|
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: 578.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 88 EAGF-LAEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCLLGDG 156
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 157 ELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDiYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH--Q 234
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 235 PTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQiiqeiysqiqsKKKILATPPqedapsvdianirmpslpsykvgdk 314
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 315 iatRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIF------KKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCST 388
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 389 FAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA-NTKGI 467
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 468 CFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKlild 547
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 548 saratkgriltvEDHYYEGGIGEAVSSAVVGEPGIT----------VTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVR 617
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 4507521 618 GLI 620
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-271 |
3.08e-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: 392.64 E-value: 3.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLN 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 100 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNL 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 179 VAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGITGVEDKE 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 4507521 256 SWHGKPLPKNMAEQII 271
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
313-620 |
6.64e-119 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 355.55 E-value: 6.64e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 313 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAF 392
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 393 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFI 470
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 471 RTSRPENAIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSAR 550
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507521 551 ATkGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVN-RVPRSGKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-620 |
3.28e-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: 263.50 E-value: 3.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYksqDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 92 LAEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCLLGDGELSEG 161
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 162 SVWEAMAFASIYKLDNLVAILDINRLgQSDPAPLQHQMDIYQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQPTA 237
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 238 IIAKTFKGRGITGVEDKESWHGKPLPK------------NMAEQII-QEIY------------SQIQSKKKILAT----P 288
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAykkkY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 289 PQEDAPSVDIANIRMPS-----LPSYKVGDK-IATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKEHPD 357
Cdd:TIGR00232 317 PELAAEFTRRLSGELPAdwdkqLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHENPLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 358 RFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMF 437
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 438 RSVPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEAL 516
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 517 AAAELLKKEKINIRVLDPFTIKPLD------RKLILDSARAtkgrILTVE----DHYYeggigeavssAVVGEPGitvTH 586
Cdd:TIGR00232 557 EAAKKLAAENIKVRVVSMPSFDLFDkqdeeyRESVLPANVT----RLAIEagaaDEWY----------KYAGLVG---AI 619
|
650 660 670
....*....|....*....|....*....|....
gi 4507521 587 LAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:TIGR00232 620 LGMDSFGESAPGDKLFEEFGFTVENVVAKAKKLL 653
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
313-476 |
9.46e-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: 175.82 E-value: 9.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 313 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPD---RFIECYIAEQNMVSIAVGCATRNR-TVPFCST 388
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 389 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGI 467
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 4507521 468 --CFIRTSRPE 476
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-474 |
5.26e-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: 120.28 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 314 KIATRKAYGQALAKLGhasdriialdgdtknstfseifkkehpdrfIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAFF 393
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 394 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTS 473
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 4507521 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: 578.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 88 EAGF-LAEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCLLGDG 156
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 157 ELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDiYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH--Q 234
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 235 PTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQiiqeiysqiqsKKKILATPPqedapsvdianirmpslpsykvgdk 314
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 315 iatRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIF------KKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCST 388
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 389 FAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA-NTKGI 467
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 468 CFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKlild 547
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 548 saratkgriltvEDHYYEGGIGEAVSSAVVGEPGIT----------VTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVR 617
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 4507521 618 GLI 620
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-271 |
3.08e-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: 392.64 E-value: 3.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLN 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 100 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNL 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 179 VAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGITGVEDKE 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 4507521 256 SWHGKPLPKNMAEQII 271
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
313-620 |
6.64e-119 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 355.55 E-value: 6.64e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 313 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAF 392
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 393 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFI 470
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 471 RTSRPENAIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSAR 550
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507521 551 ATkGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVN-RVPRSGKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
8-281 |
5.63e-113 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 339.36 E-value: 5.63e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 88 EAGFLAEAELLNLRKISSDLDGHPVPKQafT---DVATGSLGQGLGAACGMAYTGKYfDKASYRVYCLLGDGELSEGSVW 164
Cdd:COG3959 81 EKGYFPKEELATFRKLGSRLQGHPDMKK--TpgvEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 165 EAMAFASIYKLDNLVAILDINRLgQSDpAPLQHQMDIY--QKRCEAFGWHAIIVDGHSVEELCKAFGQAKH---QPTAII 239
Cdd:COG3959 158 EAAMAAAHYKLDNLIAIVDRNGL-QID-GPTEDVMSLEplAEKWEAFGWHVIEVDGHDIEALLAALDEAKAvkgKPTVII 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 4507521 240 AKTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSK 281
Cdd:COG3959 236 AHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELGDY 277
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-620 |
3.28e-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: 263.50 E-value: 3.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYksqDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 92 LAEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCLLGDGELSEG 161
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 162 SVWEAMAFASIYKLDNLVAILDINRLgQSDPAPLQHQMDIYQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQPTA 237
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 238 IIAKTFKGRGITGVEDKESWHGKPLPK------------NMAEQII-QEIY------------SQIQSKKKILAT----P 288
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAykkkY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 289 PQEDAPSVDIANIRMPS-----LPSYKVGDK-IATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKEHPD 357
Cdd:TIGR00232 317 PELAAEFTRRLSGELPAdwdkqLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHENPLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 358 RFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMF 437
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 438 RSVPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEAL 516
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 517 AAAELLKKEKINIRVLDPFTIKPLD------RKLILDSARAtkgrILTVE----DHYYeggigeavssAVVGEPGitvTH 586
Cdd:TIGR00232 557 EAAKKLAAENIKVRVVSMPSFDLFDkqdeeyRESVLPANVT----RLAIEagaaDEWY----------KYAGLVG---AI 619
|
650 660 670
....*....|....*....|....*....|....
gi 4507521 587 LAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:TIGR00232 620 LGMDSFGESAPGDKLFEEFGFTVENVVAKAKKLL 653
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
19-531 |
1.16e-73 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 249.21 E-value: 1.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 19 ANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LAEAEL 97
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 98 LNLRKISSDLDGHPvpKQAFT---DVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCLLGDGELSEGSVWE 165
Cdd:PTZ00089 90 KNFRQLGSRTPGHP--ERHITpgvEVTTGPLGQGIANAVGLAiaekhlaakFNRPGHPIFDNYVYVICGDGCLQEGVSQE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 166 AMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIyQKRCEAFGWHAIIVD-GHS-VEELCKAFGQAKH---QPTAIIA 240
Cdd:PTZ00089 168 ALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDV-EKKYEAYGWHVIEVDnGNTdFDGLRKAIEEAKKskgKPKLIIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 241 KTFKGRGiTGVEDKESWHGKPLP----KNMAEQI-------------IQEIYSQIQSKKKILATPPQE-------DAPSV 296
Cdd:PTZ00089 247 KTTIGYG-SSKAGTEKVHGAPLGdediAQVKELFgldpekkfhvseeVRQFFEQHVEKKKENYEAWKKrfakytaAFPKE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 297 DIANIRMPS----------LPSYKVGDK-IATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKEHPD-RF 359
Cdd:PTZ00089 326 AQAIERRFKgelppgwekkLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPkeandFTKASPEgRY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 360 IECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRS 439
Cdd:PTZ00089 406 IRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 440 VPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDfQVGQAKVVLKSKDD--QVTVIGAGVTLHEAL 516
Cdd:PTZ00089 486 TPNLLVIRPADGTETSGAYALAlANAKTPTILCLSRQNTPPLPGSSIE-GVLKGAYIVVDFTNspQLILVASGSEVSLCV 564
|
570
....*....|....*
gi 4507521 517 AAAELLKKEkINIRV 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 |
3.51e-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: 218.47 E-value: 3.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 319 KAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNrTVPFCSTFAAFFTRAFD 398
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507521 399 QIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSR 474
Cdd:cd07033 80 QIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
16-620 |
1.18e-60 |
|
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: 213.72 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYksqDPRNPH--N-DRFVLSKGHAAPILYAVWAEAGF- 91
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKH---NPANPKwpNrDRFVLSAGHGSMLLYSLLHLTGYd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 92 LAEAELLNLRKISSDLDGHP-------VpkqaftDVATGSLGQGLGAACGMAYTGKY----FDKASY-----RVYCLLGD 155
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPeyghtpgV------ETTTGPLGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 156 GELSEGSVWEAMAFASIYKLDNLVAILDINR--------LGQSDpaplqhqmDIyQKRCEAFGWHAI-IVDGHSVEELCK 226
Cdd:COG0021 156 GDLMEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdLAFSE--------DV-AKRFEAYGWHVIrVEDGHDLEAIDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 227 AFGQAKH---QPTAIIAKTFKGRGITGVEDKESWHGKPL-PKNMAE------------QIIQEIYSQIQSKKKILATP-- 288
Cdd:COG0021 227 AIEAAKAetdKPTLIICKTIIGYGSPNKQGTAKAHGAPLgAEEIAAtkealgwppepfEVPDEVYAHWRAAGERGAAAea 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 289 -------------PQEDAPSVDIANIRMP-----SLPSYKVGDK-IATRKAYGQALAKLGhasDRIIALDG---DTKNST 346
Cdd:COG0021 307 ewnerfaayaaayPELAAELERRLAGELPedwdaALPAFEADAKgVATRKASGKVLNALA---PVLPELIGgsaDLAGSN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 347 FSEI-----FKKEHPD-RFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAF--FTRAfdQIRMAAIsesninlcgSHCG 418
Cdd:COG0021 384 KTTIkgagsFSPEDPSgRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFsdYMRP--AIRLAAL---------MKLP 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 419 V-------SI--GEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELA-ANTKG-ICFI----------RTSRPEN 477
Cdd:COG0021 453 ViyvfthdSIglGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLAlERKDGpTALIlsrqnlptldRTAAAAE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 478 AIiynnnedfqvgqAK---VVLKSKDD-QVTVIGAGVTLHEALAAAELLKKEKINIRV-----LDPFTIKPLD-RKLILD 547
Cdd:COG0021 533 GV------------AKgayVLADAEGTpDVILIATGSEVSLAVEAAELLAAEGIKVRVvsmpsWELFEAQDAAyRESVLP 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 548 SarATKGRIltvedhyyeggigeAVSSAV-------VGEPGITVthlAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:COG0021 601 P--AVRARV--------------AVEAGVtdgwykyVGLDGAVI---GIDTFGASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PLN02790 |
PLN02790 |
transketolase |
23-620 |
5.01e-60 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 211.80 E-value: 5.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 23 RISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF--LAEAELLNL 100
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 101 RKISSDLDGHPvpkQAFT----DVATGSLGQGLGAACGMAYTGKY----FDKA-----SYRVYCLLGDGELSEGSVWEAM 167
Cdd:PLN02790 82 RQWGSRTPGHP---ENFEtpgiEVTTGPLGQGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISNEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 168 AFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIyQKRCEAFGWHAIIVDG--HSVEELCKAFGQAK---HQPTAIIAKT 242
Cdd:PLN02790 159 SLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDV-DKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKavtDKPTLIKVTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 243 FKGRGITGVEDKESWHGKPL-PKNMAE------------QIIQEIYSQIQSKKKILATP---------------PQEDAP 294
Cdd:PLN02790 238 TIGYGSPNKANSYSVHGAALgEKEVDAtrknlgwpyepfHVPEDVKSHWSKHTKEGAALeaewnakfaeykkkyPEEAAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 295 SVDIANIRMPS-----LPSYKVGDKI-ATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEI-----FKKEHP-DRFIEC 362
Cdd:PLN02790 318 LKSLISGELPSgwekaLPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPeERNVRF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 363 YIAEQNMVSIAVGCATRNRT-VPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVP 441
Cdd:PLN02790 398 GVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 442 TSTVFYPSDGVATEKAVELA-ANTKG---ICFIRTSRP-------ENA-----IIYNNNEDfqvgqakvvlkSKDDqVTV 505
Cdd:PLN02790 478 NILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPnlpgtsiEGVekggyVISDNSSG-----------NKPD-LIL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 506 IGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKlildsaratkgriltvEDHYYEGGIGEAVSSAVVGEPGITV- 584
Cdd:PLN02790 546 IGTGSELEIAAKAAKELRKEGKKVRVVSMVCWELFEEQ----------------SDEYKESVLPSSVTARVSVEAGSTFg 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 4507521 585 ---------THLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:PLN02790 610 wekyvgskgKVIGVDRFGASAPAGILYKEFGFTVENVVAAAKSLL 654
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
313-476 |
9.46e-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: 175.82 E-value: 9.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 313 DKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPD---RFIECYIAEQNMVSIAVGCATRNR-TVPFCST 388
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 389 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGI 467
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 4507521 468 --CFIRTSRPE 476
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-620 |
3.93e-50 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 182.97 E-value: 3.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 129 LGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKlDNLVAILDINrlgqsdpaplqhQMDI------- 201
Cdd:PRK05444 123 ISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDN------------EMSIspnvgal 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 202 --YQKRC------EAFGWHAI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGITGVE-DKESWHG-KPLPKNMAE 268
Cdd:PRK05444 190 snYLARLrsstlfEELGFNYIgPIDGHDLDALIETLKNAKdlKGPVLLHVVTKKGKGYAPAEaDPIKYHGvGKFDPETGE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 269 QIiqeiysqiqSKKKilatppqedapsvdianirmPSLPSYKvgdkiatrKAYGQALAKLGHASDRIIALDGDTKNSTFS 348
Cdd:PRK05444 270 QP---------KSSK--------------------PGKPSYT--------KVFGETLCELAEKDPKIVAITAAMPEGTGL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 349 EIFKKEHPDRFIECYIAEQNMVSIAVGCATRNrTVPFCSTFAAFFTRAFDQIRM-AAISESNINLCGSHCGVSiGEDGPS 427
Cdd:PRK05444 313 VKFSKRFPDRYFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHdVALQNLPVTFAIDRAGLV-GADGPT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 428 QMALEDLAMFRSVPTSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENA-IIYNNNEDFQVGQAKVVLKSKDdqVTV 505
Cdd:PRK05444 391 HQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRGNGVgVELPELEPLPIGKGEVLREGED--VAI 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 506 IGAGVTLHEALAAAELLKkekiNIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVSSAVVGE-PGITV 584
Cdd:PRK05444 469 LAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLEFLADHgLDVPV 543
|
490 500 510
....*....|....*....|....*....|....*...
gi 4507521 585 THLAV--NRVPRsGKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:PRK05444 544 LNLGLpdEFIDH-GSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
216-620 |
8.26e-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: 174.43 E-value: 8.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 216 VDGHSVEELCKAFGQAKHQPTAII--AKTFKGRGIT-GVEDKESWHGkPLPKNMAeqiiqeiySQIQSKKKilatppqed 292
Cdd:COG1154 252 IDGHDLDALVETLRNAKDLKGPVLlhVVTKKGKGYApAEKDPDKFHG-VGPFDPE--------TGEPKKSK--------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 293 apsvdianirmPSLPSYkvgdkiaTrKAYGQALAKLGHASDRIIA-----LDGdtknsTFSEIFKKEHPDRFIECYIAEQ 367
Cdd:COG1154 314 -----------SSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERFPDRFFDVGIAEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 368 NMVSIAVGCATRNrTVPFCSTFAAFFTRAFDQIRM-AAISesniNLcgshcGVSI--------GEDGPSQMALEDLAMFR 438
Cdd:COG1154 370 HAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHdVALQ----NL-----PVTFaidraglvGADGPTHHGVFDLSYLR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 439 SVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSR--PENAIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEAL 516
Cdd:COG1154 440 CIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgnGPGVELPAELEPLPIGKGEVLREGKD--VAILAFGTMVAEAL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 517 AAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVSSAVVGEpGIT--VTHLAvnrVPR 594
Cdd:COG1154 518 EAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEFLADA-GLDvpVLRLG---LPD 592
|
410 420 430
....*....|....*....|....*....|
gi 4507521 595 S----GKPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:COG1154 593 RfiehGSRAELLAELGLDAEGIARAILELL 622
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
16-262 |
2.56e-41 |
|
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: 152.93 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LAE 94
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 95 AELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCLLGDGELSEGSVW 164
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPeFGHTAGVEVTTGPLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 165 EAMAFASIYKLDNLVAILDINRL---GQSDPAPLQHQmdiyQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQPTA 237
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQIsidGETKISFTEDT----AARFEAYGWHVIeVEDGHDVEAIAAAIEEAKaekDKPTL 238
|
250 260
....*....|....*....|....*
gi 4507521 238 IIAKTFKGRGITGVEDKESWHGKPL 262
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAPL 263
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
492-612 |
8.73e-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: 130.41 E-value: 8.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 492 AKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEA 571
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 4507521 572 VSSAVVGE----PGITVTHLAVNRVPRSGKPAELLKMFGIDRDAI 612
Cdd:pfam02780 80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-622 |
1.41e-34 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 139.09 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 129 LGAACGMAyTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKlDNLVAILDIN----------------RLGQSDP 192
Cdd:PRK12571 125 ISAALGFA-KARALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAAD-RRLIVILNDNemsiappvgalaaylsTLRSSDP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 193 -APLQHQMDIYQKRC-------------------------EAFGWHAI-IVDGHSVEELCKAFGQAKHQ---PTAIIAKT 242
Cdd:PRK12571 203 fARLRAIAKGVEERLpgplrdgarrarelvtgmigggtlfEELGFTYVgPIDGHDMEALLSVLRAARARadgPVLVHVVT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 243 FKGRGITGVE-DKESWHGkplpknmaeqiiqeiYSQIQskkkiLATPPQEDAPsvdianirmPSLPSYKvgdkiatrKAY 321
Cdd:PRK12571 283 EKGRGYAPAEaDEDKYHA---------------VGKFD-----VVTGLQKKSA---------PSAPSYT--------SVF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 322 GQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNrTVPFCSTFAAFFTRAFDQIR 401
Cdd:PRK12571 326 GEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 402 M-AAISESNINLCGSHCGVsIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAV-ELAANTKGICFIRTSRPE--N 477
Cdd:PRK12571 405 HdVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEgvG 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 478 AIIYNNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLIldsARATKGRI- 556
Cdd:PRK12571 484 VEIPAEGTILGIGKGRVPREGPD--VAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALT---DLLVRHHIv 558
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507521 557 LTVEDHYYEGGIGEAVSSAvvgepgITVTHLAVNRVP-----------RSGKPAELLKMFGIDRDAIAQAVRGLITK 622
Cdd:PRK12571 559 VIVEEQGAMGGFGAHVLHH------LADTGLLDGGLKlrtlglpdrfiDHASREEMYAEAGLTAPDIAAAVTGALAR 629
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-474 |
5.26e-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: 120.28 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 314 KIATRKAYGQALAKLGhasdriialdgdtknstfseifkkehpdrfIECYIAEQNMVSIAVGCATRNRtVPFCSTFAAFF 393
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 394 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTS 473
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 4507521 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 |
4.50e-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: 110.47 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 36 GHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHndrfVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSD--LDGHPVP 113
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEGGGGDL----VYFQGHASPGIYARAFLEGRLTEEQLDNFRQEVGGggLSSYPHP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 114 KQ--AFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDIN 185
Cdd:cd02017 107 WLmpDFWEFPTVSMGLGPIQAIYQARFNRYLedrglkDTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 186 RlgQSDPAPLQHQMDIYQkRCEAF----GWHAIIV--------------------------------------------- 216
Cdd:cd02017 187 L--QRLDGPVRGNGKIIQ-ELEGIfrgaGWNVIKViwgskwdellakdgggalrqrmeetvdgdyqtlkakdgayvrehf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 217 ---------------D---------GHSVEELCKAFGQA---KHQPTAIIAKTFKGRGItgvedKESWHGkplpKNMAEQ 269
Cdd:cd02017 264 fgkypelkalvtdlsDedlwalnrgGHDPRKVYAAYKKAvehKGKPTVILAKTIKGYGL-----GAAGEG----RNHAHQ 334
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
132-620 |
1.82e-21 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 98.54 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 132 ACGMAyTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKlDNLVAILDINrlgqsdpaplqhQMDI-------YQK 204
Cdd:PRK12315 122 ATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDN------------QMSIaenhgglYKN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 205 ---------RCE-----AFGWHAIIV-DGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGIT-GVEDKESWH-------- 258
Cdd:PRK12315 188 lkelrdtngQSEnnlfkAMGLDYRYVeDGNDIESLIEAFKEVKdiDHPIVLHIHTLKGKGYQpAEENKEAFHwhmpfdle 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 259 -GKPLPKNMAEQ----IIQEIYSQIQSKKKILATppqedapsvdianirmpslpsykvgdKIATRKAYGqalaklghasd 333
Cdd:PRK12315 268 tGQSKVPASGESyssvTLDYLLKKIKEGKPVVAI--------------------------NAAIPGVFG----------- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 334 riialdgdtknstFSEiFKKEHPDRFIECYIAEQNMVSIAVGCAtRNRTVPFCSTFAAFFTRAFDQIR--MAAISESNIN 411
Cdd:PRK12315 311 -------------LKE-FRKKYPDQYVDVGIAEQESVAFASGIA-ANGARPVIFVNSTFLQRAYDQLShdLAINNNPAVM 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 412 LCGshcGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPsdgvaTEKAVELA------ANTKGICFIRTsrPENAIIYNNNE 485
Cdd:PRK12315 376 IVF---GGSISGNDVTHLGIFDIPMISNIPNLVYLAP-----TTKEELIAmlewalTQHEHPVAIRV--PEHGVESGPTV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 486 DFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKE-KINIRVLDPFTIKPLDRKLiLDSARATKGRILTVEDHYY 564
Cdd:PRK12315 446 DTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVVTLEDGIL 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507521 565 EGGIGEAVSSaVVGEPGITVTHLA-----VNRVPrsgkPAELLKMFGIDRDAIAQAVRGLI 620
Cdd:PRK12315 525 DGGFGEKIAR-YYGNSDMKVLNYGakkefNDRVP----VEELYKRNHLTPEQIVEDILSVL 580
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
121-569 |
1.34e-20 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 95.94 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 121 ATGSLGQGLGAACGMAyTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASiYKLDNLVAILDINRL---------GQSD 191
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG-YLHSNMIVILNDNKQvslptanldGPTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 192 P-APLQHQMDIYQKRC-----------EAFGWHAI-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTFKGRGITGVED- 253
Cdd:PLN02234 253 PvGALSCALSRLQSNCgmiretsstlfEELGFHYVgPVDGHNIDDLVSILETLKSTktigPVLIHVVTEKGRGYPYAERa 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 254 KESWHGkplpknmaeqiiqeiysqiqskkkILATPPQEDAPSVDIANIRmpslpSYKvgdkiatrKAYGQALAKLGHASD 333
Cdd:PLN02234 333 DDKYHG------------------------VLKFDPETGKQFKNISKTQ-----SYT--------SCFVEALIAEAEADK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 334 RIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTvPFCSTFAAFFTRAFDQ-IRMAAISESNINL 412
Cdd:PLN02234 376 DIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQvVHDVDLQKLPVRF 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 413 CGSHCGVsIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA--NTKGICF-------IRTSRPENaiiyNN 483
Cdd:PLN02234 455 AIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCFryhrgngIGVSLPPG----NK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 484 NEDFQVGQAKVVlkSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEdhy 563
Cdd:PLN02234 530 GVPLQIGRGRIL--RDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE-VLITVE--- 603
|
....*.
gi 4507521 564 yEGGIG 569
Cdd:PLN02234 604 -EGSIG 608
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
351-577 |
8.38e-20 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 91.20 E-value: 8.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 351 FKKEHPDRFIECYIAEQNMVSIAVGCATrNRTVPFCS-TFAAFFTRAFDQIrmaaisesnIN-------LCGS--HCGVS 420
Cdd:PTZ00182 76 LDKYGPDRVFDTPITEQGFAGFAIGAAM-NGLRPIAEfMFADFIFPAFDQI---------VNeaakyryMSGGqfDCPIV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 421 I-GEDGPS-QMALEDL----AMFRSVPTSTVFYPSDgvatekavelAANTKGICF--IRTSRP----ENAIIYNN----- 483
Cdd:PTZ00182 146 IrGPNGAVgHGGAYHSqsfeAYFAHVPGLKVVAPSD----------PEDAKGLLKaaIRDPNPvvffEPKLLYREsvevv 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 484 -NEDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVE 560
Cdd:PTZ00182 216 pEADYTLplGKAKVVREGKD--VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVH 292
|
250
....*....|....*..
gi 4507521 561 DHYYEGGIGEAVSSAVV 577
Cdd:PTZ00182 293 EAPPTCGIGAEIAAQIM 309
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
12-569 |
8.41e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 90.34 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 12 LQALKDTANRLRISSIQATTAAGsGHPTSCCSAAEIMAVLFFhtmryksqdPRNPHNDRFVLSKGHAA------------ 79
Cdd:PLN02582 48 VKELKQLADELRSDVIFNVSKTG-GHLGSSLGVVELTVALHY---------VFNAPQDKILWDVGHQSyphkiltgrrdk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 80 -PILYAVWAEAGFLAEAEllnlrkisSDLD----GHpvpkqaftdvATGSLGQGLGAACGMAYTGKyfdkaSYRVYCLLG 154
Cdd:PLN02582 118 mHTMRQTNGLSGFTKRAE--------SEYDcfgtGH----------SSTTISAGLGMAVGRDLKGK-----KNNVVAVIG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 155 DGELSEGSVWEAMAFASiYKLDNLVAILDIN-------------------------RLGQSDPA---------------- 193
Cdd:PLN02582 175 DGAMTAGQAYEAMNNAG-YLDSDMIVILNDNkqvslptatldgpappvgalssalsRLQSSRPLrelrevakgvtkqigg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 194 ---PLQHQMDIYQKRC---------EAFGWHAI-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTFKGRGITGVEDK-E 255
Cdd:PLN02582 254 pmhELAAKVDEYARGMisgsgstlfEELGLYYIgPVDGHNIDDLVTILREVKSTkttgPVLIHVVTEKGRGYPYAERAaD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 256 SWHGkplpknmaeqiiqeiysqiqSKKKILATPPQEDAPSvdianiRMPSLPSYkvgdkiatrkaYGQALAKLGHASDRI 335
Cdd:PLN02582 334 KYHG--------------------VVKFDPATGKQFKVKA------KTQSYTTY-----------FAEALIAEAEVDKDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 336 IALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTvPFCSTFAAFFTRAFDQ-IRMAAISESNINLCG 414
Cdd:PLN02582 377 VAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQvVHDVDLQKLPVRFAM 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 415 SHCGVsIGEDGPSQMALEDLAMFRSVPTSTVFYPSDG------VATEKAVElaanTKGICF-------IRTSRPENaiiy 481
Cdd:PLN02582 456 DRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEaelfhmVATAAAID----DRPSCFryprgngIGVQLPPN---- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 482 NNNEDFQVGQAKVVLKSkdDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEd 561
Cdd:PLN02582 527 NKGIPIEVGKGRILLEG--ERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVE- 602
|
....*...
gi 4507521 562 hyyEGGIG 569
Cdd:PLN02582 603 ---EGSIG 607
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
351-576 |
4.83e-17 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 85.15 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 351 FKKEHPDRFIECYIAEQNMVSIAVGCATRNRTvPFCSTFAAFFTRAFDQIRMAAISESN-INLCGSHCGVsIGEDGPSQM 429
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 430 ALEDLAMFRSVPTSTVFYPSDGVATEKAVELAA--NTKGICFirtSRPENAIIYNN-----NEDFQVGQAKVVLKSKDdq 502
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCF---RFPRGSIVNMNylvptGLPIEIGRGRVLVEGQD-- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4507521 503 VTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYeGGIGEAVSSAV 576
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; ... |
121-243 |
5.63e-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: 78.69 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 121 ATGSLGQGLGAACGMAYTGKYFDKASYrVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDiNRLGQSDPAPLQHQMD 200
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPTSRQTAGT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4507521 201 IYQKRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 243
Cdd:cd02000 180 SIADRAAAYGIPGIRVDGNDVLAVYEAAKEAveraraGGGPTLIEAVTY 228
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
356-576 |
1.08e-14 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 75.53 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 356 PDRFIECYIAEQNMVSIAVGCATRN-RTVPFCSTFAaFFTRAFDQIRMAAISESNINlcGSHCGVSIGEDGP----SQMA 430
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAGlRPIVEFMTFN-FSMQAIDQIVNSAAKTNYMS--GGQLKCPIVFRGPngaaARVA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 431 LEDLAMFRS----VPTSTVFYPSdgvatekaveLAANTKG--ICFIRTSRP----ENAIIY-------NNNEDFQVGQAK 493
Cdd:PRK09212 127 AQHSQCYAAwyshIPGLKVVAPY----------FAADCKGllKTAIRDPNPviflENEILYghshevpEEEESIPIGKAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 494 VVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEAVS 573
Cdd:PRK09212 197 ILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAEIA 273
|
...
gi 4507521 574 SAV 576
Cdd:PRK09212 274 ALI 276
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
46-242 |
2.76e-13 |
|
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: 68.05 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 46 EIMAVLFFHTmryksqdprnPHNDRFVLSKGHAAPILYAVWAeagflaeaellnlrkissdldgHPVPKQAFTDVATGSL 125
Cdd:cd00568 1 RVLAALRAAL----------PEDAIVVNDAGNSAYWAYRYLP----------------------LRRGRRFLTSTGFGAM 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 126 GQGLGAACGMAYTGKyfDKasyRVYCLLGDGELSEGsvWEAMAFASIYKLdNLVAILDIN-----------RLGQSDPAP 194
Cdd:cd00568 49 GYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGL-PVIVVVFNNggygtirmhqeAFYGGRVSG 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 4507521 195 LQHQMDIYQKRCEAFGWHAIIVDghSVEELCKAFGQAK--HQPTAIIAKT 242
Cdd:cd00568 121 TDLSNPDFAALAEAYGAKGVRVE--DPEDLEAALAEALaaGGPALIEVKT 168
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
121-243 |
8.95e-13 |
|
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: 69.78 E-value: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 121 ATGSLGQGLGAACGMAYTGKYF--DKAsyrVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDiNRLGQSDPAPLQ-H 197
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAISTPVERQtA 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 4507521 198 QMDIYQkRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 243
Cdd:COG1071 201 VETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEAveraraGEGPTLIEAKTY 251
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
350-579 |
3.03e-12 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 68.31 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 350 IFKKEHPDRFIECYIAEQNMVSIAVGCATRN-RTVPFCSTFAaFFTRAFDQIRMAAiSESNInLCGSHCGVSIGEDGP-- 426
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHIINSA-AKTNY-MSAGQISVPIVFRGPng 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 427 ------SQMALEDLAMFRSVPTSTVFYPSDgvaTEKAVEL--AAntkgicfIRTSRP----ENAIIYNNN---------E 485
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYS---SEDARGLlkAA-------IRDPDPvvflENELLYGESfpvsaevldS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 486 DF--QVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHY 563
Cdd:PLN02683 214 SFvlPIGKAKIEREGKD--VTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|....*.
gi 4507521 564 YEGGIGEAVSSAVVGE 579
Cdd:PLN02683 291 PQHGVGAEICASVVEE 306
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
461-585 |
1.27e-11 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 67.25 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 461 AANTKGI--CFIRTSRP----ENAIIYNNN------EDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAELLKKEK 526
Cdd:PRK11892 289 AADAKGLlkAAIRDPNPviflENEILYGQSfdvpklDDFVLpiGKARIHREGKD--VTIVSFSIGMTYALKAAEELAKEG 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507521 527 INIRVLDPFTIKPLDRKLILDSARATkGRILTVEDHYYEGGIGEAVSSAVVGE-------PGITVT 585
Cdd:PRK11892 367 IDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARVMEQafdyldaPVLRVT 431
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
122-247 |
3.21e-10 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 59.87 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 122 TGSLGQGLGAACGMAYTGKYFDKaSYRVYCLLGDGELSEGSVWEAMAFASiYKLDNLVAILDINRLGQSDPAPLQHQMdi 201
Cdd:cd02007 74 TGHSSTSISAALGMAVARDLKGK-KRKVIAVIGDGALTGGMAFEALNNAG-YLKSNMIVILNDNEMSISPNVGTPGNL-- 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4507521 202 yqkrCEAFGWHAI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRG 247
Cdd:cd02007 150 ----FEELGFRYIgPVDGHNIEALIKVLKEVKdlKGPVLLHVVTKKGKG 194
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
36-187 |
4.38e-07 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 53.01 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 36 GHPTSCCSAAEIMAVLFFHTMRYKSQDprnpHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKissDLDG------ 109
Cdd:PRK13012 116 GHIASYASAADLFEVGFNHFFRGRDDA----GGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQ---EIGGpglssy 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 110 -HPVPKQAFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAIL 182
Cdd:PRK13012 189 pHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLqhrglkDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLVFVI 268
|
....*..
gi 4507521 183 DIN--RL 187
Cdd:PRK13012 269 NCNlqRL 275
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
36-187 |
7.14e-07 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 52.45 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 36 GHPTSCCSAAEIMAVLFFHTMRYKSQdprnPHNDRFVLSKGHAAPILYA-VWAEaGFLAEAELLNLRK------ISSdld 108
Cdd:PRK09405 108 GHISSFASSATLYEVGFNHFFRAPNE----PHGGDLVFFQGHASPGIYArAFLE-GRLTEEQLDNFRQevdgkgLSS--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 109 gHPVPK--QAFTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCLLGDGELSE----GsvweAMAFASIYK 174
Cdd:PRK09405 180 -YPHPWlmPDFWQFPTVSMG--LGPIMAIyqARFLKYLenrglkDTSDQKVWAFLGDGEMDEpeslG----AISLAAREK 252
|
170
....*....|....*
gi 4507521 175 LDNLVAILDIN--RL 187
Cdd:PRK09405 253 LDNLIFVINCNlqRL 267
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
358-576 |
1.37e-05 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 47.43 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 358 RFIECYIAEQNMVSIAVGCA-TRNRTVpFCSTFAAFFTRAFDQI--RMAAISESNinlcGSHCGVSIGEDGPS----QMA 430
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAmTGLRPI-VEGMNMGFLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 431 LEDL----AMFRSVPTSTVFypsdgvatekAVELAANTKGI--CFIRTSRP----ENAIIYNNNED-------FQVGQAK 493
Cdd:CHL00144 127 AEHSqrleSYFQSVPGLQIV----------ACSTPYNAKGLlkSAIRSNNPviffEHVLLYNLKEEipdneylLPLEKAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 494 VVLKSKDdqVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKgRILTVEDHYYEGGIGEAVS 573
Cdd:CHL00144 197 VVRPGND--ITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIGAELI 273
|
...
gi 4507521 574 SAV 576
Cdd:CHL00144 274 AQI 276
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
36-187 |
1.40e-05 |
|
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: 48.15 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 36 GHPTSCCSAAEIMAVLFFHTMRYKSQdprnPHNDRFVLSKGHAAPILYAvwaEA---GFLAEAELLNLRKissDLDGH-- 110
Cdd:COG2609 109 GHISSFASAATLYEVGFNHFFRGPDH----PGGGDLVYFQGHASPGIYA---RAfleGRLTEEQLDNFRQ---EVDGKgl 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 111 ---PVPKQA--FTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCLLGDGELSE----GsvweAMAFASIY 173
Cdd:COG2609 179 ssyPHPWLMpdFWQFPTVSMG--LGPINAIyqARFMKYLhnrglkDTSDRKVWAFLGDGEMDEpeslG----AISLAARE 252
|
170
....*....|....*.
gi 4507521 174 KLDNLVAILDIN--RL 187
Cdd:COG2609 253 KLDNLIFVINCNlqRL 268
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
121-244 |
2.33e-05 |
|
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: 46.55 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 121 ATGSLGQGLGAACGMAYTGKYfDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDnLVAILDINRLGQSDPAPLQHQMD 200
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKY-RGKKEVAITLYGDGAANQGDFFEGLNFAALWKLP-VIFVCENNQYGISTPAERASAST 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 4507521 201 IYQKRCEAFGWHAIIVDGHSVEELCKAFGQAK------HQPTAIIAKTFK 244
Cdd:pfam00676 177 TYADRARGYGIPGLHVDGMDPLAVYQASKFAAerartgKGPFLIELVTYR 226
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
125-279 |
7.73e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 45.24 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 125 LGQGLGAACGMAYTGKYF-----DKASYRVY-CLLGDGELSEGSVWEAMAFASIYKL-------DNLVAILDINRLGQSD 191
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRqqvlkEVQPLRVTaCFFGDGTTNNGQFFECLNMAVLWKLpiifvveNNQWAIGMAHHRSTSI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 192 PaplqhqmDIYqKRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTFKGRG--------ITGVEDKESW 257
Cdd:CHL00149 210 P-------EIH-KKAEAFGLPGIEVDGMDVLAVREVAKEAverarqGDGPTLIEALTYRFRGhsladpdeLRSKQEKEAW 281
|
170 180
....*....|....*....|...
gi 4507521 258 HGKPLPKNMAEQII-QEIYSQIQ 279
Cdd:CHL00149 282 VARDPIKKLKSYIIdNELASQKE 304
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
125-247 |
2.11e-04 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 44.16 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 125 LGQGLGAACGMAYTGKYFDKASYRVYC------LLGDGELSEGSVWEAMAFASIYKL-------DNLVAILDINRLGQSD 191
Cdd:PLN02374 196 IGEGIPVATGAAFSSKYRREVLKEESCddvtlaFFGDGTCNNGQFFECLNMAALWKLpivfvveNNLWAIGMSHLRATSD 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507521 192 PaplqhqmDIYqKRCEAFGWHAIIVDGH---SVEELCK-AFGQAKH--QPTAIIAKTFKGRG 247
Cdd:PLN02374 276 P-------EIW-KKGPAFGMPGVHVDGMdvlKVREVAKeAIERARRgeGPTLVECETYRFRG 329
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
113-231 |
1.27e-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: 41.68 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 113 PKQAFTDVATGSLGQGLGAACG--MAYTGKyfdkasyRVYCLLGDG-------ELsegsvweamAFASIYKLDNLVAILD 183
Cdd:COG0028 402 PRRFLTSGGLGTMGYGLPAAIGakLARPDR-------PVVAITGDGgfqmnlqEL---------ATAVRYGLPVKVVVLN 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4507521 184 INRLGqsdpAPLQHQMDIYQKRC--------------EAFGWHAIIVDghSVEELCKAFGQA 231
Cdd:COG0028 466 NGGLG----MVRQWQELFYGGRYsgtdlpnpdfaklaEAFGAKGERVE--TPEELEAALEEA 521
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
330-450 |
4.19e-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: 38.09 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507521 330 HASDRIIALDGDTKNSTFSEIfkKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESN 409
Cdd:cd06586 10 WGVRHVFGYPGDEISSLLDAL--REGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAEHLP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 4507521 410 INLCGSHCGVSiGEDGPSQMALEDLAMFRSVPTSTVFYPSD 450
Cdd:cd06586 88 VVFLIGARGIS-AQAKQTFQSMFDLGMYRSIPEANISSPSP 127
|
|
| |
