
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 430 ALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA--NTKGICFirtSRPENAIIYSN-----NEDFQVGQAKVVLKSKDdq 502
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCF---RFPRGSIVNMNylvptGLPIEIGRGRVLVEGQD-- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678359 503 VTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYeGGIGEAVS 573
Cdd:PLN02225 570 VALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHK-FLITVEEGCV-GGFGSHVA 638
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
121-243 |
5.28e-14 |
|
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: 73.64 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 121 ATGSLGQGLGAACGMAYTGKYF--DKAsyrVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDiNRLGQSDPAPLQ-H 197
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAISTPVERQtA 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6678359 198 QVDIYQkRCEAFGWHTIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 243
Cdd:COG1071 201 VETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEAveraraGEGPTLIEAKTY 251
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
350-576 |
6.21e-14 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 73.22 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 350 LFKKEHPDRFIECYIAEQNMVSIAVGCAtrdrtvpFCS--------TFAaFFTRAFDQIRMAAISESNINlcGSHCGVSI 421
Cdd:PRK09212 44 LLEQFGPKRVIDTPITEHGFAGLAVGAA-------FAGlrpivefmTFN-FSMQAIDQIVNSAAKTNYMS--GGQLKCPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 422 GEDGP----SQMALEDLAMFRS----VPMSTVFYPSdgvatekaveLAANTKG--ICFIRTSRP----ENAIIYSNNEDF 487
Cdd:PRK09212 114 VFRGPngaaARVAAQHSQCYAAwyshIPGLKVVAPY----------FAADCKGllKTAIRDPNPviflENEILYGHSHEV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 488 -------QVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATkGRILTVE 560
Cdd:PRK09212 184 peeeesiPIGKAAILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVE 260
|
250
....*....|....*.
gi 6678359 561 DHYYEGGIGEAVSAAV 576
Cdd:PRK09212 261 EGWPFAGVGAEIAALI 276
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
461-617 |
3.88e-13 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 71.87 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 461 AANTKGI--CFIRTSRP----ENAIIYSNN------EDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDK 526
Cdd:PRK11892 289 AADAKGLlkAAIRDPNPviflENEILYGQSfdvpklDDFVLpiGKARIHREGKD--VTIVSFSIGMTYALKAAEELAKEG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 527 ISIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEAVSAAVVGE-------PgvtVTRLAVSQVPRsgkP- 598
Cdd:PRK11892 367 IDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARVMEQafdyldaP---VLRVTGKDVPM---Py 439
|
170 180
....*....|....*....|
gi 6678359 599 -AELLKMFGIDKDAIVQAVK 617
Cdd:PRK11892 440 aANLEKLALPSVAEVVEAVK 459
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
350-617 |
5.31e-13 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 70.62 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 350 LFKKEHPDRFIECYIAEQNMVSIAVGCATRD-RTVPFCSTFAaFFTRAFDQIRMAAiSESNInLCGSHCGVSIGEDGP-- 426
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHIINSA-AKTNY-MSAGQISVPIVFRGPng 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 427 ------SQMALEDLAMFRSVPMSTVFYPSDgvaTEKAVEL--AAntkgicfIRTSRP----ENAIIYSNN---------E 485
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYS---SEDARGLlkAA-------IRDPDPvvflENELLYGESfpvsaevldS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 486 DF--QVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHY 563
Cdd:PLN02683 214 SFvlPIGKAKIEREGKD--VTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6678359 564 YEGGIGEAVSAAVVGEP----GVTVTRLAVSQVPRSgKPAELLKMFGIDKDAIVQAVK 617
Cdd:PLN02683 291 PQHGVGAEICASVVEESfdylDAPVERIAGADVPMP-YAANLERLALPQVEDIVRAAK 347
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
58-242 |
6.67e-12 |
|
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: 64.20 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 58 YKALDPRNPHNDRFVLSKGHAAPILYAVWAeagflpeaellnlrkissdldgHPVPKQAFTDVATGSLGQGLGAACGMAY 137
Cdd:cd00568 3 LAALRAALPEDAIVVNDAGNSAYWAYRYLP----------------------LRRGRRFLTSTGFGAMGYGLPAAIGAAL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 138 TGKyfDKasyRVYCMLGDGEVSEGsvWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQ------VDI----YQKRCE 207
Cdd:cd00568 61 AAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYggrvsgTDLsnpdFAALAE 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 6678359 208 AFGWHTIIVDghSVEELCKAFGQAK--HQPTAIIAKT 242
Cdd:cd00568 134 AYGAKGVRVE--DPEDLEAALAEALaaGGPALIEVKT 168
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
122-247 |
3.99e-09 |
|
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: 56.79 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 122 TGSLGQGLGAACGMAYTGKYFDKaSYRVYCMLGDGEVSEGSVWEAMAFAGiYKLDNLVAIFDINRLGQSDPAPLQhqvdi 201
Cdd:cd02007 74 TGHSSTSISAALGMAVARDLKGK-KRKVIAVIGDGALTGGMAFEALNNAG-YLKSNMIVILNDNEMSISPNVGTP----- 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 6678359 202 yQKRCEAFGWHTI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRG 247
Cdd:cd02007 147 -GNLFEELGFRYIgPVDGHNIEALIKVLKEVKdlKGPVLLHVVTKKGKG 194
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
36-187 |
2.91e-07 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 53.61 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 36 GHPTSCCSAAEIMAVLFFHTMRykalDPRNPHNDRFVLSKGHAAPILYA-VWAEaGFLPEAELLNLRK------ISSdld 108
Cdd:PRK09405 108 GHISSFASSATLYEVGFNHFFR----APNEPHGGDLVFFQGHASPGIYArAFLE-GRLTEEQLDNFRQevdgkgLSS--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 109 gHPVPK--QAFTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCMLGDGEVSE----GsvweAMAFAGIYK 174
Cdd:PRK09405 180 -YPHPWlmPDFWQFPTVSMG--LGPIMAIyqARFLKYLenrglkDTSDQKVWAFLGDGEMDEpeslG----AISLAAREK 252
|
170
....*....|....*..
gi 6678359 175 LDNLvaIFDIN----RL 187
Cdd:PRK09405 253 LDNL--IFVINcnlqRL 267
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
36-185 |
7.21e-07 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 52.63 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 36 GHPTSCCSAAEIMAVLFFHTMRYKAldprNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLNLRKiSSDLDG-----H 110
Cdd:PRK13012 116 GHIASYASAADLFEVGFNHFFRGRD----DAGGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQ-EIGGPGlssypH 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 111 PVPKQAFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVaiFDI 184
Cdd:PRK13012 191 PWLMPDFWQFPTGSMGIGPINAIYQARFMRYLqhrglkDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLV--FVI 268
|
.
gi 6678359 185 N 185
Cdd:PRK13012 269 N 269
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
36-187 |
4.26e-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: 50.07 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 36 GHPTSCCSAAEIMAVLFFHTMRykalDPRNPHNDRFVLSKGHAAPILYAvwaEA---GFLPEAELLNLRKissDLDGH-- 110
Cdd:COG2609 109 GHISSFASAATLYEVGFNHFFR----GPDHPGGGDLVYFQGHASPGIYA---RAfleGRLTEEQLDNFRQ---EVDGKgl 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 111 ---PVPKQA--FTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCMLGDGEVSE----GsvweAMAFAGIY 173
Cdd:COG2609 179 ssyPHPWLMpdFWQFPTVSMG--LGPINAIyqARFMKYLhnrglkDTSDRKVWAFLGDGEMDEpeslG----AISLAARE 252
|
170
....*....|....*...
gi 6678359 174 KLDNLvaIFDIN----RL 187
Cdd:COG2609 253 KLDNL--IFVINcnlqRL 268
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
358-621 |
1.62e-05 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 47.43 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 358 RFIECYIAEQNMVSIAVGCA-TRDRTVpFCSTFAAFFTRAFDQI--RMAAISESNinlcGSHCGVSIGEDGPS----QMA 430
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAmTGLRPI-VEGMNMGFLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 431 LEDL----AMFRSVP-MSTVfypsdgvatekAVELAANTKGI--CFIRTSRP----ENAIIYSNNED-------FQVGQA 492
Cdd:CHL00144 127 AEHSqrleSYFQSVPgLQIV-----------ACSTPYNAKGLlkSAIRSNNPviffEHVLLYNLKEEipdneylLPLEKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 493 KVVLKSKDdqVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAV 572
Cdd:CHL00144 196 EVVRPGND--ITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIGAEL 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6678359 573 SAAVV----GEPGVTVTRLAVSQVPR--SGKpaeLLKMFGIDKDAIVQAVKGLVT 621
Cdd:CHL00144 273 IAQINehlfDELDAPIVRLSSQDVPTpyNGP---LEEATVIQPAQIIEAVEQIIT 324
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
125-279 |
1.71e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 47.17 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 125 LGQGLGAACGMAYTGKYF-----DKASYRVY-CMLGDGEVSEGSVWEAMAFAGIYKL-------DNLVAIFDINRLGQSd 191
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRqqvlkEVQPLRVTaCFFGDGTTNNGQFFECLNMAVLWKLpiifvveNNQWAIGMAHHRSTS- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 192 paplqhQVDIYqKRCEAFGWHTIIVDGHSVEELCKAFGQA------KHQPTAIIAKTFKGRG--------ITGIEDKEAW 257
Cdd:CHL00149 209 ------IPEIH-KKAEAFGLPGIEVDGMDVLAVREVAKEAverarqGDGPTLIEALTYRFRGhsladpdeLRSKQEKEAW 281
|
170 180
....*....|....*....|...
gi 6678359 258 HGKPLPKNMAEQII-QEIYSQVQ 279
Cdd:CHL00149 282 VARDPIKKLKSYIIdNELASQKE 304
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
121-244 |
1.04e-04 |
|
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: 44.62 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 121 ATGSLGQGLGAACGMAYTGKYfDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDnlvAIFDI--NRLGQSDPAPLQHQ 198
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKY-RGKKEVAITLYGDGAANQGDFFEGLNFAALWKLP---VIFVCenNQYGISTPAERASA 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6678359 199 VDIYQKRCEAFGWHTIIVDGHSVEELCKAFGQAK------HQPTAIIAKTFK 244
Cdd:pfam00676 175 STTYADRARGYGIPGLHVDGMDPLAVYQASKFAAerartgKGPFLIELVTYR 226
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
125-247 |
2.32e-04 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 44.16 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678359 125 LGQGLGAACGMAYTGKYFDKASYRVYCM------LGDGEVSEGSVWEAMAFAGIYKL-------DNLVAIFDINRLGQSD 191
Cdd:PLN02374 196 IGEGIPVATGAAFSSKYRREVLKEESCDdvtlafFGDGTCNNGQFFECLNMAALWKLpivfvveNNLWAIGMSHLRATSD 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678359 192 PaplqhqvDIYqKRCEAFGWHTIIVDGH---SVEELCK-AFGQAKH--QPTAIIAKTFKGRG 247
Cdd:PLN02374 276 P-------EIW-KKGPAFGMPGVHVDGMdvlKVREVAKeAIERARRgeGPTLVECETYRFRG 329
|
|
| |
