|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-628 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 578.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 88 EAGF-LAEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKaslPSSWDYSYRVYCLL 161
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNR---PGLDIVDHYTYVLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 162 GDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDiYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH 241
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 242 --QPTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQiiqeiysqiqsKKKILATPPqedapsvdianirmpslpsykv 319
Cdd:PRK05899 237 stKPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY---------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 320 gdkiatRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIF------KKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPF 393
Cdd:PRK05899 284 ------RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 394 CSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA-NT 472
Cdd:PRK05899 358 GGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRK 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 473 KGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKl 552
Cdd:PRK05899 438 DGPSALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 553 ildsaratkgriltvEDHYYEGGIGEAVSSAVVGEPGIT----------VTHLAVNRVPRSGKPAELLKMFGIDRDAIAQ 622
Cdd:PRK05899 516 ---------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVA 580
|
....*.
gi 384475521 623 AVRGLI 628
Cdd:PRK05899 581 AAKELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-279 |
3.25e-132 |
|
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: 388.02 E-value: 3.25e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLN 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 100 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFDKaslpsswdySYRVYCLLGDGELSEGSVWEAMAFA 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLLGF---------DYRVYVLLGDGELQEGSVWEAASFA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 179 SIYKLDNLVAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRG 255
Cdd:cd02012 152 GHYKLDNLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKG 231
|
250 260
....*....|....*....|....
gi 384475521 256 ITGVEDKESWHGKPLPKNMAEQII 279
Cdd:cd02012 232 VPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
321-628 |
3.32e-119 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 356.70 E-value: 3.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 321 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAF 400
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 401 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFI 478
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 479 RTSRPENAIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSAR 558
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384475521 559 ATkGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVN-RVPRSGKPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-628 |
3.59e-79 |
|
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: 263.88 E-value: 3.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYksqDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 92 LAEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASLPSSWDYsyrVYCLLGDGEL 166
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIVDHY---TYVFVGDGCL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 167 SEGSVWEAMAFASIYKLDNLVAILDINRLgQSDPAPLQHQMDIYQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQ 242
Cdd:TIGR00232 155 QEGISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 243 PTAIIAKTFKGRGITGVEDKESWHGKPLPK------------NMAEQII-QEIY------------SQIQSKKKILAT-- 295
Cdd:TIGR00232 234 PTLIEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAyk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 296 --PPQEDAPSVDIANIRMPS-----LPSYKVGDK-IATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKE 362
Cdd:TIGR00232 314 kkYPELAAEFTRRLSGELPAdwdkqLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 363 HPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDL 442
Cdd:TIGR00232 394 PLGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 443 AMFRSVPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLH 521
Cdd:TIGR00232 474 ASLRAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 522 EALAAAELLKKEKINIRVLDPFTIKPLD------RKLILDSARAtkgrILTVE----DHYYeggigeavssAVVGEPGit 591
Cdd:TIGR00232 554 LAVEAAKKLAAENIKVRVVSMPSFDLFDkqdeeyRESVLPANVT----RLAIEagaaDEWY----------KYAGLVG-- 617
|
650 660 670
....*....|....*....|....*....|....*..
gi 384475521 592 vTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:TIGR00232 618 -AILGMDSFGESAPGDKLFEEFGFTVENVVAKAKKLL 653
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
321-484 |
8.28e-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: 176.20 E-value: 8.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 321 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPD---RFIECYIAEQNMVSIAVGCATRNR-TVPFCST 396
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 397 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGI 475
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 384475521 476 --CFIRTSRPE 484
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
322-482 |
4.27e-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: 120.67 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 322 KIATRKAYGQALAKLGhasdriialdgdtknstfseifkkehpdrfIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAFF 401
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 402 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTS 481
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 384475521 482 R 482
Cdd:smart00861 131 R 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-628 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 578.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 88 EAGF-LAEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKaslPSSWDYSYRVYCLL 161
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNR---PGLDIVDHYTYVLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 162 GDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDiYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH 241
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 242 --QPTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQiiqeiysqiqsKKKILATPPqedapsvdianirmpslpsykv 319
Cdd:PRK05899 237 stKPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY---------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 320 gdkiatRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIF------KKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPF 393
Cdd:PRK05899 284 ------RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 394 CSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA-NT 472
Cdd:PRK05899 358 GGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRK 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 473 KGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKl 552
Cdd:PRK05899 438 DGPSALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 553 ildsaratkgriltvEDHYYEGGIGEAVSSAVVGEPGIT----------VTHLAVNRVPRSGKPAELLKMFGIDRDAIAQ 622
Cdd:PRK05899 516 ---------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVA 580
|
....*.
gi 384475521 623 AVRGLI 628
Cdd:PRK05899 581 AAKELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-279 |
3.25e-132 |
|
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: 388.02 E-value: 3.25e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLN 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 100 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFDKaslpsswdySYRVYCLLGDGELSEGSVWEAMAFA 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLLGF---------DYRVYVLLGDGELQEGSVWEAASFA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 179 SIYKLDNLVAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRG 255
Cdd:cd02012 152 GHYKLDNLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKG 231
|
250 260
....*....|....*....|....
gi 384475521 256 ITGVEDKESWHGKPLPKNMAEQII 279
Cdd:cd02012 232 VPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
321-628 |
3.32e-119 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 356.70 E-value: 3.32e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 321 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAF 400
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 401 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFI 478
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 479 RTSRPENAIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSAR 558
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384475521 559 ATkGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVN-RVPRSGKPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
8-289 |
2.27e-110 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 332.81 E-value: 2.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 88 EAGFLAEAELLNLRKISSDLDGHPVPKQafT---DVATGSLGQGLGAACGMAYTGKYFDKaslpsswdySYRVYCLLGDG 164
Cdd:COG3959 81 EKGYFPKEELATFRKLGSRLQGHPDMKK--TpgvEMSTGSLGQGLSVAVGMALAAKLDGK---------DYRVYVLLGDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 165 ELSEGSVWEAMAFASIYKLDNLVAILDINRLgQSDpAPLQHQMDIY--QKRCEAFGWHAIIVDGHSVEELCKAFGQAKH- 241
Cdd:COG3959 150 ELQEGQVWEAAMAAAHYKLDNLIAIVDRNGL-QID-GPTEDVMSLEplAEKWEAFGWHVIEVDGHDIEALLAALDEAKAv 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 384475521 242 --QPTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSK 289
Cdd:COG3959 228 kgKPTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELGDY 277
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-628 |
3.59e-79 |
|
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: 263.88 E-value: 3.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYksqDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 92 LAEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASLPSSWDYsyrVYCLLGDGEL 166
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIVDHY---TYVFVGDGCL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 167 SEGSVWEAMAFASIYKLDNLVAILDINRLgQSDPAPLQHQMDIYQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQ 242
Cdd:TIGR00232 155 QEGISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 243 PTAIIAKTFKGRGITGVEDKESWHGKPLPK------------NMAEQII-QEIY------------SQIQSKKKILAT-- 295
Cdd:TIGR00232 234 PTLIEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAyk 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 296 --PPQEDAPSVDIANIRMPS-----LPSYKVGDK-IATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKE 362
Cdd:TIGR00232 314 kkYPELAAEFTRRLSGELPAdwdkqLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 363 HPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDL 442
Cdd:TIGR00232 394 PLGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 443 AMFRSVPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLH 521
Cdd:TIGR00232 474 ASLRAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 522 EALAAAELLKKEKINIRVLDPFTIKPLD------RKLILDSARAtkgrILTVE----DHYYeggigeavssAVVGEPGit 591
Cdd:TIGR00232 554 LAVEAAKKLAAENIKVRVVSMPSFDLFDkqdeeyRESVLPANVT----RLAIEagaaDEWY----------KYAGLVG-- 617
|
650 660 670
....*....|....*....|....*....|....*..
gi 384475521 592 vTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:TIGR00232 618 -AILGMDSFGESAPGDKLFEEFGFTVENVVAKAKKLL 653
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
19-539 |
1.45e-73 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 248.82 E-value: 1.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 19 ANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LAEAEL 97
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 98 LNLRKISSDLDGHPvpKQAFT---DVATGSLGQGLGAACGMAYTGKYF-DKASLPSSWDYSYRVYCLLGDGELSEGSVWE 173
Cdd:PTZ00089 90 KNFRQLGSRTPGHP--ERHITpgvEVTTGPLGQGIANAVGLAIAEKHLaAKFNRPGHPIFDNYVYVICGDGCLQEGVSQE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 174 AMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIyQKRCEAFGWHAIIVD-GHS-VEELCKAFGQAKH---QPTAIIA 248
Cdd:PTZ00089 168 ALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDV-EKKYEAYGWHVIEVDnGNTdFDGLRKAIEEAKKskgKPKLIIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 249 KTFKGRGiTGVEDKESWHGKPLP----KNMAEQI-------------IQEIYSQIQSKKKILATPPQE-------DAPSV 304
Cdd:PTZ00089 247 KTTIGYG-SSKAGTEKVHGAPLGdediAQVKELFgldpekkfhvseeVRQFFEQHVEKKKENYEAWKKrfakytaAFPKE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 305 DIANIRMPS----------LPSYKVGDK-IATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKEHPD-RF 367
Cdd:PTZ00089 326 AQAIERRFKgelppgwekkLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPkeandFTKASPEgRY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 368 IECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRS 447
Cdd:PTZ00089 406 IRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 448 VPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDfQVGQAKVVLKSKDD--QVTVIGAGVTLHEAL 524
Cdd:PTZ00089 486 TPNLLVIRPADGTETSGAYALAlANAKTPTILCLSRQNTPPLPGSSIE-GVLKGAYIVVDFTNspQLILVASGSEVSLCV 564
|
570
....*....|....*
gi 384475521 525 AAAELLKKEkINIRV 539
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), ... |
327-482 |
2.61e-68 |
|
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: 219.24 E-value: 2.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 327 KAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNrTVPFCSTFAAFFTRAFD 406
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384475521 407 QIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSR 482
Cdd:cd07033 80 QIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PLN02790 |
PLN02790 |
transketolase |
23-628 |
1.26e-59 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 211.03 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 23 RISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF--LAEAELLNL 100
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 101 RKISSDLDGHPvpkQAFT----DVATGSLGQGLGAACGMAYTGKY----FDKaslPSSWDYSYRVYCLLGDGELSEGSVW 172
Cdd:PLN02790 82 RQWGSRTPGHP---ENFEtpgiEVTTGPLGQGIANAVGLALAEKHlaarFNK---PDHKIVDHYTYCILGDGCQMEGISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 173 EAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIyQKRCEAFGWHAIIVDG--HSVEELCKAFGQAK---HQPTAII 247
Cdd:PLN02790 156 EAASLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDV-DKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKavtDKPTLIK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 248 AKTFKGRGITGVEDKESWHGKPL-PKNMAE------------QIIQEIYSQIQSKKKILATP---------------PQE 299
Cdd:PLN02790 235 VTTTIGYGSPNKANSYSVHGAALgEKEVDAtrknlgwpyepfHVPEDVKSHWSKHTKEGAALeaewnakfaeykkkyPEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 300 DAPSVDIANIRMPS-----LPSYKVGDKI-ATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKEHP-DRF 367
Cdd:PLN02790 315 AAELKSLISGELPSgwekaLPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPeERN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 368 IECYIAEQNMVSIAVGCATRNRT-VPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFR 446
Cdd:PLN02790 395 VRFGVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 447 SVPTSTVFYPSDGVATEKAVELA-ANTKG---ICFIRTSRP-------ENA-----IIYNNNEDfqvgqakvvlkSKDDq 510
Cdd:PLN02790 475 AMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPnlpgtsiEGVekggyVISDNSSG-----------NKPD- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 511 VTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKlildsaratkgriltvEDHYYEGGIGEAVSSAVVGEPGI 590
Cdd:PLN02790 543 LILIGTGSELEIAAKAAKELRKEGKKVRVVSMVCWELFEEQ----------------SDEYKESVLPSSVTARVSVEAGS 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 384475521 591 TV----------THLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:PLN02790 607 TFgwekyvgskgKVIGVDRFGASAPAGILYKEFGFTVENVVAAAKSLL 654
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
16-628 |
1.49e-59 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 211.02 E-value: 1.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYksqDPRNPH--N-DRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKH---NPANPKwpNrDRFVLSAGHGSMLLYSLLHLTGYd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 92 LAEAELLNLRKISSDLDGHP-------VpkqaftDVATGSLGQGLGAACGMAYTGKY----FDKAslpsswDYS---YRV 157
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPeyghtpgV------ETTTGPLGQGIANAVGMAIAERHlaarFNRP------GHDivdHYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 158 YCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDINR--------LGQSDpaplqhqmDIyQKRCEAFGWHAI-IVDGHS 228
Cdd:COG0021 150 YVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdLAFSE--------DV-AKRFEAYGWHVIrVEDGHD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 229 VEELCKAFGQAKH---QPTAIIAKTFKGRGITGVEDKESWHGKPL-PKNMAE------------QIIQEIYSQIQSKKKI 292
Cdd:COG0021 221 LEAIDAAIEAAKAetdKPTLIICKTIIGYGSPNKQGTAKAHGAPLgAEEIAAtkealgwppepfEVPDEVYAHWRAAGER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 293 LATP---------------PQEDAPSVDIANIRMP-----SLPSYKVGDK-IATRKAYGQALAKLGhasDRIIALDG--- 348
Cdd:COG0021 301 GAAAeaewnerfaayaaayPELAAELERRLAGELPedwdaALPAFEADAKgVATRKASGKVLNALA---PVLPELIGgsa 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 349 DTKNSTFSEI-----FKKEHPD-RFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAF--FTRAfdQIRMAAIsesninl 420
Cdd:COG0021 378 DLAGSNKTTIkgagsFSPEDPSgRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFsdYMRP--AIRLAAL------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 421 cgSHCGV-------SI--GEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELA-ANTKG-ICFI----------R 479
Cdd:COG0021 449 --MKLPViyvfthdSIglGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLAlERKDGpTALIlsrqnlptldR 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 480 TSRPENAIiynnnedfqvgqAK---VVLKSKDD-QVTVIGAG--VTLheALAAAELLKKEKINIRV-----LDPFTIKPL 548
Cdd:COG0021 527 TAAAAEGV------------AKgayVLADAEGTpDVILIATGseVSL--AVEAAELLAAEGIKVRVvsmpsWELFEAQDA 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 549 D-RKLILDSarATKGRIltvedhyyeggigeAVSSAV-------VGEPGITVthlAVNRVPRSGKPAELLKMFGIDRDAI 620
Cdd:COG0021 593 AyRESVLPP--AVRARV--------------AVEAGVtdgwykyVGLDGAVI---GIDTFGASAPAKVLFEEFGFTVENV 653
|
....*...
gi 384475521 621 AQAVRGLI 628
Cdd:COG0021 654 VAAAKELL 661
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
321-484 |
8.28e-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: 176.20 E-value: 8.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 321 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPD---RFIECYIAEQNMVSIAVGCATRNR-TVPFCST 396
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 397 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGI 475
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 384475521 476 --CFIRTSRPE 484
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-628 |
6.62e-49 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 179.89 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 129 LGAACGMAytgKYFDKASlpsswDYSYRVYCLLGDGELSEGSVWEAMAFASIYKlDNLVAILDINrlgqsdpaplqhQMD 208
Cdd:PRK05444 123 ISAALGMA---KARDLKG-----GEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDN------------EMS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 209 I---------YQKRC------EAFGWHAI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGITGVE-DKESWHG-K 268
Cdd:PRK05444 182 IspnvgalsnYLARLrsstlfEELGFNYIgPIDGHDLDALIETLKNAKdlKGPVLLHVVTKKGKGYAPAEaDPIKYHGvG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 269 PLPKNMAEQIiqeiysqiqSKKKilatppqedapsvdianirmPSLPSYKvgdkiatrKAYGQALAKLGHASDRIIALDG 348
Cdd:PRK05444 262 KFDPETGEQP---------KSSK--------------------PGKPSYT--------KVFGETLCELAEKDPKIVAITA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 349 DTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNrTVPFCSTFAAFFTRAFDQIRM-AAISESNINLCGSHCGV 427
Cdd:PRK05444 305 AMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHdVALQNLPVTFAIDRAGL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 428 SiGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENA-IIYNNNEDFQVGQAKVVLK 505
Cdd:PRK05444 384 V-GADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRGNGVgVELPELEPLPIGKGEVLRE 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 506 SKDdqVTVIGAGVTLHEALAAAELLKkekiNIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVSSAVV 585
Cdd:PRK05444 463 GED--VAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLEFLA 535
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 384475521 586 GE-PGITVTHLAV--NRVPRsGKPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:PRK05444 536 DHgLDVPVLNLGLpdEFIDH-GSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
224-628 |
5.52e-47 |
|
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: 175.20 E-value: 5.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 224 VDGHSVEELCKAFGQAKHQPTAII--AKTFKGRGIT-GVEDKESWHGkPLPKNMAeqiiqeiySQIQSKKKilatppqed 300
Cdd:COG1154 252 IDGHDLDALVETLRNAKDLKGPVLlhVVTKKGKGYApAEKDPDKFHG-VGPFDPE--------TGEPKKSK--------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 301 apsvdianirmPSLPSYkvgdkiaTrKAYGQALAKLGHASDRIIA-----LDGdtknsTFSEIFKKEHPDRFIECYIAEQ 375
Cdd:COG1154 314 -----------SSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERFPDRFFDVGIAEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 376 NMVSIAVGCATRNrTVPFCSTFAAFFTRAFDQIRM-AAISesniNLcgshcGVSI--------GEDGPSQMALEDLAMFR 446
Cdd:COG1154 370 HAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHdVALQ----NL-----PVTFaidraglvGADGPTHHGVFDLSYLR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 447 SVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSR--PENAIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEAL 524
Cdd:COG1154 440 CIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgnGPGVELPAELEPLPIGKGEVLREGKD--VAILAFGTMVAEAL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 525 AAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVSSAVVGEpGIT--VTHLAvnrVPR 602
Cdd:COG1154 518 EAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEFLADA-GLDvpVLRLG---LPD 592
|
410 420 430
....*....|....*....|....*....|
gi 384475521 603 S----GKPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:COG1154 593 RfiehGSRAELLAELGLDAEGIARAILELL 622
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
16-270 |
1.46e-40 |
|
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: 151.00 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LAE 94
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 95 AELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMA-YTGKYFDKASLPSSWDYSYRVYCLLGDGELSEGSVW 172
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPeFGHTAGVEVTTGPLGQGIANAVGMAiAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 173 EAMAFASIYKLDNLVAILDINRL---GQSDPAPLQHQmdiyQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQPTA 245
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQIsidGETKISFTEDT----AARFEAYGWHVIeVEDGHDVEAIAAAIEEAKaekDKPTL 238
|
250 260
....*....|....*....|....*
gi 384475521 246 IIAKTFKGRGITGVEDKESWHGKPL 270
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAPL 263
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
500-620 |
6.74e-36 |
|
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: 130.79 E-value: 6.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 500 AKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEA 579
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 384475521 580 VSSAVVGE----PGITVTHLAVNRVPRSGKPAELLKMFGIDRDAI 620
Cdd:pfam02780 80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
224-630 |
2.29e-34 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 138.70 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 224 VDGHSVEELCKAFGQAKHQ---PTAIIAKTFKGRGITGVE-DKESWHGkplpknmaeqiiqeiYSQIQskkkiLATPPQE 299
Cdd:PRK12571 253 IDGHDMEALLSVLRAARARadgPVLVHVVTEKGRGYAPAEaDEDKYHA---------------VGKFD-----VVTGLQK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 300 DAPsvdianirmPSLPSYKvgdkiatrKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVS 379
Cdd:PRK12571 313 KSA---------PSAPSYT--------SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 380 IAVGCATRNrTVPFCSTFAAFFTRAFDQIRM-AAISESNINLCGSHCGVsIGEDGPSQMALEDLAMFRSVPTSTVFYPSD 458
Cdd:PRK12571 376 FAAGLAAAG-LKPFCAVYSTFLQRGYDQLLHdVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRD 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 459 GVATEKAV-ELAANTKGICFIRTSRPE--NAIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKI 535
Cdd:PRK12571 454 EAELRHMLrTAAAHDDGPIAVRFPRGEgvGVEIPAEGTILGIGKGRVPREGPD--VAILSVGAHLHECLDAADLLEAEGI 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 536 NIRVLDPFTIKPLDRKLIldsARATKGRI-LTVEDHYYEGGIGEAVSSAvvgepgITVTHLAVNRVP-----------RS 603
Cdd:PRK12571 532 SVTVADPRFVKPLDEALT---DLLVRHHIvVIVEEQGAMGGFGAHVLHH------LADTGLLDGGLKlrtlglpdrfiDH 602
|
410 420
....*....|....*....|....*..
gi 384475521 604 GKPAELLKMFGIDRDAIAQAVRGLITK 630
Cdd:PRK12571 603 ASREEMYAEAGLTAPDIAAAVTGALAR 629
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
322-482 |
4.27e-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: 120.67 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 322 KIATRKAYGQALAKLGhasdriialdgdtknstfseifkkehpdrfIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAFF 401
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 402 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTS 481
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 384475521 482 R 482
Cdd:smart00861 131 R 131
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
36-277 |
5.82e-26 |
|
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: 110.09 E-value: 5.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 36 GHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHndrfVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSD--LDGHPVP 113
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEGGGGDL----VYFQGHASPGIYARAFLEGRLTEEQLDNFRQEVGGggLSSYPHP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 114 KQ--AFTDVATGSLGQGLGAACGMAYTGKYFDKASLPSSWDYsyRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILD 191
Cdd:cd02017 107 WLmpDFWEFPTVSMGLGPIQAIYQARFNRYLEDRGLKDTSDQ--KVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 192 INRlgQSDPAPLQHQMDIYQkRCEAF----GWHAIIV------------------------------------------- 224
Cdd:cd02017 185 CNL--QRLDGPVRGNGKIIQ-ELEGIfrgaGWNVIKViwgskwdellakdgggalrqrmeetvdgdyqtlkakdgayvre 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 225 -----------------D---------GHSVEELCKAFGQA---KHQPTAIIAKTFKGRGItgvedKESWHGkplpKNMA 275
Cdd:cd02017 262 hffgkypelkalvtdlsDedlwalnrgGHDPRKVYAAYKKAvehKGKPTVILAKTIKGYGL-----GAAGEG----RNHA 332
|
..
gi 384475521 276 EQ 277
Cdd:cd02017 333 HQ 334
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
157-628 |
5.78e-21 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 97.00 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 157 VYCLLGDGELSEGSVWEAMAFASIYKlDNLVAILDINrlgqsdpaplqhQMDI-------YQK---------RCE----- 215
Cdd:PRK12315 138 IIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDN------------QMSIaenhgglYKNlkelrdtngQSEnnlfk 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 216 AFGWHAIIV-DGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGIT-GVEDKESWH---------GKPLPKNMAEQ----I 278
Cdd:PRK12315 205 AMGLDYRYVeDGNDIESLIEAFKEVKdiDHPIVLHIHTLKGKGYQpAEENKEAFHwhmpfdletGQSKVPASGESyssvT 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 279 IQEIYSQIQSKKKILATppqedapsvdianirmpslpsykvgdKIATRKAYGqalaklghasdriialdgdtknstFSEi 358
Cdd:PRK12315 285 LDYLLKKIKEGKPVVAI--------------------------NAAIPGVFG------------------------LKE- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 359 FKKEHPDRFIECYIAEQNMVSIAVGCAtRNRTVPFCSTFAAFFTRAFDQIR--MAAISESNINLCGshcGVSIGEDGPSQ 436
Cdd:PRK12315 314 FRKKYPDQYVDVGIAEQESVAFASGIA-ANGARPVIFVNSTFLQRAYDQLShdLAINNNPAVMIVF---GGSISGNDVTH 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 437 MALEDLAMFRSVPTSTVFYPsdgvaTEKAVELA------ANTKGICFIRTsrPENAIIYNNNEDFQVGQAKVVLKSKDDQ 510
Cdd:PRK12315 390 LGIFDIPMISNIPNLVYLAP-----TTKEELIAmlewalTQHEHPVAIRV--PEHGVESGPTVDTDYSTLKYEVTKAGEK 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 511 VTVIGAGVTLHEALAAAELLKKE-KINIRVLDPFTIKPLDRKLiLDSARATKGRILTVEDHYYEGGIGEAVSSaVVGEPG 589
Cdd:PRK12315 463 VAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVVTLEDGILDGGFGEKIAR-YYGNSD 540
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 384475521 590 ITVTHLA-----VNRVPrsgkPAELLKMFGIDRDAIAQAVRGLI 628
Cdd:PRK12315 541 MKVLNYGakkefNDRVP----VEELYKRNHLTPEQIVEDILSVL 580
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
359-585 |
6.62e-20 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 91.58 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 359 FKKEHPDRFIECYIAEQNMVSIAVGCATrNRTVPFCS-TFAAFFTRAFDQIrmaaisesnIN-------LCGS--HCGVS 428
Cdd:PTZ00182 76 LDKYGPDRVFDTPITEQGFAGFAIGAAM-NGLRPIAEfMFADFIFPAFDQI---------VNeaakyryMSGGqfDCPIV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 429 I-GEDGPS-QMALEDL----AMFRSVPTSTVFYPSDgvatekavelAANTKGICF--IRTSRP----ENAIIYNN----- 491
Cdd:PTZ00182 146 IrGPNGAVgHGGAYHSqsfeAYFAHVPGLKVVAPSD----------PEDAKGLLKaaIRDPNPvvffEPKLLYREsvevv 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 492 -NEDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVE 568
Cdd:PTZ00182 216 pEADYTLplGKAKVVREGKD--VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVH 292
|
250
....*....|....*..
gi 384475521 569 DHYYEGGIGEAVSSAVV 585
Cdd:PTZ00182 293 EAPPTCGIGAEIAAQIM 309
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
118-577 |
4.29e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 91.31 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 118 TDVATGSLGQGLGAACGMAYTGkyfdkaslpsswdYSYRVYCLLGDGELSEGSVWEAMAFASiYKLDNLVAILDINRL-- 195
Cdd:PLN02234 176 TGHSSTTLSAGLGMAVGRDLKG-------------MNNSVVSVIGDGAMTAGQAYEAMNNAG-YLHSNMIVILNDNKQvs 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 196 -------GQSDP-APLQHQMDIYQKRC-----------EAFGWHAI-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTF 251
Cdd:PLN02234 242 lptanldGPTQPvGALSCALSRLQSNCgmiretsstlfEELGFHYVgPVDGHNIDDLVSILETLKSTktigPVLIHVVTE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 252 KGRGITGVED-KESWHGkplpknmaeqiiqeiysqiqskkkILATPPQEDAPSVDIANIRmpslpSYKvgdkiatrKAYG 330
Cdd:PLN02234 322 KGRGYPYAERaDDKYHG------------------------VLKFDPETGKQFKNISKTQ-----SYT--------SCFV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 331 QALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTvPFCSTFAAFFTRAFDQ-IR 409
Cdd:PLN02234 365 EALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQvVH 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 410 MAAISESNINLCGSHCGVsIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA--NTKGICF-------IRT 480
Cdd:PLN02234 444 DVDLQKLPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCFryhrgngIGV 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 481 SRPENaiiyNNNEDFQVGQAKVVlkSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARAT 560
Cdd:PLN02234 523 SLPPG----NKGVPLQIGRGRIL--RDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH 596
|
490
....*....|....*..
gi 384475521 561 KgRILTVEdhyyEGGIG 577
Cdd:PLN02234 597 E-VLITVE----EGSIG 608
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
329-577 |
1.39e-18 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 89.96 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 329 YGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTvPFCSTFAAFFTRAFDQ- 407
Cdd:PLN02582 362 FAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 408 IRMAAISESNINLCGSHCGVsIGEDGPSQMALEDLAMFRSVPTSTVFYPSDG------VATEKAVElaanTKGICF---- 477
Cdd:PLN02582 441 VHDVDLQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEaelfhmVATAAAID----DRPSCFrypr 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 478 ---IRTSRPENaiiyNNNEDFQVGQAKVVLKSkdDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLIL 554
Cdd:PLN02582 516 gngIGVQLPPN----NKGIPIEVGKGRILLEG--ERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIR 589
|
250 260
....*....|....*....|...
gi 384475521 555 DSARATKgRILTVEdhyyEGGIG 577
Cdd:PLN02582 590 SLAKSHE-VLITVE----EGSIG 607
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
359-584 |
5.06e-17 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 84.77 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 359 FKKEHPDRFIECYIAEQNMVSIAVGCATRNRTvPFCSTFAAFFTRAFDQIRMAAISESN-INLCGSHCGVsIGEDGPSQM 437
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 438 ALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA--NTKGICFirtSRPENAIIYNN-----NEDFQVGQAKVVLKSKDdq 510
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCF---RFPRGSIVNMNylvptGLPIEIGRGRVLVEGQD-- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384475521 511 VTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYeGGIGEAVSSAV 584
Cdd:PLN02225 570 VALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHK-FLITVEEGCV-GGFGSHVAQFI 641
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
121-251 |
3.86e-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: 76.38 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 121 ATGSLGQGLGAACGMAYTGKYFDKASLpsswdysyrVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDiNRLGQSDP 200
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV---------AVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTP 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 384475521 201 APLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 251
Cdd:cd02000 172 TSRQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAveraraGGGPTLIEAVTY 228
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
364-584 |
9.08e-15 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 75.91 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 364 PDRFIECYIAEQNMVSIAVGCATRN-RTVPFCSTFAaFFTRAFDQIRMAAISESNINlcGSHCGVSIGEDGP----SQMA 438
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAGlRPIVEFMTFN-FSMQAIDQIVNSAAKTNYMS--GGQLKCPIVFRGPngaaARVA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 439 LEDLAMFRS----VPTSTVFYPSdgvatekaveLAANTKG--ICFIRTSRP----ENAIIY-------NNNEDFQVGQAK 501
Cdd:PRK09212 127 AQHSQCYAAwyshIPGLKVVAPY----------FAADCKGllKTAIRDPNPviflENEILYghshevpEEEESIPIGKAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 502 VVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEAVS 581
Cdd:PRK09212 197 ILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAEIA 273
|
...
gi 384475521 582 SAV 584
Cdd:PRK09212 274 ALI 276
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
46-250 |
2.29e-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: 65.35 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 46 EIMAVLFFHTmryksqdprnPHNDRFVLSKGHAAPILYAVWAeagflaeaellnlrkissdldgHPVPKQAFTDVATGSL 125
Cdd:cd00568 1 RVLAALRAAL----------PEDAIVVNDAGNSAYWAYRYLP----------------------LRRGRRFLTSTGFGAM 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 126 GQGLGAACGMAYTGKyfDKaslpsswdysyRVYCLLGDGELSEGsvWEAMAFASIYKLdNLVAILDIN-----------R 194
Cdd:cd00568 49 GYGLPAAIGAALAAP--DR-----------PVVCIAGDGGFMMT--GQELATAVRYGL-PVIVVVFNNggygtirmhqeA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 384475521 195 LGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDghSVEELCKAFGQAK--HQPTAIIAKT 250
Cdd:cd00568 113 FYGGRVSGTDLSNPDFAALAEAYGAKGVRVE--DPEDLEAALAEALaaGGPALIEVKT 168
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
358-587 |
2.58e-12 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 68.69 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 358 IFKKEHPDRFIECYIAEQNMVSIAVGCATRN-RTVPFCSTFAaFFTRAFDQIRMAAiSESNInLCGSHCGVSIGEDGP-- 434
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHIINSA-AKTNY-MSAGQISVPIVFRGPng 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 435 ------SQMALEDLAMFRSVPTSTVFYPSDgvaTEKAVEL--AAntkgicfIRTSRP----ENAIIYNNN---------E 493
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYS---SEDARGLlkAA-------IRDPDPvvflENELLYGESfpvsaevldS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 494 DF--QVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHY 571
Cdd:PLN02683 214 SFvlPIGKAKIEREGKD--VTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|....*.
gi 384475521 572 YEGGIGEAVSSAVVGE 587
Cdd:PLN02683 291 PQHGVGAEICASVVEE 306
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
121-251 |
5.72e-12 |
|
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: 67.47 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 121 ATGSLGQGLGAACGMAYTGKYFDKASLpsswdysyrVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDiNRLGQSDP 200
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRGEDEV---------AVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAISTP 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 384475521 201 APLQ-HQMDIYQkRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 251
Cdd:COG1071 195 VERQtAVETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEAveraraGEGPTLIEAKTY 251
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
469-593 |
1.10e-11 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 67.25 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 469 AANTKGI--CFIRTSRP----ENAIIYNNN------EDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEK 534
Cdd:PRK11892 289 AADAKGLlkAAIRDPNPviflENEILYGQSfdvpklDDFVLpiGKARIHREGKD--VTIVSFSIGMTYALKAAEELAKEG 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384475521 535 INIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEAVSSAVVGE-------PGITVT 593
Cdd:PRK11892 367 IDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARVMEQafdyldaPVLRVT 431
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
122-255 |
3.35e-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: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 122 TGSLGQGLGAACGMAytgKYFDKAslpsswDYSYRVYCLLGDGELSEGSVWEAMAFASiYKLDNLVAILDINRLGQSDPA 201
Cdd:cd02007 74 TGHSSTSISAALGMA---VARDLK------GKKRKVIAVIGDGALTGGMAFEALNNAG-YLKSNMIVILNDNEMSISPNV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 384475521 202 PLQHQMdiyqkrCEAFGWHAI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRG 255
Cdd:cd02007 144 GTPGNL------FEELGFRYIgPVDGHNIEALIKVLKEVKdlKGPVLLHVVTKKGKG 194
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
36-195 |
3.15e-06 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 50.32 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 36 GHPTSCCSAAEIMAVLFFHTMRYKSQDprnpHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKissDLDG------ 109
Cdd:PRK13012 116 GHIASYASAADLFEVGFNHFFRGRDDA----GGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQ---EIGGpglssy 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 110 -HPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASLPsswDYSYR-VYCLLGDGELSEGSVWEAMAFASIYKLDNLV 187
Cdd:PRK13012 189 pHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQHRGLK---DTSGRkVWGFFGDGEMDEPESIAALSLAAREGLDNLV 265
|
170
....*....|
gi 384475521 188 AILDIN--RL 195
Cdd:PRK13012 266 FVINCNlqRL 275
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
366-584 |
1.26e-05 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 47.81 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 366 RFIECYIAEQNMVSIAVGCA-TRNRTVpFCSTFAAFFTRAFDQI--RMAAISESNinlcGSHCGVSIGEDGPS----QMA 438
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAmTGLRPI-VEGMNMGFLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 439 LEDL----AMFRSVPTSTVFypsdgvatekAVELAANTKGI--CFIRTSRP----ENAIIYNNNED-------FQVGQAK 501
Cdd:CHL00144 127 AEHSqrleSYFQSVPGLQIV----------ACSTPYNAKGLlkSAIRSNNPviffEHVLLYNLKEEipdneylLPLEKAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 502 VVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVS 581
Cdd:CHL00144 197 VVRPGND--ITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIGAELI 273
|
...
gi 384475521 582 SAV 584
Cdd:CHL00144 274 AQI 276
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
125-287 |
8.28e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 45.24 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 125 LGQGLGAACGMAYTGKYfDKASLPSSWDYSYRVyCLLGDGELSEGSVWEAMAFASIYKL-------DNLVAILDINRLGQ 197
Cdd:CHL00149 130 IGEGIPIALGAAFQSIY-RQQVLKEVQPLRVTA-CFFGDGTTNNGQFFECLNMAVLWKLpiifvveNNQWAIGMAHHRST 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 198 SDPaplqhqmDIYqKRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTFKGRG--------ITGVEDKE 263
Cdd:CHL00149 208 SIP-------EIH-KKAEAFGLPGIEVDGMDVLAVREVAKEAverarqGDGPTLIEALTYRFRGhsladpdeLRSKQEKE 279
|
170 180
....*....|....*....|....*
gi 384475521 264 SWHGKPLPKNMAEQII-QEIYSQIQ 287
Cdd:CHL00149 280 AWVARDPIKKLKSYIIdNELASQKE 304
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
121-252 |
1.01e-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: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 121 ATGSLGQGLGAACGMAYTGKYFDKASLpsswdysyrVYCLLGDGELSEGSVWEAMAFASIYKLDnLVAILDINRLGQSDP 200
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKYRGKKEV---------AITLYGDGAANQGDFFEGLNFAALWKLP-VIFVCENNQYGISTP 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 384475521 201 APLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAK------HQPTAIIAKTFK 252
Cdd:pfam00676 169 AERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAAerartgKGPFLIELVTYR 226
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
125-255 |
2.04e-04 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 44.16 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 125 LGQGLGAACGMAYTGKYfdKASLPSSWDYSYRVYCLLGDGELSEGSVWEAMAFASIYKL-------DNLVAILDINRLGQ 197
Cdd:PLN02374 196 IGEGIPVATGAAFSSKY--RREVLKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLpivfvveNNLWAIGMSHLRAT 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384475521 198 SDPaplqhqmDIYqKRCEAFGWHAIIVDGH---SVEELCK-AFGQAKH--QPTAIIAKTFKGRG 255
Cdd:PLN02374 274 SDP-------EIW-KKGPAFGMPGVHVDGMdvlKVREVAKeAIERARRgeGPTLVECETYRFRG 329
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
338-458 |
3.45e-03 |
|
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: 38.48 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 338 HASDRIIALDGDTKNSTFSEIfkKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESN 417
Cdd:cd06586 10 WGVRHVFGYPGDEISSLLDAL--REGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAEHLP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 384475521 418 INLCGSHCGVSiGEDGPSQMALEDLAMFRSVPTSTVFYPSD 458
Cdd:cd06586 88 VVFLIGARGIS-AQAKQTFQSMFDLGMYRSIPEANISSPSP 127
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
113-239 |
9.50e-03 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 38.99 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 113 PKQAFTDVATGSLGQGLGAACG--MAYTGKyfdkaslpsswdysyRVYCLLGDG-------ELsegsvweamAFASIYKL 183
Cdd:COG0028 402 PRRFLTSGGLGTMGYGLPAAIGakLARPDR---------------PVVAITGDGgfqmnlqEL---------ATAVRYGL 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475521 184 DNLVAILDINRLGqsdpAPLQHQMDIYQKR--------------CEAFGWHAIIVDghSVEELCKAFGQA 239
Cdd:COG0028 458 PVKVVVLNNGGLG----MVRQWQELFYGGRysgtdlpnpdfaklAEAFGAKGERVE--TPEELEAALEEA 521
|
|
| |
