|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
24-594 |
2.56e-150 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 445.35 E-value: 2.56e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 24 LRDMASRLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------- 84
Cdd:PRK05899 8 LQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllhlagydls 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 85 ---------------------RLSFVDVATGWLGQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDGESSEGSV 134
Cdd:PRK05899 88 iddlknfrqlgsktpghpeygHTPGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDGDLMEGIS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 135 WEAMAFASYYSLDNLVAIFDVNRLGHSGALPaEHCIDIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKhKPTAVVA 214
Cdd:PRK05899 168 HEACSLAGHLKLGNLIVIYDDNRISIDGPTE-GWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST-KPTLIIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 215 KTFKGRGTPSIEDAESWHGKPMPRERADAIIKLIesqietsrNLDPqlpiedspevnitdvrmtsppdyrvgdkiatRKA 294
Cdd:PRK05899 246 KTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL--------GWDY-------------------------------RKA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 295 CGLALAKLGYANDRVIVLDGDTKYSTFSEIF------NKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLT 368
Cdd:PRK05899 287 SGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 369 RAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAK-GMCFIRTT 447
Cdd:PRK05899 367 YARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdGPSALVLT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 448 RPETMVIY-TPQERFEIGQAKVLRHCvsDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTtiissakat 526
Cdd:PRK05899 447 RQNLPVLErTAQEEGVAKGGYVLRDD--PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ--------- 515
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453215 527 egriitvEDHYPQGGIGEAVCAAVSMDPDI----------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCML 594
Cdd:PRK05899 516 -------DAAYKESVLPAAVTARVAVEAGVadgwykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
287-591 |
7.22e-113 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 339.37 E-value: 7.22e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 287 DKIATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 366
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 367 LT-RAFDQIRI-GGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKGMCFI 444
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 445 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAK 524
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453215 525 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 591
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
30-245 |
2.00e-90 |
|
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: 279.39 E-value: 2.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 30 RLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------- 84
Cdd:cd02012 2 RIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 85 -----RL---------SFVDVATGWLGQGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLV 150
Cdd:cd02012 82 rqlgsRLpghpeygltPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 151 AIFDVNRLGHSGALPAEHCIDIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAES 230
Cdd:cd02012 161 AIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAK 240
|
250
....*....|....*
gi 388453215 231 WHGKPMPRERADAII 245
Cdd:cd02012 241 WHGKPLGEEEVELAK 255
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
25-515 |
4.08e-50 |
|
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: 183.76 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 25 RDMASRLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYkqsDPENP---DNDRFVLA------------------ 83
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPkwiNRDRFVLSnghgsmllysllhltgyd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 84 ------KR----------------LSFVDVATGWLGQGLGVACGMAYTGKY----FDRASYRVF-----CLMSDGESSEG 132
Cdd:TIGR00232 78 lsiedlKQfrqlhsktpghpeyghTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIVdhytyVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 133 SVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCIDIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTA 211
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVlEVEDGHDLAAIDAAIEEAKASTDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 212 VVAKTFKGRGTPSIEDAESWHGKPMprerADAIIKLIESQIETSRN----------------LDPQLPIEDS-------- 267
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPL----GDEEVALTKKNLGWNYNpfeipqevydhfkktvKERGAKAEQEwnelfaay 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 268 ----PEVNITDVRMTSP----------PDYRVGDK-IATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFN----KE 328
Cdd:TIGR00232 313 kkkyPELAAEFTRRLSGelpadwdkqlPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGsgdlHE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 329 YP-ERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALED 407
Cdd:TIGR00232 393 NPlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 408 IAMFRTIPKCTIFYPTDAVSTEHAVSLAanakgmcfIRTTRPETMVIYTPQ----------ERFEIGqAKVLRHCVSDKV 477
Cdd:TIGR00232 473 LASLRAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSRQnlpqleesslEKVLKG-GYVLKDSKGPDL 543
|
570 580 590
....*....|....*....|....*....|....*...
gi 388453215 478 TVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLD 515
Cdd:TIGR00232 544 ILIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFD 581
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
287-453 |
5.82e-48 |
|
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: 165.42 E-value: 5.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 287 DKIATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 362
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 363 FAAFLTRAFDQIRIG-GLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKG- 440
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|....
gi 388453215 441 -MCFIRTTRPETMV 453
Cdd:pfam02779 161 kPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
288-448 |
4.23e-30 |
|
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: 114.89 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 288 KIATRKACGLALAKLGyandrvivldgdtkystfseifnkeyperfIECFMAEQNMVSVALGCASRGRtIAFASTFAAFL 367
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 368 TRAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKGMCFIRTT 447
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 388453215 448 R 448
Cdd:smart00861 131 R 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
24-594 |
2.56e-150 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 445.35 E-value: 2.56e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 24 LRDMASRLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------- 84
Cdd:PRK05899 8 LQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllhlagydls 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 85 ---------------------RLSFVDVATGWLGQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDGESSEGSV 134
Cdd:PRK05899 88 iddlknfrqlgsktpghpeygHTPGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDGDLMEGIS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 135 WEAMAFASYYSLDNLVAIFDVNRLGHSGALPaEHCIDIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKhKPTAVVA 214
Cdd:PRK05899 168 HEACSLAGHLKLGNLIVIYDDNRISIDGPTE-GWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST-KPTLIIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 215 KTFKGRGTPSIEDAESWHGKPMPRERADAIIKLIesqietsrNLDPqlpiedspevnitdvrmtsppdyrvgdkiatRKA 294
Cdd:PRK05899 246 KTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL--------GWDY-------------------------------RKA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 295 CGLALAKLGYANDRVIVLDGDTKYSTFSEIF------NKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLT 368
Cdd:PRK05899 287 SGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 369 RAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAK-GMCFIRTT 447
Cdd:PRK05899 367 YARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdGPSALVLT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 448 RPETMVIY-TPQERFEIGQAKVLRHCvsDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTtiissakat 526
Cdd:PRK05899 447 RQNLPVLErTAQEEGVAKGGYVLRDD--PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ--------- 515
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453215 527 egriitvEDHYPQGGIGEAVCAAVSMDPDI----------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCML 594
Cdd:PRK05899 516 -------DAAYKESVLPAAVTARVAVEAGVadgwykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
287-591 |
7.22e-113 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 339.37 E-value: 7.22e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 287 DKIATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 366
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 367 LT-RAFDQIRI-GGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKGMCFI 444
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 445 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAK 524
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 388453215 525 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 591
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
30-245 |
2.00e-90 |
|
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: 279.39 E-value: 2.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 30 RLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------- 84
Cdd:cd02012 2 RIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 85 -----RL---------SFVDVATGWLGQGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLV 150
Cdd:cd02012 82 rqlgsRLpghpeygltPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 151 AIFDVNRLGHSGALPAEHCIDIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAES 230
Cdd:cd02012 161 AIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAK 240
|
250
....*....|....*
gi 388453215 231 WHGKPMPRERADAII 245
Cdd:cd02012 241 WHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
24-253 |
2.68e-73 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 235.74 E-value: 2.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 24 LRDMASRLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------RLSF--- 88
Cdd:COG3959 8 LEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKghaapalyavlaEKGYfpk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 89 ------------------------VDVATGWLGQGLGVACGMAYTGKYfDRASYRVFCLMSDGESSEGSVWEAMAFASYY 144
Cdd:COG3959 88 eelatfrklgsrlqghpdmkktpgVEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVWEAAMAAAHY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 145 SLDNLVAIFDVNRLGHSGALPAEHCIDIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPS 224
Cdd:COG3959 167 KLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKGKGVSF 246
|
250 260
....*....|....*....|....*....
gi 388453215 225 IEDAESWHGKPMPRERADAIIKLIESQIE 253
Cdd:COG3959 247 MENRPKWHGKAPNDEELEQALAELEAELG 275
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
293-448 |
3.71e-62 |
|
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: 202.29 E-value: 3.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 293 KACGLALAKLGYANDRVIVLDGDTKYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFD 372
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388453215 373 QIRI-GGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKGMCFIRTTR 448
Cdd:cd07033 80 QIRHdVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
25-515 |
4.08e-50 |
|
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: 183.76 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 25 RDMASRLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYkqsDPENP---DNDRFVLA------------------ 83
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPkwiNRDRFVLSnghgsmllysllhltgyd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 84 ------KR----------------LSFVDVATGWLGQGLGVACGMAYTGKY----FDRASYRVF-----CLMSDGESSEG 132
Cdd:TIGR00232 78 lsiedlKQfrqlhsktpghpeyghTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIVdhytyVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 133 SVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCIDIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTA 211
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVlEVEDGHDLAAIDAAIEEAKASTDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 212 VVAKTFKGRGTPSIEDAESWHGKPMprerADAIIKLIESQIETSRN----------------LDPQLPIEDS-------- 267
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPL----GDEEVALTKKNLGWNYNpfeipqevydhfkktvKERGAKAEQEwnelfaay 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 268 ----PEVNITDVRMTSP----------PDYRVGDK-IATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFN----KE 328
Cdd:TIGR00232 313 kkkyPELAAEFTRRLSGelpadwdkqlPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGsgdlHE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 329 YP-ERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALED 407
Cdd:TIGR00232 393 NPlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 408 IAMFRTIPKCTIFYPTDAVSTEHAVSLAanakgmcfIRTTRPETMVIYTPQ----------ERFEIGqAKVLRHCVSDKV 477
Cdd:TIGR00232 473 LASLRAIPNLSVWRPCDGNETAAAWKYA--------LESQDGPTALILSRQnlpqleesslEKVLKG-GYVLKDSKGPDL 543
|
570 580 590
....*....|....*....|....*....|....*...
gi 388453215 478 TVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLD 515
Cdd:TIGR00232 544 ILIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFD 581
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
287-453 |
5.82e-48 |
|
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: 165.42 E-value: 5.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 287 DKIATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 362
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 363 FAAFLTRAFDQIRIG-GLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKG- 440
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|....
gi 388453215 441 -MCFIRTTRPETMV 453
Cdd:pfam02779 161 kPVVLRLPRQLLRP 174
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
178-594 |
1.42e-42 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 161.40 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 178 EAFGWNtYV--VDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWHGkpmpreradaiikliesqiet 254
Cdd:PRK05444 203 EELGFN-YIgpIDGHDLDALIETLKNAKDLKG-PVLLHVVTKKGKGyAPAEADPIKYHG--------------------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 255 srnldpqlpiedspevnitdvrmTSPPDYRVGDKIATRKAC--------GLALAKLGYANDRVIVLDGDTKYSTFSEIFN 326
Cdd:PRK05444 260 -----------------------VGKFDPETGEQPKSSKPGkpsytkvfGETLCELAEKDPKIVAITAAMPEGTGLVKFS 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 327 KEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFDQI----------------RiGGLsesniniigsh 390
Cdd:PRK05444 317 KRFPDRYFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVihdvalqnlpvtfaidR-AGL----------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 391 cgvsVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANA-KGMCFIRTTRPE-TMVIYTPQERFEIGQAKV 468
Cdd:PRK05444 384 ----VGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYdDGPIAIRYPRGNgVGVELPELEPLPIGKGEV 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 469 LRHcvSDKVTVIGAGITVYEALAAADELLKqdifIRVIDLFTIKPLDVTTIISSAKATEgRIITVEDHYPQGGIGEAVCA 548
Cdd:PRK05444 460 LRE--GEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLE 532
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 388453215 549 AVS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 594
Cdd:PRK05444 533 FLAdHGLDVPVLNL---GLPDEfidhGSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
178-594 |
1.59e-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: 161.72 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 178 EAFGWNtYV--VDGRDVEALCQVFWQASQVKhKPTAVVAKTFKGRG-TPSIEDAESWHGkpmpreradaiIKLIEsqIET 254
Cdd:COG1154 242 EELGFK-YIgpIDGHDLDALVETLRNAKDLK-GPVLLHVVTKKGKGyAPAEKDPDKFHG-----------VGPFD--PET 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 255 SrnldpqLPIEDSPevnitdvrmtSPPDYrvgdkiaTrKACGLALAKLGYANDRVIV-----LDGdTKYSTFSeifnKEY 329
Cdd:COG1154 307 G------EPKKSKS----------SAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-TGLDKFA----ERF 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 330 PERFIECFMAEQNMVSVALGCASRGRTIAFA--STFaafLTRAFDQI----------------RiGGLsesniniigshc 391
Cdd:COG1154 358 PDRFFDVGIAEQHAVTFAAGLATEGLKPVVAiySTF---LQRAYDQVihdvalqnlpvtfaidR-AGL------------ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 392 gvsVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKGMCFIRTTR-PETMV-IYTPQERFEIGQAKVL 469
Cdd:COG1154 422 ---VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgNGPGVeLPAELEPLPIGKGEVL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 470 RHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATEgRIITVEDHYPQGGIGEAVCAA 549
Cdd:COG1154 499 RE--GKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEF 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 388453215 550 VS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 594
Cdd:COG1154 576 LAdAGLDVPVLRL---GLPDRfiehGSRAELLAELGLDAEGIARAILELL 622
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
43-594 |
4.80e-41 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 157.91 E-value: 4.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 43 SSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVL----AKRLSF------------------------------ 88
Cdd:PTZ00089 25 NSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLsnghASALLYsmlhltgydlsmedlknfrqlgsrtpghpe 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 89 ------VDVATGWLGQGLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIF 153
Cdd:PTZ00089 105 rhitpgVEVTTGPLGQGIANAVGLAIAEKHlaakFNRPGHpifdnYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 154 DVNRLGHSGALPAEHCIDIyQRRCEAFGWNTYVVD--GRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTpSIEDAESW 231
Cdd:PTZ00089 185 DDNKITIDGNTDLSFTEDV-EKKYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYGS-SKAGTEKV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 232 HGKPMPRERADAIIKLIesqietsrNLDPQLPIEDSPEV--------------------NITDVRMTSP----------- 280
Cdd:PTZ00089 263 HGAPLGDEDIAQVKELF--------GLDPEKKFHVSEEVrqffeqhvekkkenyeawkkRFAKYTAAFPkeaqaierrfk 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 281 -----------PDYRVGDK-IATRKACGLALAKLGYANDRVIVLDGDTKYSTFSEI-----FNKEYPE-RFIECFMAEQN 342
Cdd:PTZ00089 335 gelppgwekklPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPkeandFTKASPEgRYIRFGVREHA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 343 MVSVALGCASRGRTIAFASTFAAFLTRAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYP 422
Cdd:PTZ00089 415 MCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRP 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 423 TDAVSTEHAVSLA-ANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHC-VSDKVTVIGAGITVYEALAAADeLLKQD 500
Cdd:PTZ00089 495 ADGTETSGAYALAlANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFtNSPQLILVASGSEVSLCVEAAK-ALSKE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 501 IFIRVI-----DLFTIKPLDVTTIIssakategriitvedhYPQGGIGE-AVCAAVSMDPDIQVH-SLAVSGVPQSGKSE 573
Cdd:PTZ00089 574 LNVRVVsmpcwELFDQQSEEYQQSV----------------LPSGGVPVlSVEAYVSFGWEKYSHvHVGISGFGASAPAN 637
|
650 660
....*....|....*....|.
gi 388453215 574 ELLDMYGISARHIIVAVKCML 594
Cdd:PTZ00089 638 ALYKHFGFTVENVVEKARALA 658
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
464-586 |
3.00e-35 |
|
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: 128.87 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 464 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATeGRIITVEDHYPQGGIG 543
Cdd:pfam02780 1 GKAEILRE--GDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 388453215 544 EAVCAAVS----MDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHI 586
Cdd:pfam02780 78 SEVAAALAeeafDGLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PLN02790 |
PLN02790 |
transketolase |
32-521 |
4.99e-34 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 137.46 E-value: 4.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 32 RIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVLA-------------------------KRL 86
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSaghgcmlqyallhlagydsvqmedlKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 87 ------------SF----VDVATGWLGQGLGVACGMAYTGKY----FDRA-----SYRVFCLMSDGESSEGSVWEAMAFA 141
Cdd:PLN02790 82 rqwgsrtpghpeNFetpgIEVTTGPLGQGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISNEAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 142 SYYSLDNLVAIFDVNRL---GHSGALPAEhciDIyQRRCEAFGWNTYVVDG--RDVEALCQVFWQASQVKHKPTAVVAKT 216
Cdd:PLN02790 162 GHWGLGKLIVLYDDNHIsidGDTEIAFTE---DV-DKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 217 FKGRGTPSIEDAESWHGKPMPRERADAiikliesqieTSRNLD-PQLPIEDSPEVN------------------------ 271
Cdd:PLN02790 238 TIGYGSPNKANSYSVHGAALGEKEVDA----------TRKNLGwPYEPFHVPEDVKshwskhtkegaaleaewnakfaey 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 272 --------------ITDVRMT----SPPDYRVGDKI-ATRK---ACGLALAK-----LGYANDrvivLDGDTK-YSTFSE 323
Cdd:PLN02790 308 kkkypeeaaelkslISGELPSgwekALPTFTPEDPAdATRNlsqKCLNALAKvlpglIGGSAD----LASSNMtLLKDFG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 324 IFNKEYP-ERFIECFMAEQNMVSVALGCASRGRT-IAFASTFAAFLTRAFDQIRIGGLSESNINIIGSHCGVSVGEDGAS 401
Cdd:PLN02790 384 DFQKDTPeERNVRFGVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPT 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 402 QMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLA-ANAKG---MCFIRTTRPETMViyTPQERFEIGQAKVLRHCVSDK- 476
Cdd:PLN02790 464 HQPIEHLASLRAMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPNLPG--TSIEGVEKGGYVISDNSSGNKp 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 477 -VTVIGAGITVYEALAAADELLKQDIFIRVI-----DLF---------TIKPLDVTTIIS 521
Cdd:PLN02790 542 dLILIGTGSELEIAAKAAKELRKEGKKVRVVsmvcwELFeeqsdeykeSVLPSSVTARVS 601
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
288-448 |
4.23e-30 |
|
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: 114.89 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 288 KIATRKACGLALAKLGyandrvivldgdtkystfseifnkeyperfIECFMAEQNMVSVALGCASRGRtIAFASTFAAFL 367
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 368 TRAFDQIRIGGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAANAKGMCFIRTT 447
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 388453215 448 R 448
Cdd:smart00861 131 R 131
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
44-509 |
5.62e-28 |
|
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: 118.96 E-value: 5.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 44 SGHPTSCSSSAEIMSVLFFYIMRYkqsDPENP---DNDRFVLA------------------------KRL---------- 86
Cdd:COG0021 24 SGHPGLPMGMAPIAYVLWTKFLKH---NPANPkwpNRDRFVLSaghgsmllysllhltgydlslddlKNFrqlgsktpgh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 87 ------SFVDVATGWLGQGLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVA 151
Cdd:COG0021 101 peyghtPGVETTTGPLGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 152 IFDVNRL---GH-SGALpaehCIDIyQRRCEAFGWNTY-VVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIE 226
Cdd:COG0021 181 LYDDNGIsidGDtDLAF----SEDV-AKRFEAYGWHVIrVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQ 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 227 DAESWHGKPMPRERADAIIKLI-------------------------------ESQIETSRNLDPQLPIE-------DSP 268
Cdd:COG0021 256 GTAKAHGAPLGAEEIAATKEALgwppepfevpdevyahwraagergaaaeaewNERFAAYAAAYPELAAElerrlagELP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 269 EvNITDVRmtspPDYRVGDK-IATRKACGLALAKLGYANDRVIV----LDGDTK-YSTFSEIFNKEYPE-RFIECFMAEQ 341
Cdd:COG0021 336 E-DWDAAL----PAFEADAKgVATRKASGKVLNALAPVLPELIGgsadLAGSNKtTIKGAGSFSPEDPSgRNIHFGVREH 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 342 NMVSVALGCASRGRTIAFASTFAAFltraFD----QIRIGGLSESNINIIGSHCGVSVGEDGASQMALEDIAMFRTIPKC 417
Cdd:COG0021 411 AMGAIMNGIALHGGLRPYGGTFLVF----SDymrpAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASLRAIPNL 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 418 TIFYPTDAVSTEHAVSLAANakgmcfiRTTRPeTMVIYT----PQERFEIGQAK-------VLRHCVSD-KVTVIGAGIT 485
Cdd:COG0021 487 DVIRPADANETAAAWKLALE-------RKDGP-TALILSrqnlPTLDRTAAAAEgvakgayVLADAEGTpDVILIATGSE 558
|
570 580
....*....|....*....|....*....
gi 388453215 486 VYEALAAADELLKQDIFIRVI-----DLF 509
Cdd:COG0021 559 VSLAVEAAELLAAEGIKVRVVsmpswELF 587
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
25-236 |
1.15e-26 |
|
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: 110.94 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 25 RDMASRLRIHSIRATCSTSSGHPTSCSSSAEIMSVLFFYIMRYKQSDPENPDNDRFVL---------------------- 82
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLsnghgsmllysllhltgydlsm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 83 AKRLSF------------------VDVATGWLGQGLGVACGMA---------YTGKYFDRASYRVFCLMSDGESSEGSVW 135
Cdd:pfam00456 83 EDLKSFrqlgsktpghpefghtagVEVTTGPLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 136 EAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCIDIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTAVVA 214
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDT-AARFEAYGWHViEVEDGHDVEAIAAAIEEAKAEKDKPTLIKC 241
|
250 260
....*....|....*....|..
gi 388453215 215 KTFKGRGTPSIEDAESWHGKPM 236
Cdd:pfam00456 242 RTVIGYGSPNKQGTHDVHGAPL 263
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
339-551 |
8.50e-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: 108.18 E-value: 8.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 339 AEQNMVSVALGCASRG-RTIAFAsTFAAFLTRAFDQI---------RIGGLSESNInIIGSHCGVSVGEdGA--SQMaLE 406
Cdd:COG0022 59 SEAGIVGAAIGAALAGlRPVVEI-QFADFIYPAFDQIvnqaaklryMSGGQFKVPM-VIRTPYGGGIGA-GAqhSQS-LE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 407 diAMFRTIPKCTIFYPtdavSTehavslAANAKGM---CfIRTTRP----ETMVIYT-----PQERFEI--GQAKVLRHc 472
Cdd:COG0022 135 --AWFAHIPGLKVVAP----ST------PYDAKGLlkaA-IRDDDPviflEHKRLYRlkgevPEEDYTVplGKARVVRE- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 388453215 473 vSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATeGRIITVEDHYPQGGIGEAVCAAVS 551
Cdd:COG0022 201 -GTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEIAARIA 277
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
184-594 |
9.08e-25 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 109.04 E-value: 9.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 184 TYV--VDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAEswhgkpmprERADAIIKLiesqietsrNLDPQ 261
Cdd:PRK12571 248 TYVgpIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADE---------DKYHAVGKF---------DVVTG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 262 LPIEDSPevnitdvrmtSPPDYRvgdkiatrKACGLALAKLGYANDRVIVLDGDTKYSTFSEIFNKEYPERFIECFMAEQ 341
Cdd:PRK12571 310 LQKKSAP----------SAPSYT--------SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 342 NMVSVALGCASRGrTIAFASTFAAFLTRAFDQIRIG-GLSESNINIIGSHCGVsVGEDGASQMALEDIAMFRTIPKCTIF 420
Cdd:PRK12571 372 HAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLHDvALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVM 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 421 YPTDAVSTEHAV-SLAANAKGMCFIRTTRPETMVIYTPqERFEIGQAKVLRHCVSDK-VTVIGAGITVYEALAAADELLK 498
Cdd:PRK12571 450 APRDEAELRHMLrTAAAHDDGPIAVRFPRGEGVGVEIP-AEGTILGIGKGRVPREGPdVAILSVGAHLHECLDAADLLEA 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 499 QDIFIRVIDLFTIKPLDVTTIissAKATEGRI-ITVEDHYPQGGIGEAVCAAVS----MDPDIQVHSLavsGVP----QS 569
Cdd:PRK12571 529 EGISVTVADPRFVKPLDEALT---DLLVRHHIvVIVEEQGAMGGFGAHVLHHLAdtglLDGGLKLRTL---GLPdrfiDH 602
|
410 420
....*....|....*....|....*
gi 388453215 570 GKSEELLDMYGISARHIIVAVKCML 594
Cdd:PRK12571 603 ASREEMYAEAGLTAPDIAAAVTGAL 627
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
330-550 |
1.00e-21 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 96.97 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 330 PERFIECFMAEQNMVSVALGCASRG-RTIAfASTFAAFLTRAFDQI---------RIGGLSESNInIIGSHCGVsVGEDG 399
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNGlRPIA-EFMFADFIFPAFDQIvneaakyryMSGGQFDCPI-VIRGPNGA-VGHGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 400 A--SQmALEdiAMFRTIPKCTIFYPTDAVstehavslaaNAKGMCF--IRTTRP----ETMVIY------TPQERFE--I 463
Cdd:PTZ00182 158 AyhSQ-SFE--AYFAHVPGLKVVAPSDPE----------DAKGLLKaaIRDPNPvvffEPKLLYresvevVPEADYTlpL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 464 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATeGRIITVEDHYPQGGIG 543
Cdd:PTZ00182 225 GKAKVVRE--GKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPTCGIG 301
|
....*..
gi 388453215 544 EAVCAAV 550
Cdd:PTZ00182 302 AEIAAQI 308
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
435-550 |
6.42e-18 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 86.51 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 435 AANAKGM--CFIRTTRPetmVIYTPQE-----RFE----------IGQAKVLRhcVSDKVTVIGAGITVYEALAAADELL 497
Cdd:PRK11892 289 AADAKGLlkAAIRDPNP---VIFLENEilygqSFDvpklddfvlpIGKARIHR--EGKDVTIVSFSIGMTYALKAAEELA 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 388453215 498 KQDIFIRVIDLFTIKPLDVTTIISSAKATeGRIITVEDHYPQGGIGEAVCAAV 550
Cdd:PRK11892 364 KEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARV 415
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
96-553 |
1.50e-17 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 86.31 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 96 LGQGLGVACGMAYTGkyfdrASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFD--------VNRLGHSGALPAE 167
Cdd:PLN02234 183 LSAGLGMAVGRDLKG-----MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDnkqvslptANLDGPTQPVGAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 168 HC-IDIYQRRC-----------EAFGWNtYV--VDGRDVEALCQVFWQASQVKH-KPTAVVAKTFKGRGTPSIEDAE-SW 231
Cdd:PLN02234 258 SCaLSRLQSNCgmiretsstlfEELGFH-YVgpVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERADdKY 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 232 HGkpmpreradaIIKLiesqietsrnlDPQlpiedspevnitdvrmtSPPDYRVGDKIATRKACGL-ALAKLGYANDRVI 310
Cdd:PLN02234 337 HG----------VLKF-----------DPE-----------------TGKQFKNISKTQSYTSCFVeALIAEAEADKDIV 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 311 VLDGDTKYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDQI-RIGGLSESNINIIGS 389
Cdd:PLN02234 379 AIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQVvHDVDLQKLPVRFAID 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 390 HCGVsVGEDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAA--NAKGMCFiRTTRPETMVIYTPQER----FEI 463
Cdd:PLN02234 458 RAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSLPPGNkgvpLQI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 464 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATEgRIITVEDHyPQGGIG 543
Cdd:PLN02234 536 GRGRILRD--GERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE-VLITVEEG-SIGGFG 611
|
490
....*....|
gi 388453215 544 EAVCAAVSMD 553
Cdd:PLN02234 612 SHVVQFLALD 621
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
185-546 |
1.16e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 83.52 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 185 YVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWH---------GK---PMPRERA-DAIIKLIES 250
Cdd:PRK12315 212 YVEDGNDIESLIEAFKEVKDIDH-PIVLHIHTLKGKGyQPAEENKEAFHwhmpfdletGQskvPASGESYsSVTLDYLLK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 251 QIEtsrnldpqlpiEDSPEVNITDvrmtsppdyrvgdkiATRKACGLalaklgyandrvivldgdtkystfsEIFNKEYP 330
Cdd:PRK12315 291 KIK-----------EGKPVVAINA---------------AIPGVFGL-------------------------KEFRKKYP 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 331 ERFIECFMAEQNMVSVALGCASRG-RTIAFasTFAAFLTRAFDQIrIGGLSESNINIIGSHCGVSVGEDGASQMALEDIA 409
Cdd:PRK12315 320 DQYVDVGIAEQESVAFASGIAANGaRPVIF--VNSTFLQRAYDQL-SHDLAINNNPAVMIVFGGSISGNDVTHLGIFDIP 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 410 MFRTIPKCTIFYPTDA-----------VSTEHAVslaanakgmcFIRTtrPETMVIYTPQE-------RFEIGQAkvlrh 471
Cdd:PRK12315 397 MISNIPNLVYLAPTTKeeliamlewalTQHEHPV----------AIRV--PEHGVESGPTVdtdystlKYEVTKA----- 459
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388453215 472 cvSDKVTVIGAGiTVYEALAAADELLKQDIFIR--VIDLFTIKPLDVTTiISSAKATEGRIITVEDHYPQGGIGEAV 546
Cdd:PRK12315 460 --GEKVAILALG-DFYELGEKVAKKLKEELGIDatLINPKFITGLDEEL-LEKLKEDHELVVTLEDGILDGGFGEKI 532
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
435-550 |
1.57e-16 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 80.92 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 435 AANAKGM--CFIRTTRP----ETMVIY-----TPQERF--EIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDI 501
Cdd:PRK09212 151 AADCKGLlkTAIRDPNPviflENEILYghsheVPEEEEsiPIGKAAILRE--GSDVTIVTFSIQVKLALEAAELLEKEGI 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 388453215 502 FIRVIDLFTIKPLDVTTIISSAKATeGRIITVEDHYPQGGIGEAVCAAV 550
Cdd:PRK09212 229 SVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAEIAALI 276
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
324-553 |
9.01e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 80.71 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 324 IFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDQIRIG-GLSESNINIIGSHCGVsVGEDGASQ 402
Cdd:PLN02582 391 LFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQVVHDvDLQKLPVRFAMDRAGL-VGADGPTH 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 403 MALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAA--NAKGMCFiRTTRPETMVIYTPQER----FEIGQAKVLRHcvSDK 476
Cdd:PLN02582 469 CGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNNkgipIEVGKGRILLE--GER 545
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388453215 477 VTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATEgRIITVEDHyPQGGIGEAVCAAVSMD 553
Cdd:PLN02582 546 VALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVEEG-SIGGFGSHVAQFMALD 620
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
463-553 |
4.10e-14 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 74.09 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 463 IGQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVTTIISSAKATeGRIITVEDHYPQGGI 542
Cdd:PLN02683 219 IGKAKIERE--GKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGWPQHGV 295
|
90
....*....|.
gi 388453215 543 GEAVCAAVSMD 553
Cdd:PLN02683 296 GAEICASVVEE 306
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
92-217 |
2.27e-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: 64.82 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 92 ATGWLGQGLGVACGMAYTGKYFDRASYrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGALPAEHC 169
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFA---ALWKLPVIFVCenNGYAISTPTSRQTA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 388453215 170 IDIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQ---VKHKPTAVVAKTF 217
Cdd:cd02000 178 GTSIADRAAAYGIPGIRVDGNDVLAVYEAAKEAVErarAGGGPTLIEAVTY 228
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
325-594 |
2.45e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 66.66 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 325 FNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDQ-IRIGGLSESNINIIGSHCGVsVGEDGASQM 403
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQvVHDVDRQRKAVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 404 ALEDIAMFRTIPKCTIFYPTDAVSTEHAVSLAA--NAKGMC--FIRTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTV 479
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEIGRGRVLVE--GQDVAL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 480 IGAGITVYEALAAADELLKQDIFIRVIDLFTIKPLDVtTIISSAKATEGRIITVEDHYpQGGIGEAVCAAVS----MDPD 555
Cdd:PLN02225 573 LGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDI-KLVRDLCQNHKFLITVEEGC-VGGFGSHVAQFIAldgqLDGN 650
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 388453215 556 IQVHSLAV-SGVPQSGKSEELLDMYGISARHIIVAVKCML 594
Cdd:PLN02225 651 IKWRPIVLpDGYIEEASPREQLALAGLTGHHIAATALSLL 690
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
45-195 |
1.97e-10 |
|
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: 62.71 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 45 GHPTSCSSSAEIMSVLFFYIMRYKQSDP---------------------------ENPDNDR-FVLAKRLS--------- 87
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEGGggdlvyfqghaspgiyaraflegrlteEQLDNFRqEVGGGGLSsyphpwlmp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 88 -FVDVATGWLGQGLGVACGMAYTGKYFDRASY------RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNR--- 157
Cdd:cd02017 111 dFWEFPTVSMGLGPIQAIYQARFNRYLEDRGLkdtsdqKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLqrl 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 388453215 158 ----LGHSGAlpaehcIDIYQRRCEAFGWN-TYVVDGRDVEAL 195
Cdd:cd02017 191 dgpvRGNGKI------IQELEGIFRGAGWNvIKVIWGSKWDEL 227
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
96-275 |
5.83e-10 |
|
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: 61.31 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 96 LGQGLGVACGMAYTGKYF--DRAsyrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGalPAEH--- 168
Cdd:COG1071 129 VGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFA---AVWKLPVVFVCenNGYAIST--PVERqta 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 169 CIDIYQrRCEAFGWNTYVVDGRDVEALCQVFWQAsqVKH-----KPTAVVAKTFKGRG-----TPSI----EDAESWHGK 234
Cdd:COG1071 201 VETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEA--VERarageGPTLIEAKTYRLGGhstsdDPTRyrtkEEVEEWRER 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 388453215 235 -PMPR-------------ERADAIIKLIESQIETSRNLdpqlpIEDSPEVNITDV 275
Cdd:COG1071 278 dPIERlraylleegllteEELEAIEAEAKAEVEEAVEF-----AEASPEPDPEEL 327
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
306-596 |
7.31e-09 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 57.44 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 306 NDRVIVLDGDT-----KYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFASTFAAFLTRAFDQI--RIGG 378
Cdd:CHL00144 21 DPRVFVIGEDVghyggSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFNQIsnNAGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 379 L---SESNINI---------IGSHCGVSvgedgASQMaLEdiAMFRTIPKCTIFyptdavstehAVSLAANAKGM--CFI 444
Cdd:CHL00144 101 LhytSGGNFTIpivirgpggVGRQLGAE-----HSQR-LE--SYFQSVPGLQIV----------ACSTPYNAKGLlkSAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 445 RTTRP----ETMVIYT-----PQERF--EIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELLKQDIFIRVIDLFTIKP 513
Cdd:CHL00144 163 RSNNPviffEHVLLYNlkeeiPDNEYllPLEKAEVVRP--GNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 514 LDVTTIISSAKATEgRIITVEDHYPQGGIGEAVCAAV------SMDPDIQVHSLAVSGVPQSGKSEELLDmygISARHII 587
Cdd:CHL00144 241 LDLGTISKSVKKTH-KVLIVEECMKTGGIGAELIAQInehlfdELDAPIVRLSSQDVPTPYNGPLEEATV---IQPAQII 316
|
....*....
gi 388453215 588 VAVKCMLLN 596
Cdd:CHL00144 317 EAVEQIITN 325
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
93-221 |
3.07e-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: 47.93 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 93 TGWLGQGLGVACGMAytgKYFDRA--SYRVFCLMSDGESSEGSVWEAMAFASYYsLDNLVAIFDVNRL------GHSGAL 164
Cdd:cd02007 74 TGHSSTSISAALGMA---VARDLKgkKRKVIAVIGDGALTGGMAFEALNNAGYL-KSNMIVILNDNEMsispnvGTPGNL 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 388453215 165 paehcidiyqrrCEAFGWN-TYVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG 221
Cdd:cd02007 150 ------------FEELGFRyIGPVDGHNIEALIKVLKEVKDLKG-PVLLHVVTKKGKG 194
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
80-216 |
3.62e-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: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 80 FVLAKRLSFVdVATGW--LGQGLGVACGMAYTGKyfDRasyRVFCLMSDGESSEGsvWEAMAFASYYSLDNLVAIFDVNR 157
Cdd:cd00568 31 LPLRRGRRFL-TSTGFgaMGYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 388453215 158 LG---------HSGALPA-EHCIDIYQRRCEAFGWNTYVVDgrDVEALCQVFWQASQvKHKPTAVVAKT 216
Cdd:cd00568 103 YGtirmhqeafYGGRVSGtDLSNPDFAALAEAYGAKGVRVE--DPEDLEAALAEALA-AGGPALIEVKT 168
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
95-276 |
8.46e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 44.86 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 95 WLGQGLGVACGMAYTGKYF-----DRASYRV-FCLMSDGESSEGSVWEAMAFASYYsldNLVAIFDVNR------LGH-- 160
Cdd:CHL00149 129 FIGEGIPIALGAAFQSIYRqqvlkEVQPLRVtACFFGDGTTNNGQFFECLNMAVLW---KLPIIFVVENnqwaigMAHhr 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 161 SGALPAEHcidiyqRRCEAFGWNTYVVDGRDVEALCQVFWQA---SQVKHKPTAVVAKTFKGRGTP--------SIEDAE 229
Cdd:CHL00149 206 STSIPEIH------KKAEAFGLPGIEVDGMDVLAVREVAKEAverARQGDGPTLIEALTYRFRGHSladpdelrSKQEKE 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 388453215 230 SWhgkpMPReraDAIIKL----IESQIETSRNLDP-----QLPIED-------SPEVNITDVR 276
Cdd:CHL00149 280 AW----VAR---DPIKKLksyiIDNELASQKELNKiqrevKIEIEQavqfaisSPEPNISDLK 335
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
327-441 |
5.81e-03 |
|
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919 [Multi-domain] Cd Length: 167 Bit Score: 37.84 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453215 327 KEY-PERFIECFMAEQNMVSVALGCASRG-RTIAfASTFAAFLTRAFDQI---------RIGGLSESNINIIGSHCGvsv 395
Cdd:cd07036 39 DKFgPDRVIDTPIAEAGIVGLAVGAAMNGlRPIV-EIMFADFALPAFDQIvneaaklryMSGGQFKVPIVIRGPNGG--- 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 388453215 396 GEDGASQ--MALEdiAMFRTIPKCTIFYPTDavstehavslAANAKGM 441
Cdd:cd07036 115 GIGGGAQhsQSLE--AWFAHIPGLKVVAPST----------PYDAKGL 150
|
|
| |
