|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-538 |
5.55e-132 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 396.43 E-value: 5.55e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 1 MSVLFFYIMRYKQSDPENPDNDRFVLAK----------------------------------------RLSFVDVATGWL 40
Cdd:PRK05899 41 AYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllhlagydlsiddlknfrqlgsktpghpeygHTPGVETTTGPL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 41 GQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPaE 111
Cdd:PRK05899 121 GQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTE-G 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 112 HCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKhKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKL 191
Cdd:PRK05899 200 WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST-KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 192 IesqiqtsrNLDPqppiedspevnitdvrmtsppdyrvgdkiatRKACGLALAKLGYANNRVVVLDGD------TRYSTF 265
Cdd:PRK05899 279 L--------GWDY-------------------------------RKASGKALNALAKALPELVGGSADlagsnnTKIKGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 266 SEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGAS 345
Cdd:PRK05899 320 KDFAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 346 QMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAK-GMCFIRTTRPETMVIY-TPQERFEIGQAKVLRHCvsDKVTV 423
Cdd:PRK05899 400 HQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdGPSALVLTRQNLPVLErTAQEEGVAKGGYVLRDD--PDVIL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 424 IGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVAtivssakategriitvEDHYPQGGIGEAVCAAVSMDPDI--- 500
Cdd:PRK05899 478 IATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ----------------DAAYKESVLPAAVTARVAVEAGVadg 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 225637463 501 -------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCML 538
Cdd:PRK05899 542 wykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
231-535 |
1.49e-111 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 333.98 E-value: 1.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 231 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 310
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 311 LT-RAFDHIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFI 388
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 389 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAK 468
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225637463 469 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 535
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
1-189 |
1.29e-75 |
|
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: 239.71 E-value: 1.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 1 MSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------------RL---------SFVDVATGWLG 41
Cdd:cd02012 29 LAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktfrqlgsRLpghpeygltPGVEVTTGSLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 42 QGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRC 121
Cdd:cd02012 109 QGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLIAIVDSNRIQIDGPTDDILFTEDLAKKF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225637463 122 EAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAII 189
Cdd:cd02012 188 EAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
231-397 |
6.67e-47 |
|
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: 161.56 E-value: 6.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 231 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 306
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 307 FAAFLTRAFDHIRIG-GLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAV--ALAANAK 383
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAIRRDGR 160
|
170
....*....|....
gi 225637463 384 GMCFIRTTRPETMV 397
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
232-392 |
1.28e-28 |
|
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: 110.27 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 232 KIATRKACGLALAKLGyannrvvvldgdtrystfseifnkeyperfIECFMAEQNMVSVALGCASRGRtIAFASTFAAFL 311
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 312 TRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTT 391
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 225637463 392 R 392
Cdd:smart00861 131 R 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-538 |
5.55e-132 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 396.43 E-value: 5.55e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 1 MSVLFFYIMRYKQSDPENPDNDRFVLAK----------------------------------------RLSFVDVATGWL 40
Cdd:PRK05899 41 AYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllhlagydlsiddlknfrqlgsktpghpeygHTPGVETTTGPL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 41 GQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPaE 111
Cdd:PRK05899 121 GQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTE-G 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 112 HCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKhKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKL 191
Cdd:PRK05899 200 WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST-KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 192 IesqiqtsrNLDPqppiedspevnitdvrmtsppdyrvgdkiatRKACGLALAKLGYANNRVVVLDGD------TRYSTF 265
Cdd:PRK05899 279 L--------GWDY-------------------------------RKASGKALNALAKALPELVGGSADlagsnnTKIKGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 266 SEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGAS 345
Cdd:PRK05899 320 KDFAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 346 QMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAK-GMCFIRTTRPETMVIY-TPQERFEIGQAKVLRHCvsDKVTV 423
Cdd:PRK05899 400 HQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdGPSALVLTRQNLPVLErTAQEEGVAKGGYVLRDD--PDVIL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 424 IGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVAtivssakategriitvEDHYPQGGIGEAVCAAVSMDPDI--- 500
Cdd:PRK05899 478 IATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ----------------DAAYKESVLPAAVTARVAVEAGVadg 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 225637463 501 -------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCML 538
Cdd:PRK05899 542 wykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
231-535 |
1.49e-111 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 333.98 E-value: 1.49e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 231 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 310
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 311 LT-RAFDHIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFI 388
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 389 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAK 468
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225637463 469 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 535
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
1-189 |
1.29e-75 |
|
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: 239.71 E-value: 1.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 1 MSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------------RL---------SFVDVATGWLG 41
Cdd:cd02012 29 LAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktfrqlgsRLpghpeygltPGVEVTTGSLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 42 QGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRC 121
Cdd:cd02012 109 QGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLIAIVDSNRIQIDGPTDDILFTEDLAKKF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225637463 122 EAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAII 189
Cdd:cd02012 188 EAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
1-197 |
3.97e-60 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 199.92 E-value: 3.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 1 MSVLFFYIMRYKQSDPENPDNDRFVLAK------------RLSF---------------------------VDVATGWLG 41
Cdd:COG3959 41 LAALYFKVMNIDPKNPDWPDRDRFILSKghaapalyavlaEKGYfpkeelatfrklgsrlqghpdmkktpgVEMSTGSLG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 42 QGLGVACGMAYTGKYfDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGalPAEHCINIY--QR 119
Cdd:COG3959 121 QGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDG--PTEDVMSLEplAE 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225637463 120 RCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIESQIQ 197
Cdd:COG3959 198 KWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELG 275
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
237-392 |
9.20e-60 |
|
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: 194.58 E-value: 9.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 237 KACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFD 316
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225637463 317 HIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR 392
Cdd:cd07033 80 QIRHdVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
231-397 |
6.67e-47 |
|
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: 161.56 E-value: 6.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 231 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 306
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 307 FAAFLTRAFDHIRIG-GLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAV--ALAANAK 383
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAIRRDGR 160
|
170
....*....|....
gi 225637463 384 GMCFIRTTRPETMV 397
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-538 |
1.12e-42 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 160.63 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 122 EAFGWNtYV--VDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWHAkpmpreradaiikliesqiqt 198
Cdd:PRK05444 203 EELGFN-YIgpIDGHDLDALIETLKNAKDLKG-PVLLHVVTKKGKGyAPAEADPIKYHG--------------------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 199 srnldpqppiedspevnitdvrmTSPPDYRVGDKIATRKAC--------GLALAKLGYANNRVVVLDGDTRYSTFSEIFN 270
Cdd:PRK05444 260 -----------------------VGKFDPETGEQPKSSKPGkpsytkvfGETLCELAEKDPKIVAITAAMPEGTGLVKFS 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 271 KEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFDHI----------------RiGGLaesniniigsh 334
Cdd:PRK05444 317 KRFPDRYFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVihdvalqnlpvtfaidR-AGL----------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 335 cgvsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANA-KGMCFIRTTRPE-TMVIYTPQERFEIGQAKV 412
Cdd:PRK05444 384 ----VGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYdDGPIAIRYPRGNgVGVELPELEPLPIGKGEV 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 413 LRHcvSDKVTVIGAGITVYEALAAADELSKqdifIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCA 492
Cdd:PRK05444 460 LRE--GEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLE 532
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 225637463 493 AVS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 538
Cdd:PRK05444 533 FLAdHGLDVPVLNL---GLPDEfidhGSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
122-538 |
3.21e-42 |
|
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: 159.79 E-value: 3.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 122 EAFGWNtYV--VDGRDVEALCQVFWQASQVKhKPTAVVAKTFKGRG-TPSIEDAESWHAkpmpreradaiikliesqiqt 198
Cdd:COG1154 242 EELGFK-YIgpIDGHDLDALVETLRNAKDLK-GPVLLHVVTKKGKGyAPAEKDPDKFHG--------------------- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 199 srnldpQPPIEdsPEVNITDVRMTSPPDYrvgdkiaTrKACGLALAKLGYANNRVVV-----LDGdtrysTFSEIFNKEY 273
Cdd:COG1154 299 ------VGPFD--PETGEPKKSKSSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERF 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 274 PERFIECFMAEQNMVSVALGCASRGRTIAFA--STFaafLTRAFDHI----------------RiGGLaesniniigshc 335
Cdd:COG1154 358 PDRFFDVGIAEQHAVTFAAGLATEGLKPVVAiySTF---LQRAYDQVihdvalqnlpvtfaidR-AGL------------ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 336 gvsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR-PETMV-IYTPQERFEIGQAKVL 413
Cdd:COG1154 422 ---VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgNGPGVeLPAELEPLPIGKGEVL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 414 RHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCAA 493
Cdd:COG1154 499 RE--GKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEF 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 225637463 494 VS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 538
Cdd:COG1154 576 LAdAGLDVPVLRL---GLPDRfiehGSRAELLAELGLDAEGIARAILELL 622
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
408-530 |
4.80e-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: 4.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 408 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIG 487
Cdd:pfam02780 1 GKAEILRE--GDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 225637463 488 EAVCAAVS----MDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHI 530
Cdd:pfam02780 78 SEVAAALAeeafDGLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
3-538 |
1.96e-34 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 137.88 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 3 VLFFYIMRYKQSDPENPDNDRFVL----AKRLSF------------------------------------VDVATGWLGQ 42
Cdd:PTZ00089 41 ILWSEVMKYNPKDPRWINRDRFVLsnghASALLYsmlhltgydlsmedlknfrqlgsrtpghperhitpgVEVTTGPLGQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 43 GLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHC 113
Cdd:PTZ00089 121 GIANAVGLAIAEKHlaakFNRPGHpifdnYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 114 INIyQRRCEAFGWNTYVVD--GRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTpSIEDAESWHAKPMPRERADAIIKL 191
Cdd:PTZ00089 201 EDV-EKKYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYGS-SKAGTEKVHGAPLGDEDIAQVKEL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 192 IesqiqtsrNLDPQPPIEDSPEV--------------------NITDVRMTSP----------------------PDYRV 229
Cdd:PTZ00089 279 F--------GLDPEKKFHVSEEVrqffeqhvekkkenyeawkkRFAKYTAAFPkeaqaierrfkgelppgwekklPKYTT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 230 GDK-IATRKACGLALAKLGYANNRVVVLDGD------TRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIA 302
Cdd:PTZ00089 351 NDKaIATRKASENVLNPLFQILPELIGGSADltpsnlTRPKEANDFTKASPEGRYIRFGVREHAMCAIMNGIAAHGGFIP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 303 FASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALA-AN 381
Cdd:PTZ00089 431 FGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYALAlAN 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 382 AKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHC-VSDKVTVIGAGITVYEALAAADELSKqDIFIRVI-----DLFTI 455
Cdd:PTZ00089 511 AKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFtNSPQLILVASGSEVSLCVEAAKALSK-ELNVRVVsmpcwELFDQ 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 456 KPLDVATIVssakategriitvedhYPQGGIGE-AVCAAVSMDPDIQVH-SLAVSGVPQSGKSEELLDMYGISARHIIVA 533
Cdd:PTZ00089 590 QSEEYQQSV----------------LPSGGVPVlSVEAYVSFGWEKYSHvHVGISGFGASAPANALYKHFGFTVENVVEK 653
|
....*
gi 225637463 534 VKCML 538
Cdd:PTZ00089 654 ARALA 658
|
|
| PLN02790 |
PLN02790 |
transketolase |
3-452 |
3.53e-29 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 122.05 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 3 VLFFYIMRYKQSDPENPDNDRFVLA-------------------------KRL------------SF----VDVATGWLG 41
Cdd:PLN02790 29 VLYDEVMKYNPKNPYWFNRDRFVLSaghgcmlqyallhlagydsvqmedlKQFrqwgsrtpghpeNFetpgIEVTTGPLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 42 QGLGVACGMAYTGKY----FDRA-----SYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRL---GHSGALP 109
Cdd:PLN02790 109 QGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISNEAASLAGHWGLGKLIVLYDDNHIsidGDTEIAF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 110 AEHCIniyqRRCEAFGWNTYVVDG--RDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADA 187
Cdd:PLN02790 189 TEDVD----KRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEKEVDA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 188 iikliesqiqTSRNLD-PQPPIEDSPEVN--------------------------------------ITDVRMT----SP 224
Cdd:PLN02790 265 ----------TRKNLGwPYEPFHVPEDVKshwskhtkegaaleaewnakfaeykkkypeeaaelkslISGELPSgwekAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 225 PDYRVGDKI-ATRK---ACGLALAKL------GYAN----NRVVVLD-GDtrystfseiFNKEYP-ERFIECFMAEQNMV 288
Cdd:PLN02790 335 PTFTPEDPAdATRNlsqKCLNALAKVlpgligGSADlassNMTLLKDfGD---------FQKDTPeERNVRFGVREHGMG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 289 SVALGCASRGRT-IAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPT 367
Cdd:PLN02790 406 AICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNILMLRPA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 368 DAVSTEHAVALA-ANAKG---MCFIRTTRPETMViyTPQERFEIGQAKVLRHCVSDK--VTVIGAGITVYEALAAADELS 441
Cdd:PLN02790 486 DGNETAGAYKVAvTNRKRptvLALSRQKVPNLPG--TSIEGVEKGGYVISDNSSGNKpdLILIGTGSELEIAAKAAKELR 563
|
570
....*....|.
gi 225637463 442 KQDIFIRVIDL 452
Cdd:PLN02790 564 KEGKKVRVVSM 574
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
232-392 |
1.28e-28 |
|
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: 110.27 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 232 KIATRKACGLALAKLGyannrvvvldgdtrystfseifnkeyperfIECFMAEQNMVSVALGCASRGRtIAFASTFAAFL 311
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 312 TRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTT 391
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 225637463 392 R 392
Cdd:smart00861 131 R 131
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
283-495 |
8.18e-26 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 107.79 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 283 AEQNMVSVALGCASRG-RTIAFAsTFAAFLTRAFDHI---------RIGGLAESNInIIGSHCGVSVGDdGA--SQMaLE 350
Cdd:COG0022 59 SEAGIVGAAIGAALAGlRPVVEI-QFADFIYPAFDQIvnqaaklryMSGGQFKVPM-VIRTPYGGGIGA-GAqhSQS-LE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 351 diAMFRTIPKCTIFYPtdavSTehavalAANAKGM---CfIRTTRP----ETMVIYT-----PQERFEI--GQAKVLRHc 416
Cdd:COG0022 135 --AWFAHIPGLKVVAP----ST------PYDAKGLlkaA-IRDDDPviflEHKRLYRlkgevPEEDYTVplGKARVVRE- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225637463 417 vSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVCAAVS 495
Cdd:COG0022 201 -GTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEIAARIA 277
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
128-538 |
1.42e-25 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 110.97 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 128 TYV--VDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAEswhakpmprERADAIIKLiesQIQTSRNLDPQ 205
Cdd:PRK12571 248 TYVgpIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADE---------DKYHAVGKF---DVVTGLQKKSA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 206 PpiedspevnitdvrmtSPPDYRvgdkiatrKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQ 285
Cdd:PRK12571 316 P----------------SAPSYT--------SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 286 NMVSVALGCASRGrTIAFASTFAAFLTRAFDHIrigglaesnINIIGSH-CGVS--------VGDDGASQMALEDIAMFR 356
Cdd:PRK12571 372 HAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQL---------LHDVALQnLPVRfvldraglVGADGATHAGAFDLAFLT 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 357 TIPKCTIFYPTDAVSTEHAVALA-ANAKGMCFIRTTRPETMVIYTPqERFEIGQAKVLRHCVSDK-VTVIGAGITVYEAL 434
Cdd:PRK12571 442 NLPNMTVMAPRDEAELRHMLRTAaAHDDGPIAVRFPRGEGVGVEIP-AEGTILGIGKGRVPREGPdVAILSVGAHLHECL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 435 AAADELSKQDIFIRVIDLFTIKPLDVATIvssAKATEGRI-ITVEDHYPQGGIGEAVCAAVS----MDPDIQVHSLavsG 509
Cdd:PRK12571 521 DAADLLEAEGISVTVADPRFVKPLDEALT---DLLVRHHIvVIVEEQGAMGGFGAHVLHHLAdtglLDGGLKLRTL---G 594
|
410 420 430
....*....|....*....|....*....|...
gi 225637463 510 VP----QSGKSEELLDMYGISARHIIVAVKCML 538
Cdd:PRK12571 595 LPdrfiDHASREEMYAEAGLTAPDIAAAVTGAL 627
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-453 |
4.71e-22 |
|
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: 100.08 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 3 VLFFYIMRYkqsDPENP---DNDRFVLA------------------------KRL----------------SFVDVATGW 39
Cdd:COG0021 39 VLWTKFLKH---NPANPkwpNRDRFVLSaghgsmllysllhltgydlslddlKNFrqlgsktpghpeyghtPGVETTTGP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 40 LGQGLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRlghsgalpa 110
Cdd:COG0021 116 LGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNG--------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 111 ehcINI-----------YQRRCEAFGWNTY-VVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAK 178
Cdd:COG0021 187 ---ISIdgdtdlafsedVAKRFEAYGWHVIrVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 179 PMPrerADAIIKLIEsqiqtsrNLD-PQPPIEDSPEV-NITD-------------------------------VRMTSP- 224
Cdd:COG0021 264 PLG---AEEIAATKE-------ALGwPPEPFEVPDEVyAHWRaagergaaaeaewnerfaayaaaypelaaelERRLAGe 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 225 ---------PDYRVGDK-IATRKACGLALAKLGYANNRVVV----LDGdtrySTFSEI-----FNKEYPE-RFIECFMAE 284
Cdd:COG0021 334 lpedwdaalPAFEADAKgVATRKASGKVLNALAPVLPELIGgsadLAG----SNKTTIkgagsFSPEDPSgRNIHFGVRE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 285 QNMVSVALGCASRGRTIAFASTFAAFltraFDH----IRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPK 360
Cdd:COG0021 410 HAMGAIMNGIALHGGLRPYGGTFLVF----SDYmrpaIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASLRAIPN 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 361 CTIFYPTDAVSTEHAVALAANakgmcfiRTTRPeTMVIYT----PQERFEIGQAK-------VLRHCVSD-KVTVIGAGI 428
Cdd:COG0021 486 LDVIRPADANETAAAWKLALE-------RKDGP-TALILSrqnlPTLDRTAAAAEgvakgayVLADAEGTpDVILIATGS 557
|
570 580 590
....*....|....*....|....*....|
gi 225637463 429 TVYEALAAADELSKQDIFIRVI-----DLF 453
Cdd:COG0021 558 EVSLAVEAAELLAAEGIKVRVVsmpswELF 587
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
274-494 |
1.31e-21 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 96.20 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 274 PERFIECFMAEQNMVSVALGCASRG-RTIAfASTFAAFLTRAFDHI---------RIGGLAESNInIIGSHCGVsVGDDG 343
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNGlRPIA-EFMFADFIFPAFDQIvneaakyryMSGGQFDCPI-VIRGPNGA-VGHGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 344 A--SQmALEdiAMFRTIPKCTIFYPTDAVstehavalaaNAKGMCF--IRTTRP----ETMVIY------TPQERFE--I 407
Cdd:PTZ00182 158 AyhSQ-SFE--AYFAHVPGLKVVAPSDPE----------DAKGLLKaaIRDPNPvvffEPKLLYresvevVPEADYTlpL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 408 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIG 487
Cdd:PTZ00182 225 GKAKVVRE--GKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPTCGIG 301
|
....*..
gi 225637463 488 EAVCAAV 494
Cdd:PTZ00182 302 AEIAAQI 308
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
3-214 |
1.95e-19 |
|
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: 89.37 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 3 VLFFYIMRYKQSDPENPDNDRFVL----------------------AKRLSF------------------VDVATGWLGQ 42
Cdd:pfam00456 37 VLFKRFLKHNPNDPKWINRDRFVLsnghgsmllysllhltgydlsmEDLKSFrqlgsktpghpefghtagVEVTTGPLGQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 43 GLGVACGMA---------YTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHC 113
Cdd:pfam00456 117 GIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 114 INIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMpreRADAIikli 192
Cdd:pfam00456 197 EDT-AARFEAYGWHViEVEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNKQGTHDVHGAPL---GADEV---- 268
|
250 260
....*....|....*....|..
gi 225637463 193 eSQIQTSRNLDPQPPIEDSPEV 214
Cdd:pfam00456 269 -AALKQKLGWDPYKPFEIPAEV 289
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
40-497 |
3.43e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 91.31 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 40 LGQGLGVACGMAYTGkyfdrASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFD--------VNRLGHSGALPAE 111
Cdd:PLN02234 183 LSAGLGMAVGRDLKG-----MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDnkqvslptANLDGPTQPVGAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 112 HC-INIYQRRC-----------EAFGWNtYV--VDGRDVEALCQVFWQASQVKH-KPTAVVAKTFKGRGTPSIEDAEswh 176
Cdd:PLN02234 258 SCaLSRLQSNCgmiretsstlfEELGFH-YVgpVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERAD--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 177 akpmprERADAIIKLiesqiqtsrnlDPQppiedspevnitdvrmtSPPDYRVGDKIATRKACGL-ALAKLGYANNRVVV 255
Cdd:PLN02234 334 ------DKYHGVLKF-----------DPE-----------------TGKQFKNISKTQSYTSCFVeALIAEAEADKDIVA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 256 LDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDHI-RIGGLAESNINIIGSH 334
Cdd:PLN02234 380 IHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQVvHDVDLQKLPVRFAIDR 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 335 CGVsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMCFiRTTRPETMVIYTPQER----FEIG 408
Cdd:PLN02234 459 AGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSLPPGNkgvpLQIG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 409 QAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHyPQGGIGE 488
Cdd:PLN02234 537 RGRILRD--GERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE-VLITVEEG-SIGGFGS 612
|
....*....
gi 225637463 489 AVCAAVSMD 497
Cdd:PLN02234 613 HVVQFLALD 621
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
379-494 |
8.83e-19 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 89.21 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 379 AANAKGM--CFIRTTRPetmVIYTPQE-----RFE----------IGQAKVLRhcVSDKVTVIGAGITVYEALAAADELS 441
Cdd:PRK11892 289 AADAKGLlkAAIRDPNP---VIFLENEilygqSFDvpklddfvlpIGKARIHR--EGKDVTIVSFSIGMTYALKAAEELA 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 225637463 442 KQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVCAAV 494
Cdd:PRK11892 364 KEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARV 415
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
274-494 |
7.36e-17 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 81.69 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 274 PERFIECFMAEQNMVSVALGCASRG-RTIAFASTFAaFLTRAFDHIrIGGLAESNInIIGSHCGVSV---GDDGA----- 344
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAGlRPIVEFMTFN-FSMQAIDQI-VNSAAKTNY-MSGGQLKCPIvfrGPNGAaarva 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 345 SQMALEDIAMFRTIPKCTIFYPtdavstehavALAANAKGM--CFIRTTRP----ETMVIY-----TPQERF--EIGQAK 411
Cdd:PRK09212 127 AQHSQCYAAWYSHIPGLKVVAP----------YFAADCKGLlkTAIRDPNPviflENEILYghsheVPEEEEsiPIGKAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 412 VLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVC 491
Cdd:PRK09212 197 ILRE--GSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAEIA 273
|
...
gi 225637463 492 AAV 494
Cdd:PRK09212 274 ALI 276
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
268-497 |
3.79e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 81.49 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 268 IFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDHIRIG-GLAESNINIIGSHCGVsVGDDGASQ 346
Cdd:PLN02582 391 LFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQVVHDvDLQKLPVRFAMDRAGL-VGADGPTH 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 347 MALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMCFiRTTRPETMVIYTPQER----FEIGQAKVLRHcvSDK 420
Cdd:PLN02582 469 CGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNNkgipIEVGKGRILLE--GER 545
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225637463 421 VTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHyPQGGIGEAVCAAVSMD 497
Cdd:PLN02582 546 VALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVEEG-SIGGFGSHVAQFMALD 620
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-490 |
4.39e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 81.21 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 129 YVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWHAKpMPReradaiikliesqiqtsrNLDPQPP 207
Cdd:PRK12315 212 YVEDGNDIESLIEAFKEVKDIDH-PIVLHIHTLKGKGyQPAEENKEAFHWH-MPF------------------DLETGQS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 208 IEDSPEVNITDVRMtsppDYrVGDKIATRKacglalaklgyannRVVVLDGDTRySTFS-EIFNKEYPERFIECFMAEQN 286
Cdd:PRK12315 272 KVPASGESYSSVTL----DY-LLKKIKEGK--------------PVVAINAAIP-GVFGlKEFRKKYPDQYVDVGIAEQE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 287 MVSVALGCASRG-RTIAFasTFAAFLTRAFDHIrIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFY 365
Cdd:PRK12315 332 SVAFASGIAANGaRPVIF--VNSTFLQRAYDQL-SHDLAINNNPAVMIVFGGSISGNDVTHLGIFDIPMISNIPNLVYLA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 366 PTDA-----------VSTEHAVAlaanakgmcfIRTtrPETMVIYTPQE-------RFEIGQAkvlrhcvSDKVTVIGAG 427
Cdd:PRK12315 409 PTTKeeliamlewalTQHEHPVA----------IRV--PEHGVESGPTVdtdystlKYEVTKA-------GEKVAILALG 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225637463 428 iTVYE-ALAAADELSKQD-IFIRVIDLFTIKPLDVATIvSSAKATEGRIITVEDHYPQGGIGEAV 490
Cdd:PRK12315 470 -DFYElGEKVAKKLKEELgIDATLINPKFITGLDEELL-EKLKEDHELVVTLEDGILDGGFGEKI 532
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
268-497 |
4.43e-15 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 76.78 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 268 IFNKEYPERFIECFMAEQNMVSVALGCASRG-RTIAFASTFAaFLTRAFDHIrIGGLAESNINIIGShcgVSV-----GD 341
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHI-INSAAKTNYMSAGQ---ISVpivfrGP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 342 DGAS-----QMALEDIAMFRTIPKCTIFYPTDAvstEHAVALAANAkgmcfIRTTRP----ETMVIY-----------TP 401
Cdd:PLN02683 142 NGAAagvgaQHSQCFAAWYSSVPGLKVLAPYSS---EDARGLLKAA-----IRDPDPvvflENELLYgesfpvsaevlDS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 402 QERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHY 481
Cdd:PLN02683 214 SFVLPIGKAKIERE--GKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|....*.
gi 225637463 482 PQGGIGEAVCAAVSMD 497
Cdd:PLN02683 291 PQHGVGAEICASVVEE 306
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
269-538 |
2.52e-12 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 69.36 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 269 FNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDH-IRIGGLAESNINIIGSHCGVsVGDDGASQM 347
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQvVHDVDRQRKAVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 348 ALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMC--FIRTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTV 423
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEIGRGRVLVE--GQDVAL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 424 IGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVaTIVSSAKATEGRIITVEDHYpQGGIGEAVCAAVS----MDPD 499
Cdd:PLN02225 573 LGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDI-KLVRDLCQNHKFLITVEEGC-VGGFGSHVAQFIAldgqLDGN 650
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 225637463 500 IQVHSLAV-SGVPQSGKSEELLDMYGISARHIIVAVKCML 538
Cdd:PLN02225 651 IKWRPIVLpDGYIEEASPREQLALAGLTGHHIAATALSLL 690
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
36-161 |
2.80e-11 |
|
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: 64.44 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 36 ATGWLGQGLGVACGMAYTGKYFDRASYrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGALP-AEH 112
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFA---ALWKLPVIFVCenNGYAISTPTSrQTA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 225637463 113 CINIYQrRCEAFGWNTYVVDGRDVEALCQVFWQASQ---VKHKPTAVVAKTF 161
Cdd:cd02000 178 GTSIAD-RAAAYGIPGIRVDGNDVLAVYEAAKEAVErarAGGGPTLIEAVTY 228
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
40-210 |
4.61e-11 |
|
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: 64.39 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 40 LGQGLGVACGMAYTGKYF--DRAsyrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGalPAEH--- 112
Cdd:COG1071 129 VGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFA---AVWKLPVVFVCenNGYAIST--PVERqta 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 113 CINIYQrRCEAFGWNTYVVDGRDVEALCQVFWQAsqVKH-----KPTAVVAKTFKGRG-----TPSI----EDAESWHAK 178
Cdd:COG1071 201 VETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEA--VERarageGPTLIEAKTYRLGGhstsdDPTRyrtkEEVEEWRER 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 225637463 179 -PMPR-------------ERADAIIKLIESQIQTSRNL---DPQPPIED 210
Cdd:COG1071 278 dPIERlraylleegllteEELEAIEAEAKAEVEEAVEFaeaSPEPDPEE 326
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
37-165 |
1.26e-06 |
|
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: 49.08 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 37 TGWLGQGLGVACGMAytgKYFDRA--SYRVFCLMSDGESSEGSVWEAMAFASYYsLDNLVAIFDVNRlgHSGALPAEHCI 114
Cdd:cd02007 74 TGHSSTSISAALGMA---VARDLKgkKRKVIAVIGDGALTGGMAFEALNNAGYL-KSNMIVILNDNE--MSISPNVGTPG 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 225637463 115 NIYqrrcEAFGWN-TYVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG 165
Cdd:cd02007 148 NLF----EELGFRyIGPVDGHNIEALIKVLKEVKDLKG-PVLLHVVTKKGKG 194
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
353-540 |
1.41e-06 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 50.51 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 353 AMFRTIPKCTIFyptdAVSTEHavalaaNAKGM--CFIRTTRP----ETMVIYT-----PQERF--EIGQAKVLRHcvSD 419
Cdd:CHL00144 135 SYFQSVPGLQIV----ACSTPY------NAKGLlkSAIRSNNPviffEHVLLYNlkeeiPDNEYllPLEKAEVVRP--GN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 420 KVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCAAV----- 494
Cdd:CHL00144 203 DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIGAELIAQInehlf 281
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 225637463 495 -SMDPDIQVHSLAVSGVPQSGKSEELLDmygISARHIIVAVKCMLLN 540
Cdd:CHL00144 282 dELDAPIVRLSSQDVPTPYNGPLEEATV---IQPAQIIEAVEQIITN 325
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
32-139 |
3.59e-06 |
|
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: 49.23 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 32 FVDVATGWLGQGLGVACGMAYTGKYFDRASY------RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNR---- 101
Cdd:cd02017 112 FWEFPTVSMGLGPIQAIYQARFNRYLEDRGLkdtsdqKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLqrld 191
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 225637463 102 ---LGHSGAlpaehcINIYQRRCEAFGWN-TYVVDGRDVEAL 139
Cdd:cd02017 192 gpvRGNGKI------IQELEGIFRGAGWNvIKVIWGSKWDEL 227
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
24-160 |
3.01e-05 |
|
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: 44.55 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 24 FVLAKRLSFVdVATGW--LGQGLGVACGMAYTGKyfDRasyRVFCLMSDGESSEGsvWEAMAFASYYSLDNLVAIFDVNR 101
Cdd:cd00568 31 LPLRRGRRFL-TSTGFgaMGYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225637463 102 LG---------HSGALPAEHCINI-YQRRCEAFGWNTYVVDgrDVEALCQVFWQASQvKHKPTAVVAKT 160
Cdd:cd00568 103 YGtirmhqeafYGGRVSGTDLSNPdFAALAEAYGAKGVRVE--DPEDLEAALAEALA-AGGPALIEVKT 168
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
39-220 |
4.31e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 45.63 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 39 WLGQGLGVACGMAYTGKYF-----DRASYRV-FCLMSDGESSEGSVWEAMAFASYYsldNLVAIFDVNR------LGH-- 104
Cdd:CHL00149 129 FIGEGIPIALGAAFQSIYRqqvlkEVQPLRVtACFFGDGTTNNGQFFECLNMAVLW---KLPIIFVVENnqwaigMAHhr 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637463 105 SGALPAEHciniyqRRCEAFGWNTYVVDGRDVEALCQVFWQA---SQVKHKPTAVVAKTFKGRGTP--------SIEDAE 173
Cdd:CHL00149 206 STSIPEIH------KKAEAFGLPGIEVDGMDVLAVREVAKEAverARQGDGPTLIEALTYRFRGHSladpdelrSKQEKE 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225637463 174 SWHAKpmpreraDAIIKL----IESQIQTSRNLDP-----QPPIED-------SPEVNITDVR 220
Cdd:CHL00149 280 AWVAR-------DPIKKLksyiIDNELASQKELNKiqrevKIEIEQavqfaisSPEPNISDLK 335
|
|
| |
