|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
40-652 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 574.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 40 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWA 119
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 120 EAGF-LPEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCMLGDG 188
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 189 EVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDvYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH--Q 266
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 267 PTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQiiqeiysqvqsKKKILATPPqedapsvdianirmptppnykvgdk 346
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 347 iatRKAYGLALAKLGHASDRIIALDGDTKNSTFSELF------KKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCST 420
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 421 FAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA-NTKGI 499
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 500 CFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKlild 579
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 580 caratkgriltvEDHYYEGGIGEAVSAAVVGEPGVT----------VTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVK 649
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 1937369892 650 GLV 652
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
52-303 |
2.74e-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: 394.18 E-value: 2.74e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 52 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLN 131
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 132 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNL 210
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 211 VAIFDINRLGQSDPAPLQHQVDVYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGITGIEDKE 287
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 1937369892 288 AWHGKPLPKNMAEQII 303
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
345-652 |
6.73e-117 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 351.31 E-value: 6.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 345 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAF 424
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 425 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFI 502
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 503 RTSRPENAIIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCAR 582
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369892 583 ATkGRILTVEDHYYEGGIGEAVSAAVVGEPGVTVTRLAVSQVP-RSGKPAELLKMFGIDKDAIVQAVKGLV 652
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
48-651 |
1.89e-77 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 259.65 E-value: 1.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 48 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRykaLDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 123
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLK---FNPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 124 LPEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCMLGDGEVSEG 193
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 194 SVWEAMAFAGIYKLDNLVAIFDINRLgQSDPAPLQHQVDVYQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQPTA 269
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 270 IIAKTFKGRGITGIEDKEAWHGKPLPK------------NMAEQII-QEIY------------SQVQSKKKILAT----P 320
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAykkkY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 321 PQEDAPSVDIANIRMP-----TPPNYKVGDK-IATRKAYGLALAKLGHASDRIIALDGDTKNSTFSEL-----FKKEHPD 389
Cdd:TIGR00232 317 PELAAEFTRRLSGELPadwdkQLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHENPLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 390 RFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMF 469
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 470 RSVPMSTVFYPSDGVATEKAVELAantkgicfIRTSRPENAIIYS-----NNEDFQVGQAK----VVLKSKDDQVTVIGA 540
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSrqnlpQLEESSLEKVLkggyVLKDSKGPDLILIAT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 541 GVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDK------KLILDCARAtkgrILTVED------HYYEGGIGEAVSAAV 608
Cdd:TIGR00232 549 GSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDKqdeeyrESVLPANVT----RLAIEAgaadewYKYAGLVGAILGMDS 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1937369892 609 VGEpgvtvtrlavsqvprSGKPAELLKMFGIDKDAIVQAVKGL 651
Cdd:TIGR00232 625 FGE---------------SAPGDKLFEEFGFTVENVVAKAKKL 652
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
345-508 |
4.74e-50 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 171.96 E-value: 4.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 345 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPD---RFIECYIAEQNMVSIAVGCATRDR-TVPFCST 420
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 421 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGI 499
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 1937369892 500 --CFIRTSRPE 508
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
346-506 |
1.52e-31 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 119.51 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 346 KIATRKAYGLALAKLGhasdriialdgdtknstfselfkkehpdrfIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAFF 425
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 426 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTS 505
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 1937369892 506 R 506
Cdd:smart00861 131 R 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
40-652 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 574.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 40 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWA 119
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 120 EAGF-LPEAELLNLRKISSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCMLGDG 188
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 189 EVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDvYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH--Q 266
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 267 PTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQiiqeiysqvqsKKKILATPPqedapsvdianirmptppnykvgdk 346
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAA-----------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 347 iatRKAYGLALAKLGHASDRIIALDGDTKNSTFSELF------KKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCST 420
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 421 FAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA-NTKGI 499
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 500 CFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKlild 579
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 580 caratkgriltvEDHYYEGGIGEAVSAAVVGEPGVT----------VTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVK 649
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 1937369892 650 GLV 652
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
52-303 |
2.74e-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: 394.18 E-value: 2.74e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 52 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLN 131
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 132 LRKISSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNL 210
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 211 VAIFDINRLGQSDPAPLQHQVDVYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGITGIEDKE 287
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 1937369892 288 AWHGKPLPKNMAEQII 303
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
345-652 |
6.73e-117 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 351.31 E-value: 6.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 345 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAF 424
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 425 FT-RAFDQIRMA-AISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFI 502
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 503 RTSRPENAIIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCAR 582
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369892 583 ATkGRILTVEDHYYEGGIGEAVSAAVVGEPGVTVTRLAVSQVP-RSGKPAELLKMFGIDKDAIVQAVKGLV 652
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
40-313 |
3.89e-111 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 335.51 E-value: 3.89e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 40 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWA 119
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 120 EAGFLPEAELLNLRKISSDLDGHPVPKQafT---DVATGSLGQGLGAACGMAYTGKYfDKASYRVYCMLGDGEVSEGSVW 196
Cdd:COG3959 81 EKGYFPKEELATFRKLGSRLQGHPDMKK--TpgvEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 197 EAMAFAGIYKLDNLVAIFDINRLgQSD--------PAPLqhqvdvyQKRCEAFGWHAIIVDGHSVEELCKAFGQAKH--- 265
Cdd:COG3959 158 EAAMAAAHYKLDNLIAIVDRNGL-QIDgptedvmsLEPL-------AEKWEAFGWHVIEVDGHDIEALLAALDEAKAvkg 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1937369892 266 QPTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQIIQEIYSQVQSK 313
Cdd:COG3959 230 KPTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELGDY 277
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
48-651 |
1.89e-77 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 259.65 E-value: 1.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 48 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRykaLDPRNPH---NDRFVLSKGHAAPILYAVWAEAGF- 123
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLK---FNPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 124 LPEAELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCMLGDGEVSEG 193
Cdd:TIGR00232 78 LSIEDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 194 SVWEAMAFAGIYKLDNLVAIFDINRLgQSDPAPLQHQVDVYQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQPTA 269
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRI-SIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 270 IIAKTFKGRGITGIEDKEAWHGKPLPK------------NMAEQII-QEIY------------SQVQSKKKILAT----P 320
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPLGDeevaltkknlgwNYNPFEIpQEVYdhfkktvkergaKAEQEWNELFAAykkkY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 321 PQEDAPSVDIANIRMP-----TPPNYKVGDK-IATRKAYGLALAKLGHASDRIIALDGDTKNSTFSEL-----FKKEHPD 389
Cdd:TIGR00232 317 PELAAEFTRRLSGELPadwdkQLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWkgsgdLHENPLG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 390 RFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMF 469
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 470 RSVPMSTVFYPSDGVATEKAVELAantkgicfIRTSRPENAIIYS-----NNEDFQVGQAK----VVLKSKDDQVTVIGA 540
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSrqnlpQLEESSLEKVLkggyVLKDSKGPDLILIAT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 541 GVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDK------KLILDCARAtkgrILTVED------HYYEGGIGEAVSAAV 608
Cdd:TIGR00232 549 GSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDKqdeeyrESVLPANVT----RLAIEAgaadewYKYAGLVGAILGMDS 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1937369892 609 VGEpgvtvtrlavsqvprSGKPAELLKMFGIDKDAIVQAVKGL 651
Cdd:TIGR00232 625 FGE---------------SAPGDKLFEEFGFTVENVVAKAKKL 652
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
51-563 |
6.74e-69 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 236.88 E-value: 6.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 51 ANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPEAEL 129
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 130 LNLRKISSDLDGHPvpKQAFT---DVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCMLGDGEVSEGSVWE 197
Cdd:PTZ00089 90 KNFRQLGSRTPGHP--ERHITpgvEVTTGPLGQGIANAVGLAiaekhlaakFNRPGHPIFDNYVYVICGDGCLQEGVSQE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 198 AMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDVyQKRCEAFGWHAIIVD-GHS-VEELCKAFGQAKH---QPTAIIA 272
Cdd:PTZ00089 168 ALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDV-EKKYEAYGWHVIEVDnGNTdFDGLRKAIEEAKKskgKPKLIIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 273 KTFKGRGiTGIEDKEAWHGKPLP----KNMAEQI-------------IQEIYSQVQSKKKILATPPQE-------DAPSV 328
Cdd:PTZ00089 247 KTTIGYG-SSKAGTEKVHGAPLGdediAQVKELFgldpekkfhvseeVRQFFEQHVEKKKENYEAWKKrfakytaAFPKE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 329 DIANIRM---PTPPNYK--------VGDKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFS-----ELFKKEHPD-RF 391
Cdd:PTZ00089 326 AQAIERRfkgELPPGWEkklpkyttNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTrpkeaNDFTKASPEgRY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 392 IECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRS 471
Cdd:PTZ00089 406 IRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 472 VPMSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRpENAIIYSNNEDFQVGQAKVVLKSKDD--QVTVIGAGVTLHEAL 548
Cdd:PTZ00089 486 TPNLLVIRPADGTETSGAYALAlANAKTPTILCLSR-QNTPPLPGSSIEGVLKGAYIVVDFTNspQLILVASGSEVSLCV 564
|
570
....*....|....*
gi 1937369892 549 AAAEMLKKEkIGVRV 563
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), ... |
351-506 |
4.44e-66 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 213.84 E-value: 4.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 351 KAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDrTVPFCSTFAAFFTRAFD 430
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369892 431 QIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSR 506
Cdd:cd07033 80 QIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
48-652 |
1.33e-61 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 217.18 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 48 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYkalDPRNPH--N-DRFVLSKGHAAPILYAVWAEAGF- 123
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKH---NPANPKwpNrDRFVLSAGHGSMLLYSLLHLTGYd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 124 LPEAELLNLRKISSDLDGHP-------VpkqaftDVATGSLGQGLGAACGMAYTGKY----FDKASY-----RVYCMLGD 187
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPeyghtpgV------ETTTGPLGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 188 GEVSEGSVWEAMAFAGIYKLDNLVAIFDINR--------LGQSDpaplqhqvDVyQKRCEAFGWHAI-IVDGHSVEELCK 258
Cdd:COG0021 156 GDLMEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdLAFSE--------DV-AKRFEAYGWHVIrVEDGHDLEAIDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 259 AFGQAKH---QPTAIIAKTFKGRGITGIEDKEAWHGKPL-PKNMAE------------QIIQEIYSQVQSKKKILATP-- 320
Cdd:COG0021 227 AIEAAKAetdKPTLIICKTIIGYGSPNKQGTAKAHGAPLgAEEIAAtkealgwppepfEVPDEVYAHWRAAGERGAAAea 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 321 -------------PQEDAPSVDIANIRMP-----TPPNYKVGDK-IATRKAYGLALAKLGhasDRIIALDG---DTKNST 378
Cdd:COG0021 307 ewnerfaayaaayPELAAELERRLAGELPedwdaALPAFEADAKgVATRKASGKVLNALA---PVLPELIGgsaDLAGSN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 379 FSEL-----FKKEHPD-RFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAF--FTRAfdQIRMAAIsesninlcgSHCG 450
Cdd:COG0021 384 KTTIkgagsFSPEDPSgRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFsdYMRP--AIRLAAL---------MKLP 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 451 V-------SI--GEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANtkgicfiRTSRPeNAIIYS------- 514
Cdd:COG0021 453 ViyvfthdSIglGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLALE-------RKDGP-TALILSrqnlptl 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 515 NNEDFQVGQAK----VVLKSKDD-QVTVIGAGVTLHEALAAAEMLKKEKIGVRV-----LDPFTIKPLD-KKLILDcaRA 583
Cdd:COG0021 525 DRTAAAAEGVAkgayVLADAEGTpDVILIATGSEVSLAVEAAELLAAEGIKVRVvsmpsWELFEAQDAAyRESVLP--PA 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369892 584 TKGRIltvedhyyeggigeAVSAAV-------VGEPGVTVTrlavsqVPR---SGKPAELLKMFGIDKDAIVQAVKGLV 652
Cdd:COG0021 603 VRARV--------------AVEAGVtdgwykyVGLDGAVIG------IDTfgaSAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PLN02790 |
PLN02790 |
transketolase |
55-652 |
1.27e-58 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 208.72 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 55 RISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYkalDPRNP---HNDRFVLSKGHAAPILYAVWAEAGF--LPEAEL 129
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKY---NPKNPywfNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 130 LNLRKISSDLDGHPvpkQAFT----DVATGSLGQGLGAACGMAYTGKY----FDKA-----SYRVYCMLGDGEVSEGSVW 196
Cdd:PLN02790 79 KQFRQWGSRTPGHP---ENFEtpgiEVTTGPLGQGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 197 EAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDVyQKRCEAFGWHAIIVDG--HSVEELCKAFGQAK---HQPTAII 271
Cdd:PLN02790 156 EAASLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDV-DKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKavtDKPTLIK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 272 AKTFKGRGITGIEDKEAWHGKPL-PKNMAE------------QIIQEIYSQVQSKKKILATP---------------PQE 323
Cdd:PLN02790 235 VTTTIGYGSPNKANSYSVHGAALgEKEVDAtrknlgwpyepfHVPEDVKSHWSKHTKEGAALeaewnakfaeykkkyPEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 324 DAPSVDIANIRMPTP-----PNYKVGDKI-ATRKAYGLALAKLGHASDRIIALDGDTKNSTFSEL-----FKKEHP-DRF 391
Cdd:PLN02790 315 AAELKSLISGELPSGwekalPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPeERN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 392 IECYIAEQNMVSIAVGCAT-RDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFR 470
Cdd:PLN02790 395 VRFGVREHGMGAICNGIALhSSGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 471 SVPMSTVFYPSDGVATEKAVELA-ANTKG---ICFIRTSRP-----------ENAIIYSNNEDfqvgqakvvlKSKDDqV 535
Cdd:PLN02790 475 AMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPnlpgtsiegveKGGYVISDNSS----------GNKPD-L 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 536 TVIGAGVTLHEALAAAEMLKKEKIGVRVLDpftikpldkkliLDCARAtkgrILTVEDHYYEGGIGEAVSAAVVGEPGVT 615
Cdd:PLN02790 544 ILIGTGSELEIAAKAAKELRKEGKKVRVVS------------MVCWEL----FEEQSDEYKESVLPSSVTARVSVEAGST 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1937369892 616 V----------TRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVKGLV 652
Cdd:PLN02790 608 FgwekyvgskgKVIGVDRFGASAPAGILYKEFGFTVENVVAAAKSLL 654
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
345-508 |
4.74e-50 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 171.96 E-value: 4.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 345 DKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPD---RFIECYIAEQNMVSIAVGCATRDR-TVPFCST 420
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 421 FAAFFTRAFDQIR-MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGI 499
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 1937369892 500 --CFIRTSRPE 508
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
161-652 |
1.31e-47 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 176.43 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 161 LGAACGMAYTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKlDNLVAIFDINRLGQSDP--------APLQHQVd 232
Cdd:PRK05444 123 ISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDNEMSISPNvgalsnylARLRSST- 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 233 VYqkrcEAFGWHAI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGITGIE-DKEAWHGkpLPKnmaeqiiqeiyS 308
Cdd:PRK05444 201 LF----EELGFNYIgPIDGHDLDALIETLKNAKdlKGPVLLHVVTKKGKGYAPAEaDPIKYHG--VGK-----------F 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 309 QVQSKKKILATPPQedapsvdianirmptPPNYKvgdkiatrKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHP 388
Cdd:PRK05444 264 DPETGEQPKSSKPG---------------KPSYT--------KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 389 DRFIECYIAEQNMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQIRM-AAISESNINLCGSHCGVSiGEDGPSQMALEDLA 467
Cdd:PRK05444 321 DRYFDVGIAEQHAVTFAAGLAT-EGLKPVVAIYSTFLQRAYDQVIHdVALQNLPVTFAIDRAGLV-GADGPTHQGAFDLS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 468 MFRSVPMSTVFYPSDGVATEKAVELA-ANTKGICFIRTSRPENA-IIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLH 545
Cdd:PRK05444 399 YLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRGNGVgVELPELEPLPIGKGEVLREGED--VAILAFGTMLA 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 546 EALAAAEMLKKekigVRVLDPFTIKPLDKKLILDCARATKgRILTVEDHYYEGGIGEAVSAAVVGE-PGVTVTRLAVSQ- 623
Cdd:PRK05444 477 EALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLEFLADHgLDVPVLNLGLPDe 551
|
490 500 510
....*....|....*....|....*....|
gi 1937369892 624 -VPRsGKPAELLKMFGIDKDAIVQAVKGLV 652
Cdd:PRK05444 552 fIDH-GSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
248-652 |
6.59e-45 |
|
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: 169.42 E-value: 6.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 248 VDGHSVEELCKAFGQAKHQPTAII--AKTFKGRGIT-GIEDKEAWHGkPLPKNMAeqiiqeiySQVQSKKKilatppqed 324
Cdd:COG1154 252 IDGHDLDALVETLRNAKDLKGPVLlhVVTKKGKGYApAEKDPDKFHG-VGPFDPE--------TGEPKKSK--------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 325 apsvdianirmPTPPNYkvgdkiaTrKAYGLALAKLGHASDRIIA-----LDGdtknsTFSELFKKEHPDRFIECYIAEQ 399
Cdd:COG1154 314 -----------SSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERFPDRFFDVGIAEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 400 NMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQIRM-AAISesniNLcgshcGVSI--------GEDGPSQMALEDLAMFR 470
Cdd:COG1154 370 HAVTFAAGLAT-EGLKPVVAIYSTFLQRAYDQVIHdVALQ----NL-----PVTFaidraglvGADGPTHHGVFDLSYLR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 471 SVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSR--PENAIIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEAL 548
Cdd:COG1154 440 CIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgnGPGVELPAELEPLPIGKGEVLREGKD--VAILAFGTMVAEAL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 549 AAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATKgRILTVEDHYYEGGIGEAVSAAVVGEpGVT--VTRLAVSQ--V 624
Cdd:COG1154 518 EAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEFLADA-GLDvpVLRLGLPDrfI 595
|
410 420
....*....|....*....|....*...
gi 1937369892 625 PRsGKPAELLKMFGIDKDAIVQAVKGLV 652
Cdd:COG1154 596 EH-GSRAELLAELGLDAEGIARAILELL 622
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
48-294 |
3.89e-43 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 158.32 E-value: 3.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 48 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPE 126
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 127 AELLNLRKISSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCMLGDGEVSEGSVW 196
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPeFGHTAGVEVTTGPLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 197 EAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDVyQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK---HQPTAIIA 272
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDT-AARFEAYGWHVIeVEDGHDVEAIAAAIEEAKaekDKPTLIKC 241
|
250 260
....*....|....*....|..
gi 1937369892 273 KTFKGRGITGIEDKEAWHGKPL 294
Cdd:pfam00456 242 RTVIGYGSPNKQGTHDVHGAPL 263
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
524-644 |
3.24e-37 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 134.65 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 524 AKVVLKSKDDQVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATkGRILTVEDHYYEGGIGEA 603
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1937369892 604 VSAAVVGE----PGVTVTRLAVSQVPRSGKPAELLKMFGIDKDAI 644
Cdd:pfam02780 80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
161-654 |
3.33e-33 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 135.24 E-value: 3.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 161 LGAACGMAyTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFD---------------INRLGQSD-- 223
Cdd:PRK12571 125 ISAALGFA-KARALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAADRRLIVILNDnemsiappvgalaayLSTLRSSDpf 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 224 --------------PAPLQ---HQVDVYQKRC-------EAFGWHAI-IVDGHSVEELCKAFGQAKHQ---PTAIIAKTF 275
Cdd:PRK12571 204 arlraiakgveerlPGPLRdgaRRARELVTGMigggtlfEELGFTYVgPIDGHDMEALLSVLRAARARadgPVLVHVVTE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 276 KGRGITGIE-DKEAWHGkplpknmaeqiiqeiYSQVQskkkiLATPPQEDAPsvdianirmPTPPNYKvgdkiatrKAYG 354
Cdd:PRK12571 284 KGRGYAPAEaDEDKYHA---------------VGKFD-----VVTGLQKKSA---------PSAPSYT--------SVFG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 355 LALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDrTVPFCSTFAAFFTRAFDQIRM 434
Cdd:PRK12571 327 EELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLH 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 435 -AAISESNINLCGSHCGVsIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAV-ELAANTKGICFIRTSRPE--NA 510
Cdd:PRK12571 406 dVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEgvGV 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 511 IIYSNNEDFQVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLIldcARATKGRI-L 589
Cdd:PRK12571 485 EIPAEGTILGIGKGRVPREGPD--VAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALT---DLLVRHHIvV 559
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369892 590 TVEDHYYEGGIGEAVSAAvVGEPGVTVTRLAVSQV---PR---SGKPAELLKMFGIDKDAIVQAVKGLVTK 654
Cdd:PRK12571 560 IVEEQGAMGGFGAHVLHH-LADTGLLDGGLKLRTLglpDRfidHASREEMYAEAGLTAPDIAAAVTGALAR 629
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
346-506 |
1.52e-31 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 119.51 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 346 KIATRKAYGLALAKLGhasdriialdgdtknstfselfkkehpdrfIECYIAEQNMVSIAVGCATRDRtVPFCSTFAAFF 425
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 426 TRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTS 505
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 1937369892 506 R 506
Cdd:smart00861 131 R 131
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
68-301 |
1.32e-23 |
|
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: 103.15 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 68 GHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHndrfVLSKGHAAPILYAVWAEAGFLPEAELLNLRKISSD--LDGHPVP 145
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEGGGGDL----VYFQGHASPGIYARAFLEGRLTEEQLDNFRQEVGGggLSSYPHP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 146 KQ--AFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDIN 217
Cdd:cd02017 107 WLmpDFWEFPTVSMGLGPIQAIYQARFNRYLedrglkDTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 218 RlgQSDPAPLQHQVDVYQkRCEAF----GWHAIIV--------------------------------------------- 248
Cdd:cd02017 187 L--QRLDGPVRGNGKIIQ-ELEGIfrgaGWNVIKViwgskwdellakdgggalrqrmeetvdgdyqtlkakdgayvrehf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 249 ---------------D---------GHSVEELCKAFGQA---KHQPTAIIAKTFKGRGItgiedKEAWHGkplpKNMAEQ 301
Cdd:cd02017 264 fgkypelkalvtdlsDedlwalnrgGHDPRKVYAAYKKAvehKGKPTVILAKTIKGYGL-----GAAGEG----RNHAHQ 334
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
164-652 |
4.73e-21 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 97.38 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 164 ACGMAyTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKlDNLVAIFDINRLGQSDpaplqHQVDVYQK------- 236
Cdd:PRK12315 122 ATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAE-----NHGGLYKNlkelrdt 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 237 --RCE-----AFGWHAIIV-DGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGIT-GIEDKEAWH---------GKPLPK 296
Cdd:PRK12315 195 ngQSEnnlfkAMGLDYRYVeDGNDIESLIEAFKEVKdiDHPIVLHIHTLKGKGYQpAEENKEAFHwhmpfdletGQSKVP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 297 NMAEQ----IIQEIYSQVQSKKKILAtppqedapsvdianIRMPTPpnykvgdkiatrKAYGLalaklghasdriialdg 372
Cdd:PRK12315 275 ASGESyssvTLDYLLKKIKEGKPVVA--------------INAAIP------------GVFGL----------------- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 373 dtknstfsELFKKEHPDRFIECYIAEQNMVSIAVGCAtRDRTVPFCSTFAAFFTRAFDQIR--MAAISESNINLCGshcG 450
Cdd:PRK12315 312 --------KEFRKKYPDQYVDVGIAEQESVAFASGIA-ANGARPVIFVNSTFLQRAYDQLShdLAINNNPAVMIVF---G 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 451 VSIGEDGPSQMALEDLAMFRSVPMSTVFYPsdgvaTEKAVELA------ANTKGICFIRTsrPENAIIYSNNEDFQVGQA 524
Cdd:PRK12315 380 GSISGNDVTHLGIFDIPMISNIPNLVYLAP-----TTKEELIAmlewalTQHEHPVAIRV--PEHGVESGPTVDTDYSTL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 525 KVVLKSKDDQVTVIGAGVTLHEALAAAEMLKKE-KIGVRVLDPFTIKPLDKKLiLDCARATKGRILTVEDHYYEGGIGEA 603
Cdd:PRK12315 453 KYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVVTLEDGILDGGFGEK 531
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1937369892 604 VsAAVVGEPGVTV-----TRLAVSQVPrsgkPAELLKMFGIDKDAIVQAVKGLV 652
Cdd:PRK12315 532 I-ARYYGNSDMKVlnygaKKEFNDRVP----VEELYKRNHLTPEQIVEDILSVL 580
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
153-601 |
3.27e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 91.70 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 153 ATGSLGQGLGAACGMAyTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGiYKLDNLVAIFDINRL---------GQSD 223
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG-YLHSNMIVILNDNKQvslptanldGPTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 224 P-APLQHQVDVYQKRC-----------EAFGWHAI-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTFKGRGITGIED- 285
Cdd:PLN02234 253 PvGALSCALSRLQSNCgmiretsstlfEELGFHYVgPVDGHNIDDLVSILETLKSTktigPVLIHVVTEKGRGYPYAERa 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 286 KEAWHGkplpknmaeqiiqeiysqvqskkkILATPPQEDAPSVDIANIRMPTppnykvgdkiatrKAYGLALAKLGHASD 365
Cdd:PLN02234 333 DDKYHG------------------------VLKFDPETGKQFKNISKTQSYT-------------SCFVEALIAEAEADK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 366 RIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQ-IRMAAISESNINL 444
Cdd:PLN02234 376 DIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLAC-EGLKPFCTIYSSFMQRAYDQvVHDVDLQKLPVRF 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 445 CGSHCGVsIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA--NTKGICF-------IRTSRPENaiiySN 515
Cdd:PLN02234 455 AIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCFryhrgngIGVSLPPG----NK 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 516 NEDFQVGQAKVVlkSKDDQVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATKgRILTVEdhy 595
Cdd:PLN02234 530 GVPLQIGRGRIL--RDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE-VLITVE--- 603
|
....*.
gi 1937369892 596 yEGGIG 601
Cdd:PLN02234 604 -EGSIG 608
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
382-609 |
1.10e-18 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 88.11 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 382 LFKKEHPDRFIECYIAEQNMVSIAVGCATRDRTvPFCS-TFAAFFTRAFDQIrmaaisesnIN-------LCGS--HCGV 451
Cdd:PTZ00182 75 LLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLR-PIAEfMFADFIFPAFDQI---------VNeaakyryMSGGqfDCPI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 452 SI-GEDGPS-QMALEDL----AMFRSVPMSTVFYPSDgvatekavelAANTKGICF--IRTSRP----ENAIIY------ 513
Cdd:PTZ00182 145 VIrGPNGAVgHGGAYHSqsfeAYFAHVPGLKVVAPSD----------PEDAKGLLKaaIRDPNPvvffEPKLLYresvev 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 514 SNNEDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATkGRILTV 591
Cdd:PTZ00182 215 VPEADYTLplGKAKVVREGKD--VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIV 291
|
250
....*....|....*...
gi 1937369892 592 EDHYYEGGIGEAVSAAVV 609
Cdd:PTZ00182 292 HEAPPTCGIGAEIAAQIM 309
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
44-601 |
1.80e-17 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 86.49 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 44 LQALKDTANRLRISSIQATTAAGsGHPTSCCSAAEIMAVLFFhtmrykaldPRNPHNDRFVLSKGHAA------------ 111
Cdd:PLN02582 48 VKELKQLADELRSDVIFNVSKTG-GHLGSSLGVVELTVALHY---------VFNAPQDKILWDVGHQSyphkiltgrrdk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 112 -PILYAVWAEAGFLPEAEllnlrkisSDLD----GHpvpkqaftdvATGSLGQGLGAACGMAYTGKyfdkaSYRVYCMLG 186
Cdd:PLN02582 118 mHTMRQTNGLSGFTKRAE--------SEYDcfgtGH----------SSTTISAGLGMAVGRDLKGK-----KNNVVAVIG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 187 DGEVSEGSVWEAMAFAGIYKLDNLVAIFD------------------------INRLGQSDPA----------------- 225
Cdd:PLN02582 175 DGAMTAGQAYEAMNNAGYLDSDMIVILNDnkqvslptatldgpappvgalssaLSRLQSSRPLrelrevakgvtkqiggp 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 226 --PLQHQVDVYQKRC---------EAFGWHAI-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTFKGRGITGIE---DK 286
Cdd:PLN02582 255 mhELAAKVDEYARGMisgsgstlfEELGLYYIgPVDGHNIDDLVTILREVKSTkttgPVLIHVVTEKGRGYPYAEraaDK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 287 eaWHGkplpknmaeqiiqeiysqvqskkkilatppqedapsvdIANIRMPTPPNYKVGDKIATRKAY-GLALAKLGHASD 365
Cdd:PLN02582 335 --YHG--------------------------------------VVKFDPATGKQFKVKAKTQSYTTYfAEALIAEAEVDK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 366 RIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATrDRTVPFCSTFAAFFTRAFDQ-IRMAAISESNINL 444
Cdd:PLN02582 375 DVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLAC-EGLKPFCAIYSSFLQRGYDQvVHDVDLQKLPVRF 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 445 CGSHCGVsIGEDGPSQMALEDLAMFRSVPMSTVFYPSDG------VATEKAVElaanTKGICFiRTSRPeNAI---IYSN 515
Cdd:PLN02582 454 AMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEaelfhmVATAAAID----DRPSCF-RYPRG-NGIgvqLPPN 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 516 NED--FQVGQAKVVLKSkdDQVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATKgRILTVEd 593
Cdd:PLN02582 527 NKGipIEVGKGRILLEG--ERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVE- 602
|
....*...
gi 1937369892 594 hyyEGGIG 601
Cdd:PLN02582 603 ---EGSIG 607
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
156-605 |
3.37e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 82.46 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 156 SLGQGLGAACGMAYTGKyfdkaSYRVYCMLGDGEVSEGSVWEAMAFAGiYKLDNLVAIFDINR------LGQSDPAPLQH 229
Cdd:PLN02225 194 SISAGLGLAVARDIKGK-----RDRVVAVIDNATITAGQAYEAMSNAG-YLDSNMIVILNDSRhslhpnMEEGSKASISA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 230 QVDVYQKRCEAFGWHAIivdGHSVEELCKAFGQAKHQPTAIIAKTFKG----RGITGIEDKEAWHGKPLPKNMAEQII-- 303
Cdd:PLN02225 268 LSSIMSKIQSSKIFRKF---RELAKAMTKRIGKGMYEWAAKVDEYARGmvgpTGSTLFEELGLYYIGPVDGHNIEDLVcv 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 304 -QEIySQVQSKKKILATPPQEDapsvdiaNIRMPTPPNYKVGDKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSEL 382
Cdd:PLN02225 345 lREV-SSLDSMGPVLVHVITEE-------NRDAETGKNIMVKDRRTYSDCFVEALVMEAEKDRDIVVVHAGMEMDASLIT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 383 FKKEHPDRFIECYIAEQNMVSIAVGCATRDRTvPFCSTFAAFFTRAFDQIRMAAISESN-INLCGSHCGVsIGEDGPSQM 461
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVITSAGL-VGSDGPVQC 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 462 ALEDLAMFRSVPMSTVFYPSDGVATEKAVELAA--NTKGICFirtSRPENAIIYSN-----NEDFQVGQAKVVLKSKDdq 534
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCF---RFPRGSIVNMNylvptGLPIEIGRGRVLVEGQD-- 569
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369892 535 VTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATKgRILTVEDHYYeGGIGEAVS 605
Cdd:PLN02225 570 VALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHK-FLITVEEGCV-GGFGSHVA 638
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
153-275 |
4.21e-16 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 79.46 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 153 ATGSLGQGLGAACGMAYTGKYFDKASYrVYCMLGDGEVSEGSVWEAMAFAGIYKLDnlvAIFDI--NRLGQSDPAPLQHQ 230
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFAALWKLP---VIFVCenNGYAISTPTSRQTA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1937369892 231 VDVYQKRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 275
Cdd:cd02000 178 GTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAveraraGGGPTLIEAVTY 228
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
153-275 |
1.05e-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: 72.87 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 153 ATGSLGQGLGAACGMAYTGKYF--DKAsyrVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDiNRLGQSDPAPLQ-H 229
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAISTPVERQtA 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1937369892 230 QVDVYQkRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 275
Cdd:COG1071 201 VETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEAveraraGEGPTLIEAKTY 251
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
382-608 |
9.28e-13 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 69.75 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 382 LFKKEHPDRFIECYIAEQNMVSIAVGCAtrdrtvpFCS--------TFAaFFTRAFDQIRMAAISESNINlcGSHCGVSI 453
Cdd:PRK09212 44 LLEQFGPKRVIDTPITEHGFAGLAVGAA-------FAGlrpivefmTFN-FSMQAIDQIVNSAAKTNYMS--GGQLKCPI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 454 GEDGP----SQMALEDLAMFRS----VPMSTVFYPSdgvatekaveLAANTKG--ICFIRTSRP----ENAIIYSNNEDF 519
Cdd:PRK09212 114 VFRGPngaaARVAAQHSQCYAAwyshIPGLKVVAPY----------FAADCKGllKTAIRDPNPviflENEILYGHSHEV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 520 -------QVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATkGRILTVE 592
Cdd:PRK09212 184 peeeesiPIGKAAILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVE 260
|
250
....*....|....*.
gi 1937369892 593 DHYYEGGIGEAVSAAV 608
Cdd:PRK09212 261 EGWPFAGVGAEIAALI 276
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
493-649 |
1.84e-12 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 69.95 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 493 AANTKGI--CFIRTSRP----ENAIIYSNN------EDFQV--GQAKVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEK 558
Cdd:PRK11892 289 AADAKGLlkAAIRDPNPviflENEILYGQSfdvpklDDFVLpiGKARIHREGKD--VTIVSFSIGMTYALKAAEELAKEG 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 559 IGVRVLDPFTIKPLDKKLILDCARATkGRILTVEDHYYEGGIGEAVSAAVVGE-------PgvtVTRLAVSQVPRsgkP- 630
Cdd:PRK11892 367 IDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARVMEQafdyldaP---VLRVTGKDVPM---Py 439
|
170 180
....*....|....*....|
gi 1937369892 631 -AELLKMFGIDKDAIVQAVK 649
Cdd:PRK11892 440 aANLEKLALPSVAEVVEAVK 459
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
90-274 |
2.64e-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: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 90 YKALDPRNPHNDRFVLSKGHAAPILYAVWAeagflpeaellnlrkissdldgHPVPKQAFTDVATGSLGQGLGAACGMAY 169
Cdd:cd00568 3 LAALRAALPEDAIVVNDAGNSAYWAYRYLP----------------------LRRGRRFLTSTGFGAMGYGLPAAIGAAL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 170 TGKyfDKasyRVYCMLGDGEVSEGsvWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDV----------YQKRCE 239
Cdd:cd00568 61 AAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRvsgtdlsnpdFAALAE 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937369892 240 AFGWHAIIVDghSVEELCKAFGQAK--HQPTAIIAKT 274
Cdd:cd00568 134 AYGAKGVRVE--DPEDLEAALAEALaaGGPALIEVKT 168
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
382-649 |
1.67e-11 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 66.38 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 382 LFKKEHPDRFIECYIAEQNMVSIAVGCATRD-RTVPFCSTFAaFFTRAFDQIRMAAiSESNInLCGSHCGVSIGEDGP-- 458
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHIINSA-AKTNY-MSAGQISVPIVFRGPng 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 459 ------SQMALEDLAMFRSVPMSTVFYPSDgvaTEKAVEL--AAntkgicfIRTSRP----ENAIIYSNN---------E 517
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYS---SEDARGLlkAA-------IRDPDPvvflENELLYGESfpvsaevldS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 518 DF--QVGQAKVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATkGRILTVEDHY 595
Cdd:PLN02683 214 SFvlPIGKAKIEREGKD--VTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369892 596 YEGGIGEAVSAAVVGEP----GVTVTRLAVSQVPRSgKPAELLKMFGIDKDAIVQAVK 649
Cdd:PLN02683 291 PQHGVGAEICASVVEESfdylDAPVERIAGADVPMP-YAANLERLALPQVEDIVRAAK 347
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
154-279 |
1.43e-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: 57.94 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 154 TGSLGQGLGAACGMAYTGKYFDKaSYRVYCMLGDGEVSEGSVWEAMAFAGiYKLDNLVAIFDINRLGQSdpaplqHQVDV 233
Cdd:cd02007 74 TGHSSTSISAALGMAVARDLKGK-KRKVIAVIGDGALTGGMAFEALNNAG-YLKSNMIVILNDNEMSIS------PNVGT 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1937369892 234 YQKRCEAFGWHAI-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRG 279
Cdd:cd02007 146 PGNLFEELGFRYIgPVDGHNIEALIKVLKEVKdlKGPVLLHVVTKKGKG 194
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
68-219 |
3.13e-07 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 53.61 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 68 GHPTSCCSAAEIMAVLFFHTMRykalDPRNPHNDRFVLSKGHAAPILYA-VWAEaGFLPEAELLNLRK------ISSdld 140
Cdd:PRK09405 108 GHISSFASSATLYEVGFNHFFR----APNEPHGGDLVFFQGHASPGIYArAFLE-GRLTEEQLDNFRQevdgkgLSS--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 141 gHPVPK--QAFTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCMLGDGEVSE----GsvweAMAFAGIYK 206
Cdd:PRK09405 180 -YPHPWlmPDFWQFPTVSMG--LGPIMAIyqARFLKYLenrglkDTSDQKVWAFLGDGEMDEpeslG----AISLAAREK 252
|
170
....*....|....*..
gi 1937369892 207 LDNLvaIFDIN----RL 219
Cdd:PRK09405 253 LDNL--IFVINcnlqRL 267
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
68-217 |
8.31e-07 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 52.24 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 68 GHPTSCCSAAEIMAVLFFHTMRYKAldprNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLNLRKissDLDG------ 141
Cdd:PRK13012 116 GHIASYASAADLFEVGFNHFFRGRD----DAGGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQ---EIGGpglssy 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 142 -HPVPKQAFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVaiF 214
Cdd:PRK13012 189 pHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLqhrglkDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLV--F 266
|
...
gi 1937369892 215 DIN 217
Cdd:PRK13012 267 VIN 269
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
68-219 |
4.58e-06 |
|
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]; Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 442021 [Multi-domain] Cd Length: 891 Bit Score: 50.07 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 68 GHPTSCCSAAEIMAVLFFHTMRykalDPRNPHNDRFVLSKGHAAPILYAvwaEA---GFLPEAELLNLRKissDLDGH-- 142
Cdd:COG2609 109 GHISSFASAATLYEVGFNHFFR----GPDHPGGGDLVYFQGHASPGIYA---RAfleGRLTEEQLDNFRQ---EVDGKgl 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 143 ---PVPKQA--FTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCMLGDGEVSE----GsvweAMAFAGIY 205
Cdd:COG2609 179 ssyPHPWLMpdFWQFPTVSMG--LGPINAIyqARFMKYLhnrglkDTSDRKVWAFLGDGEMDEpeslG----AISLAARE 252
|
170
....*....|....*...
gi 1937369892 206 KLDNLvaIFDIN----RL 219
Cdd:COG2609 253 KLDNL--IFVINcnlqRL 268
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
157-311 |
2.04e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 47.17 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 157 LGQGLGAACGMAYTGKYF-----DKASYRVY-CMLGDGEVSEGSVWEAMAFAGIYKL-------DNLVAIFDINRLGQSd 223
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRqqvlkEVQPLRVTaCFFGDGTTNNGQFFECLNMAVLWKLpiifvveNNQWAIGMAHHRSTS- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 224 paplqhQVDVYqKRCEAFGWHAIIVDGHSVEELCKAFGQA------KHQPTAIIAKTFKGRG--------ITGIEDKEAW 289
Cdd:CHL00149 209 ------IPEIH-KKAEAFGLPGIEVDGMDVLAVREVAKEAverarqGDGPTLIEALTYRFRGhsladpdeLRSKQEKEAW 281
|
170 180
....*....|....*....|...
gi 1937369892 290 HGKPLPKNMAEQII-QEIYSQVQ 311
Cdd:CHL00149 282 VARDPIKKLKSYIIdNELASQKE 304
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
153-276 |
7.77e-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: 45.01 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 153 ATGSLGQGLGAACGMAYTGKYfDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDnlvAIFDI--NRLGQSDPAPLQHQ 230
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKY-RGKKEVAITLYGDGAANQGDFFEGLNFAALWKLP---VIFVCenNQYGISTPAERASA 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1937369892 231 VDVYQKRCEAFGWHAIIVDGHSVEELCKAFGQAK------HQPTAIIAKTFK 276
Cdd:pfam00676 175 STTYADRARGYGIPGLHVDGMDPLAVYQASKFAAerartgKGPFLIELVTYR 226
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
390-653 |
2.62e-04 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 43.57 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 390 RFIECYIAEQNMVSIAVGCA-TRDRTVpFCSTFAAFFTRAFDQI--RMAAISESNinlcGSHCGVSIGEDGPS----QMA 462
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAmTGLRPI-VEGMNMGFLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 463 LEDL----AMFRSVP-MSTVfypsdgvatekAVELAANTKGI--CFIRTSRP----ENAIIYSNNED-------FQVGQA 524
Cdd:CHL00144 127 AEHSqrleSYFQSVPgLQIV-----------ACSTPYNAKGLlkSAIRSNNPviffEHVLLYNLKEEipdneylLPLEKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 525 KVVLKSKDdqVTVIGAGVTLHEALAAAEMLKKEKIGVRVLDPFTIKPLDKKLILDCARATKgRILTVEDHYYEGGIGEAV 604
Cdd:CHL00144 196 EVVRPGND--ITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIGAEL 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1937369892 605 SAAVV----GEPGVTVTRLAVSQVPR--SGKpaeLLKMFGIDKDAIVQAVKGLVT 653
Cdd:CHL00144 273 IAQINehlfDELDAPIVRLSSQDVPTpyNGP---LEEATVIQPAQIIEAVEQIIT 324
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
157-279 |
5.18e-04 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 43.01 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 157 LGQGLGAACGMAYTGKYFDKASYRVYCM------LGDGEVSEGSVWEAMAFAGIYKL-------DNLVAIFDINRLGQSD 223
Cdd:PLN02374 196 IGEGIPVATGAAFSSKYRREVLKEESCDdvtlafFGDGTCNNGQFFECLNMAALWKLpivfvveNNLWAIGMSHLRATSD 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369892 224 PaplqhqvDVYqKRCEAFGWHAIIVDGH---SVEELCK-AFGQAKH--QPTAIIAKTFKGRG 279
Cdd:PLN02374 276 P-------EIW-KKGPAFGMPGVHVDGMdvlKVREVAKeAIERARRgeGPTLVECETYRFRG 329
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
145-263 |
9.54e-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: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369892 145 PKQAFTDVATGSLGQGLGAACG--MAYTGKyfdkasyRVYCMLGDGevseG---SVWEaMAFAGIYKLDNLVAIFDINRL 219
Cdd:COG0028 402 PRRFLTSGGLGTMGYGLPAAIGakLARPDR-------PVVAITGDG----GfqmNLQE-LATAVRYGLPVKVVVLNNGGL 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369892 220 GqsdpAPLQHQVDVYQKR--------------CEAFGWHAIIVDghSVEELCKAFGQA 263
Cdd:COG0028 470 G----MVRQWQELFYGGRysgtdlpnpdfaklAEAFGAKGERVE--TPEELEAALEEA 521
|
|
| |
