|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-578 |
4.45e-178 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 515.84 E-value: 4.45e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 1 MSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPIADLNNLRKIDSDLEGHPTPR-LNFIDVGTGSL 78
Cdd:PRK05899 41 AYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGYdLSIDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 79 GQGVAVGAGMA----YVGKNFDKA-----DYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLq 149
Cdd:PRK05899 121 GQGLANAVGMAlaekYLAALFNRPgldivDHYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEG- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 150 HKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFhCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEVVKHL 229
Cdd:PRK05899 200 WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAI-EEAKASTKPTLIIAKTIIGKGAPNKEGTHKVHGAPLG--AEEIAAAK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 230 EGLivnknvkltpkpvpktgaapdvDINNiklssppayklgdsiatRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDK- 308
Cdd:PRK05899 277 KEL----------------------GWDY-----------------RKASGKALNALAKALPELVGGSADLAGSNNTKIk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 309 -----LKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDG 383
Cdd:PRK05899 318 gskdfAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 384 PSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA-NTKGVCFIRTSRPNTCVIYD--NEEPFTIGrGKVVRqkSSDE 460
Cdd:PRK05899 398 PTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGPSALVLTRQNLPVLERtaQEEGVAKG-GYVLR--DDPD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 461 VLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAEliiehgkqcggrvvvvEDHYQQGGLGEAVLSALAGE--- 537
Cdd:PRK05899 475 VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ----------------DAAYKESVLPAAVTARVAVEagv 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 24645119 538 ----RNFV---VKHLYVPTVPRSGPPSVLIDMFGISARHVVNAVNEIL 578
Cdd:PRK05899 539 adgwYKYVgldGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
1-224 |
1.24e-115 |
|
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: 343.72 E-value: 1.24e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 1 MSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNNLRKIDSDLEGHPTPRLN-FIDVGTGSLG 79
Cdd:cd02012 29 LAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKTFRQLGSRLPGHPEYGLTpGVEVTTGSLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 80 QGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRDRL 159
Cdd:cd02012 109 QGLSVAVGMALAEK-LLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLIAIVDSNRIQIDGPTDDILFTEDLAKKF 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24645119 160 EAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGDKAAE 224
Cdd:cd02012 188 EAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAKWHGKPLGEEEVE 252
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
271-578 |
1.74e-107 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 324.73 E-value: 1.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 271 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRtvAFVSTFAT 349
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGlALAGKI--PFVSTFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 350 FFT-RAFDQIRM-GAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCF 427
Cdd:COG3958 80 FLTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 428 IRTSRPNTCVIYDNEEPFTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHG 507
Cdd:COG3958 160 LRLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645119 508 KQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVP-TVPRSGPPSVLIDMFGISARHVVNAVNEIL 578
Cdd:COG3958 238 RKT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
1-231 |
2.08e-91 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 282.35 E-value: 2.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 1 MSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNNLRKIDSDLEGHPTP-RLNFIDVGTGSLG 79
Cdd:COG3959 41 LAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKGYFPKEELATFRKLGSRLQGHPDMkKTPGVEMSTGSLG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 80 QGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRDRL 159
Cdd:COG3959 121 QGLSVAVGMALAAK-LDGKDYRVYVLLGDGELQEGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKW 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24645119 160 EAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPL-GDKAAEVVKHLEG 231
Cdd:COG3959 200 EAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKGKGVSFMENRPKWHGKAPnDEELEQALAELEA 272
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
278-432 |
1.26e-64 |
|
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: 208.45 E-value: 1.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 278 AYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQ 357
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24645119 358 IR-MGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSR 432
Cdd:cd07033 81 IRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
3-579 |
5.92e-56 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 199.90 E-value: 5.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 3 VLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPIADLNNLRKIDSDLEGHP----TPRlnfIDVGTGS 77
Cdd:PTZ00089 41 ILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDLKNFRQLGSRTPGHPerhiTPG---VEVTTGP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 78 LGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSL 148
Cdd:PTZ00089 118 LGQGIANAVGLAIAEKHlaakfnrpgHPIFDNYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 149 QHKLDVYRdRLEAFGFNAVVVD--GHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDfPNIEDLDNWHGKPLGDKAAEVV 226
Cdd:PTZ00089 198 SFTEDVEK-KYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYG-SSKAGTEKVHGAPLGDEDIAQV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 227 KHLEGL--------------IVNKNVKLTPKPVPK--------TGAAPDV----------DINNIKLSSPPAYKLGDS-I 273
Cdd:PTZ00089 276 KELFGLdpekkfhvseevrqFFEQHVEKKKENYEAwkkrfakyTAAFPKEaqaierrfkgELPPGWEKKLPKYTTNDKaI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 274 ATRLAYGTALAKIGQNNLRVVALDGD------TKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFVSTF 347
Cdd:PTZ00089 356 ATRKASENVLNPLFQILPELIGGSADltpsnlTRPKEANDFTKASPEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATF 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 348 ATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVC 426
Cdd:PTZ00089 436 LNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYALAlANAKTPT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 427 FIRTSRPNTCVIyDNEEPFTIGRGK--VVRQKSSDEVLLIGAGITLYECLAAADQLEKNcITVRVID-P----FTVKPLD 499
Cdd:PTZ00089 516 ILCLSRQNTPPL-PGSSIEGVLKGAyiVVDFTNSPQLILVASGSEVSLCVEAAKALSKE-LNVRVVSmPcwelFDQQSEE 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 500 aeliiehgkqcggrvvvvedhYQQGGL---GEAVLSALAGERNFVVK--HLYV--PTVPRSGPPSVLIDMFGISARHVVN 572
Cdd:PTZ00089 594 ---------------------YQQSVLpsgGVPVLSVEAYVSFGWEKysHVHVgiSGFGASAPANALYKHFGFTVENVVE 652
|
....*..
gi 24645119 573 AVNEILK 579
Cdd:PTZ00089 653 KARALAA 659
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
77-578 |
7.63e-55 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 195.30 E-value: 7.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 77 SLGQGVAVGAGMAyvgknfDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVIFDVNRLGQSEAT-SLQHKLDvy 155
Cdd:PRK05444 124 SAALGMAKARDLK------GGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDNEMSISPNVgALSNYLA-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 156 rdRL------EAFGFNAV-VVDGHDVEELSKAFHcAAITKNKPTAIIAKTFKGRDFPNIE-DLDNWHGkplgdkaaevvk 227
Cdd:PRK05444 195 --RLrsstlfEELGFNYIgPIDGHDLDALIETLK-NAKDLKGPVLLHVVTKKGKGYAPAEaDPIKYHG------------ 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 228 hleglivnknvklTPKPVPKTGAAPdvdinniKLSSPPAYKLGDsiatrlAYGTALAKIGQNNLRVVAL-----DGdTKN 302
Cdd:PRK05444 260 -------------VGKFDPETGEQP-------KSSKPGKPSYTK------VFGETLCELAEKDPKIVAItaampEG-TGL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 303 STFSDKLknldPQRYIECFIAEQNLVGVAVGAACRRRTVaFVSTFATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSiGE 381
Cdd:PRK05444 313 VKFSKRF----PDRYFDVGIAEQHAVTFAAGLATEGLKP-VVAIYSTFLQRAYDQVIHDvALQNLPVTFAIDRAGLV-GA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 382 DGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPN-TCVIYDNEEPFTIGRGKVVRQksSD 459
Cdd:PRK05444 387 DGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRGNgVGVELPELEPLPIGKGEVLRE--GE 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 460 EVLLIGAGITLYECLAAADQLEKncitVRVIDPFTVKPLDAELIIEHGKQcGGRVVVVEDHYQQGGLGEAVLSALAGERN 539
Cdd:PRK05444 465 DVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAK-HDLVVTVEEGAIMGGFGSAVLEFLADHGL 539
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 24645119 540 FV-VKHLYVPT--VPRsGPPSVLIDMFGISARHVVNAVNEIL 578
Cdd:PRK05444 540 DVpVLNLGLPDefIDH-GSREELLAELGLDAEGIARRILELL 580
|
|
| PLN02790 |
PLN02790 |
transketolase |
3-578 |
7.08e-53 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 191.00 E-value: 7.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 3 VLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL--FPIADLNNLRKIDSDLEGHPTprlNF----IDVGTG 76
Cdd:PLN02790 29 VLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQFRQWGSRTPGHPE---NFetpgIEVTTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 77 SLGQGVAVGAGMAYVGKN----FDKADY-----RTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATS 147
Cdd:PLN02790 106 PLGQGIANAVGLALAEKHlaarFNKPDHkivdhYTYCILGDGCQMEGISNEAASLAGHWGLGKLIVLYDDNHISIDGDTE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 148 LQHKLDVYRdRLEAFGFNAVVVDG--HDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGDKAAEV 225
Cdd:PLN02790 186 IAFTEDVDK-RYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEKEVDA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 226 VK-----HLEGLIVNKNVKLTPKPVPKTGAAPDVDIN---------------NIK-----------LSSPPAYKLGDSI- 273
Cdd:PLN02790 265 TRknlgwPYEPFHVPEDVKSHWSKHTKEGAALEAEWNakfaeykkkypeeaaELKslisgelpsgwEKALPTFTPEDPAd 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 274 ATRLAYGT---ALAK-----IG------QNNLRVVALDGDTKNSTFSdklknldpQRYIECFIAEQNLVGVAVGAACRRR 339
Cdd:PLN02790 345 ATRNLSQKclnALAKvlpglIGgsadlaSSNMTLLKDFGDFQKDTPE--------ERNVRFGVREHGMGAICNGIALHSS 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 340 T-VAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVEL 418
Cdd:PLN02790 417 GlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKV 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 419 A-ANTKG---VCFIRTSRPNTCVIYDNEepftIGRGK-VVRQKSSD---EVLLIGAGITLYECLAAADQLEKNCITVRVi 490
Cdd:PLN02790 497 AvTNRKRptvLALSRQKVPNLPGTSIEG----VEKGGyVISDNSSGnkpDLILIGTGSELEIAAKAAKELRKEGKKVRV- 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 491 dpftVKPLDAELIIEHgkqcggrvvvvEDHYQQGGLGEAVLSALA-------GERNFVV---KHLYVPTVPRSGPPSVLI 560
Cdd:PLN02790 572 ----VSMVCWELFEEQ-----------SDEYKESVLPSSVTARVSveagstfGWEKYVGskgKVIGVDRFGASAPAGILY 636
|
650
....*....|....*...
gi 24645119 561 DMFGISARHVVNAVNEIL 578
Cdd:PLN02790 637 KEFGFTVENVVAAAKSLL 654
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
271-437 |
2.83e-52 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 176.59 E-value: 2.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 271 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQ---RYIECFIAEQNLVGVAVGAACR-RRTVAFVST 346
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHgPLLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 347 FATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKG- 424
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|....
gi 24645119 425 -VCFIRTSRPNTCV 437
Cdd:pfam02779 161 kPVVLRLPRQLLRP 174
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
160-579 |
1.35e-50 |
|
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: 184.06 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 160 EAFGFNAV-VVDGHDVEELSKAFHcAAITKNKPTAIIAKTFKGRDF-PNIEDLDNWHGkplgdkaaevvkhlegliVNKN 237
Cdd:COG1154 242 EELGFKYIgPIDGHDLDALVETLR-NAKDLKGPVLLHVVTKKGKGYaPAEKDPDKFHG------------------VGPF 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 238 VKLTPKPVPKTgaapdvdinniklSSPPAYklgdsiaTRlAYGTALAKIGQNNLRVVA-----LDGdTKNSTFSDKLknl 312
Cdd:COG1154 303 DPETGEPKKSK-------------SSAPSY-------TD-VFGDTLVELAEKDPRIVAitaamPEG-TGLDKFAERF--- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 313 dPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQIRMG-AISQTNVNFVgshcgcsI------GEDGPS 385
Cdd:COG1154 358 -PDRFFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHDvALQNLPVTFA-------IdraglvGADGPT 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 386 QMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPNTC-VIYDNE-EPFTIGRGKVVRQksSDEVLL 463
Cdd:COG1154 429 HHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGPgVELPAElEPLPIGKGEVLRE--GKDVAI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 464 IGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFV-V 542
Cdd:COG1154 507 LAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREH-DLVVTVEEGVLAGGFGSAVLEFLADAGLDVpV 585
|
410 420 430
....*....|....*....|....*....|....*....
gi 24645119 543 KHLYVPT--VPRsGPPSVLIDMFGISARHVVNAVNEILK 579
Cdd:COG1154 586 LRLGLPDrfIEH-GSRAELLAELGLDAEGIARAILELLG 623
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-490 |
1.06e-49 |
|
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: 182.52 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 3 VLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPIADLNNLRKIDSDLEGHP----TPrlnFIDVGTGS 77
Cdd:COG0021 39 VLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYdLSLDDLKNFRQLGSKTPGHPeyghTP---GVETTTGP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 78 LGQGVAVGAGMAYVGK----NFDKA-----DYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNR--------L 140
Cdd:COG0021 116 LGQGIANAVGMAIAERhlaaRFNRPghdivDHYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 141 GQSEatslqhklDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLG 219
Cdd:COG0021 196 AFSE--------DV-AKRFEAYGWHVIrVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGAPLG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 220 DKAAEVVKhleglivnKNVKLTPKP--VP-----------KTGAA----------------PD-----VDINNIKL---- 261
Cdd:COG0021 267 AEEIAATK--------EALGWPPEPfeVPdevyahwraagERGAAaeaewnerfaayaaayPElaaelERRLAGELpedw 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 262 -SSPPAYKLGD-SIATRLAYGTALAKIGQN--NLrVVA---LDGDTKnsTFSDKLKNLDPQ----RYIECFIAEQnlvgv 330
Cdd:COG0021 339 dAALPAFEADAkGVATRKASGKVLNALAPVlpEL-IGGsadLAGSNK--TTIKGAGSFSPEdpsgRNIHFGVREH----- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 331 AVGAAC-----RRRTVAFVSTFATF--FTRAfdQIRMGAISQTNVNFVGSHcgCSI--GEDGPSQMGLEDIAMFRTIPGS 401
Cdd:COG0021 411 AMGAIMngialHGGLRPYGGTFLVFsdYMRP--AIRLAALMKLPVIYVFTH--DSIglGEDGPTHQPVEQLASLRAIPNL 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 402 TIFYPSDAVSTERAVELA-ANTKG-VCFIrTSRPNTCVIYDNEEPFT-IGRGKVVRQKSSD--EVLLIGAG--ITLyeCL 474
Cdd:COG0021 487 DVIRPADANETAAAWKLAlERKDGpTALI-LSRQNLPTLDRTAAAAEgVAKGAYVLADAEGtpDVILIATGseVSL--AV 563
|
570
....*....|....*.
gi 24645119 475 AAADQLEKNCITVRVI 490
Cdd:COG0021 564 EAAELLAAEGIKVRVV 579
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
3-225 |
8.96e-41 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 150.62 E-value: 8.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 3 VLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPIADLNNLRKIDSDLEGHP----TPRlnfIDVGTGS 77
Cdd:pfam00456 37 VLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSMEDLKSFRQLGSKTPGHPefghTAG---VEVTTGP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 78 LGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSL 148
Cdd:pfam00456 114 LGQGIANAVGMAIAERNlaatynrpgFDIVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFYDDNQISIDGETKI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24645119 149 QHKLDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEV 225
Cdd:pfam00456 194 SFTEDT-AARFEAYGWHVIeVEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNKQGTHDVHGAPLG--ADEV 268
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
450-570 |
1.61e-37 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 135.03 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 450 GKVVRQKSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEhGKQCGGRVVVVEDHYQQGGLGEA 529
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILE-SVKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24645119 530 VLSALAGE----RNFVVKHLYVPTVPRSGPPSVLIDMFGISARHV 570
Cdd:pfam02780 80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
78-579 |
5.31e-34 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 136.78 E-value: 5.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 78 LGQGvAVGAGMAYVG-KNFDKADYRTYVVVGDGE-------SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQ 149
Cdd:PRK12571 148 IGDG-SLTAGMAYEAlNNAGAADRRLIVILNDNEmsiappvGALAAYLSTLRSSDPFARLRAIAKGVEERLPGPLRDGAR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 150 HKLDVYRDR------LEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIE-DLDNWHGkplgdk 221
Cdd:PRK12571 227 RARELVTGMigggtlFEELGFTYVgPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEaDEDKYHA------ 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 222 aaevvkhlegliVNKNVKLTPKPvpkTGAAPdvdinniklsSPPAYklgdsiaTRLaYGTALAKIGQNNLRVVALDGDTK 301
Cdd:PRK12571 301 ------------VGKFDVVTGLQ---KKSAP----------SAPSY-------TSV-FGEELTKEAAEDSDIVAITAAMP 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 302 NSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQIRMG-AISQTNVNFVGSHCGCsIG 380
Cdd:PRK12571 348 LGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLHDvALQNLPVRFVLDRAGL-VG 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 381 EDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAV-ELAANTKGVCFIRTSRPNTC--VIYDNEEPFTIGRGKVVRQKS 457
Cdd:PRK12571 426 ADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEGVgvEIPAEGTILGIGKGRVPREGP 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 458 sdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELI---IEHGKqcggrVVVVEDHYQQGGLGEAVLSAL 534
Cdd:PRK12571 506 --DVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTdllVRHHI-----VVIVEEQGAMGGFGAHVLHHL 578
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 24645119 535 A--GERNFVVKhLYVPTVPR-----SGPPSVLIDMfGISARHVVNAVNEILK 579
Cdd:PRK12571 579 AdtGLLDGGLK-LRTLGLPDrfidhASREEMYAEA-GLTAPDIAAAVTGALA 628
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
318-434 |
1.11e-32 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 122.21 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 318 IECFIAEQNLVGVAVGAACRRRtVAFVSTFATFFTRAFDQIRMGAISQtNVNFVGSHCGC-SIGEDGPSQMGLEDIAMFR 396
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGGgGVGEDGPTHHSIEDEALLR 95
|
90 100 110
....*....|....*....|....*....|....*...
gi 24645119 397 TIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPN 434
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKS 133
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
322-540 |
1.79e-24 |
|
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: 104.33 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 322 IAEQNLVGVAVGAACR-RRTVAFVsTFATFFTRAFDQI-----RMGAIS--QTNVNFV-----GSHcgcsIGEdGP--SQ 386
Cdd:COG0022 58 ISEAGIVGAAIGAALAgLRPVVEI-QFADFIYPAFDQIvnqaaKLRYMSggQFKVPMVirtpyGGG----IGA-GAqhSQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 387 MgLEdiAMFRTIPGSTIFYPSDAvstERAVEL--AAntkgvcfIRTSRPntcVIY--------------DNEEPFTIGRG 450
Cdd:COG0022 132 S-LE--AWFAHIPGLKVVAPSTP---YDAKGLlkAA-------IRDDDP---VIFlehkrlyrlkgevpEEDYTVPLGKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 451 KVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGEAV 530
Cdd:COG0022 196 RVVRE--GTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEI 272
|
250
....*....|
gi 24645119 531 LSALAgERNF 540
Cdd:COG0022 273 AARIA-EEAF 281
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
74-535 |
5.13e-24 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 106.34 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 74 GTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEA-------- 145
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTAnldgptqp 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 146 --------TSLQHKLDVYRDR----LEAFGFNAV-VVDGHDVEELSKAFHCAAITKN-KPTAIIAKTFKGRDFPNIEDLD 211
Cdd:PLN02234 254 vgalscalSRLQSNCGMIRETsstlFEELGFHYVgPVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERAD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 212 nwhgkplgDKAAEVVKHleglivnknvkltpkpVPKTGAapdvDINNIklSSPPAYKLgdsiatrlAYGTALAKIGQNNL 291
Cdd:PLN02234 334 --------DKYHGVLKF----------------DPETGK----QFKNI--SKTQSYTS--------CFVEALIAEAEADK 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 292 RVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGA-ISQTNVNF 370
Cdd:PLN02234 376 DIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQVVHDVdLQKLPVRF 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 371 VGSHCGCsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVCFiRTSRPNTCVIY----DNEEP 444
Cdd:PLN02234 455 AIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSlppgNKGVP 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 445 FTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQG 524
Cdd:PLN02234 533 LQIGRGRILRD--GERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKS--HEVLITVEEGSIG 608
|
490
....*....|.
gi 24645119 525 GLGEAVLSALA 535
Cdd:PLN02234 609 GFGSHVVQFLA 619
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
314-578 |
2.13e-19 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 90.04 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 314 PQRYIECFIAEQNLVGVAVGAACR-RRTVAFVsTFATFFTRAFDQIrmgaisqtnVNFV-------GSHCGCSIGEDGPS 385
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNgLRPIAEF-MFADFIFPAFDQI---------VNEAakyrymsGGQFDCPIVIRGPN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 386 ----QMGLEDI----AMFRTIPGSTIFYPSDAVSTeRAVELAAntkgvcfIRTsrPNTCVIYDNE------------EPF 445
Cdd:PTZ00182 151 gavgHGGAYHSqsfeAYFAHVPGLKVVAPSDPEDA-KGLLKAA-------IRD--PNPVVFFEPKllyresvevvpeADY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 446 T--IGRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQ 523
Cdd:PTZ00182 221 TlpLGKAKVVREGK--DVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPT 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24645119 524 GGLGeAVLSALAGERNFvvKHLYVPTVPRSG-----PPSVLIDMFGI-SARHVVNAVNEIL 578
Cdd:PTZ00182 298 CGIG-AEIAAQIMEDCF--LYLEAPIKRVCGadtpfPYAKNLEPAYLpDKEKVVEAAKRVL 355
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
74-578 |
1.33e-18 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 89.57 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 74 GTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEAT------- 146
Cdd:PLN02582 142 GTGHSSTTISAGLGMA-VGRDLKGKKNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATldgpapp 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 147 ------------------------------------SLQHKLDVYRDRL---------EAFGFNAV-VVDGHDVEELSKA 180
Cdd:PLN02582 221 vgalssalsrlqssrplrelrevakgvtkqiggpmhELAAKVDEYARGMisgsgstlfEELGLYYIgPVDGHNIDDLVTI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 181 FHCAAITKNK-PTAIIAKTFKGRDFPNIEDL-DNWHGkplgdkaaeVVKHleglivnknvkltpkpVPKTGaapdvdinn 258
Cdd:PLN02582 301 LREVKSTKTTgPVLIHVVTEKGRGYPYAERAaDKYHG---------VVKF----------------DPATG--------- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 259 iklssppayKLGDSIATRLAYGT----ALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGA 334
Cdd:PLN02582 347 ---------KQFKVKAKTQSYTTyfaeALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 335 ACRRRTvAFVSTFATFFTRAFDQIRMGA-ISQTNVNFVGSHCGCsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTE 413
Cdd:PLN02582 418 ACEGLK-PFCAIYSSFLQRGYDQVVHDVdLQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELF 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 414 RAVELAA--NTKGVCFiRTSRPNTCVIYDNEE----PFTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITV 487
Cdd:PLN02582 496 HMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNnkgiPIEVGKGRILLE--GERVALLGYGTAVQSCLAAASLLERHGLSA 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 488 RVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQGGLGEAVLSALAGE---------RNFVVKHLYVptvpRSGPPSV 558
Cdd:PLN02582 573 TVADARFCKPLDRALIRSLAKS--HEVLITVEEGSIGGFGSHVAQFMALDglldgklkwRPLVLPDRYI----DHGAPAD 646
|
570 580
....*....|....*....|
gi 24645119 559 LIDMFGISARHVVNAVNEIL 578
Cdd:PLN02582 647 QLAEAGLTPSHIAATVLNVL 666
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
309-540 |
4.24e-17 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 82.46 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 309 LKNLDPQRYIECFIAEQNLVGVAVGAA-CRRRTVAFVSTFaTFFTRAFDQIRMGAiSQTNVnFVGSHCGCSIGEDGP--- 384
Cdd:PRK09212 45 LEQFGPKRVIDTPITEHGFAGLAVGAAfAGLRPIVEFMTF-NFSMQAIDQIVNSA-AKTNY-MSGGQLKCPIVFRGPnga 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 385 -----SQMGLEDIAMFRTIPGSTIFYPSdavsteraveLAANTKGVCFIRTSRPNTCVIYDNE-------------EPFT 446
Cdd:PRK09212 122 aarvaAQHSQCYAAWYSHIPGLKVVAPY----------FAADCKGLLKTAIRDPNPVIFLENEilyghshevpeeeESIP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 447 IGRGKVVRQKSSdeVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGL 526
Cdd:PRK09212 192 IGKAAILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGV 268
|
250
....*....|....
gi 24645119 527 GeAVLSALAGERNF 540
Cdd:PRK09212 269 G-AEIAALIMKEAF 281
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
1-201 |
4.76e-17 |
|
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: 83.12 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 1 MSVLFFQQLRlnlKHPRDPSSDRfILSKGHAAPILYA-AWAEaGLFPIADLNNLRKIDSD--LEGHPTPRL--NFIDVGT 75
Cdd:cd02017 43 YEVGFNHFFR---ARGEGGGGDL-VYFQGHASPGIYArAFLE-GRLTEEQLDNFRQEVGGggLSSYPHPWLmpDFWEFPT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 76 GSLGQGVAVGAGMA----YV---GKNfDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNR--------- 139
Cdd:cd02017 118 VSMGLGPIQAIYQArfnrYLedrGLK-DTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLqrldgpvrg 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 140 ----LGQSEAT--------------SLQHKL------DVYRDRLEA---------------------FG----FNAVVVD 170
Cdd:cd02017 197 ngkiIQELEGIfrgagwnvikviwgSKWDELlakdggGALRQRMEEtvdgdyqtlkakdgayvrehfFGkypeLKALVTD 276
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24645119 171 ------------GHDVEELSKAFHCAAITKNKPTAIIAKTFKG 201
Cdd:cd02017 277 lsdedlwalnrgGHDPRKVYAAYKKAVEHKGKPTVILAKTIKG 319
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
58-579 |
1.11e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 83.13 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 58 SDLEGHPTPRLN---FIDVGTGSlgQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVI 134
Cdd:PRK12315 94 DDVTGYTNPEESehdFFTVGHTS--TSIALATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIII 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 135 FDVNRLGQSEATS-LQHKLDVYRDR--------LEAFGFNAVVV-DGHDVEELSKAFHCAAITkNKPTAIIAKTFKGRDF 204
Cdd:PRK12315 170 VNDNQMSIAENHGgLYKNLKELRDTngqsennlFKAMGLDYRYVeDGNDIESLIEAFKEVKDI-DHPIVLHIHTLKGKGY 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 205 -PNIEDLDNWH-GKPLgdkaaevvkHLEglivnknvklTPKP-VPKTGAapdvDINNIKLSSppaykLGDSIAtrlaygt 281
Cdd:PRK12315 249 qPAEENKEAFHwHMPF---------DLE----------TGQSkVPASGE----SYSSVTLDY-----LLKKIK------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 282 alakigqNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRTVAFVstFATFFTRAFDQIRM 360
Cdd:PRK12315 294 -------EGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGiAANGARPVIFV--NSTFLQRAYDQLSH 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 361 G-AISQTNVNFVGShcGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAAN-TKGVCFIRTsrPNTCVI 438
Cdd:PRK12315 365 DlAINNNPAVMIVF--GGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTqHEHPVAIRV--PEHGVE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 439 YDNEEP--FTIGRGKVVRQKSsdEVLLIGAGiTLYEC-LAAADQL-EKNCITVRVIDPFTVKPLDAELiIEHGKQCGGRV 514
Cdd:PRK12315 441 SGPTVDtdYSTLKYEVTKAGE--KVAILALG-DFYELgEKVAKKLkEELGIDATLINPKFITGLDEEL-LEKLKEDHELV 516
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24645119 515 VVVEDHYQQGGLGEAVLSALAGER----NFVVKHLYVPTVprsgPPSVLIDMFGISARHVVNAVNEILK 579
Cdd:PRK12315 517 VTLEDGILDGGFGEKIARYYGNSDmkvlNYGAKKEFNDRV----PVEELYKRNHLTPEQIVEDILSVLK 581
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
74-199 |
1.79e-15 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 77.15 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 74 GTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDvNRLGQSEATSLQHKLD 153
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALK-YRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPTSRQTAGT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24645119 154 VYRDRLEAFGFNAVVVDGHDVEELSKAFHCA---AITKNKPTAIIAKTF 199
Cdd:cd02000 180 SIADRAAAYGIPGIRVDGNDVLAVYEAAKEAverARAGGGPTLIEAVTY 228
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
314-540 |
2.60e-14 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 75.34 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 314 PQRYIECFIAEQNLVGVAVGAACR--RRTVAFVsTFaTFFTRAFDQIRMGAiSQTNVnFVGSHCGCSIGEDGPS------ 385
Cdd:PRK11892 188 ARRVIDTPITEHGFAGIGVGAAFAglKPIVEFM-TF-NFAMQAIDQIINSA-AKTLY-MSGGQMGCPIVFRGPNgaaarv 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 386 --QMGLEDIAMFRTIPGSTIFYPSDAvsteravelaANTKGV--CFIRTsrPNTCVIYDNE------------EPFT--I 447
Cdd:PRK11892 264 aaQHSQDYAAWYSHIPGLKVVAPYSA----------ADAKGLlkAAIRD--PNPVIFLENEilygqsfdvpklDDFVlpI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 448 GRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLG 527
Cdd:PRK11892 332 GKARIHREGK--DVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVG 408
|
250
....*....|...
gi 24645119 528 eAVLSALAGERNF 540
Cdd:PRK11892 409 -AEIAARVMEQAF 420
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
295-570 |
2.75e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 72.83 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 295 ALDGDTKNSTFSDKLknldPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGAISQTN-VNFVGS 373
Cdd:PLN02225 407 GMEMDASLITFQERF----PDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVIT 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 374 HCGCsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVC--FIRTSRPNTCVIYDNEEPFTIGR 449
Cdd:PLN02225 482 SAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEIGR 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 450 GKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQGGLGEA 529
Cdd:PLN02225 561 GRVLVE--GQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQN--HKFLITVEEGCVGGFGSH 636
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24645119 530 VLS--ALAGERNFVVKhlYVPTVPRSG-----PPSVLIDMFGISARHV 570
Cdd:PLN02225 637 VAQfiALDGQLDGNIK--WRPIVLPDGyieeaSPREQLALAGLTGHHI 682
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
62-200 |
8.13e-11 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 63.11 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 62 GHPTPRLNFIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAghyKLDNLCVIFDV--NR 139
Cdd:pfam00676 87 GYYGAKGNRFYGGNGILGAQVPLGAGIALAAK-YRGKKEVAITLYGDGAANQGDFFEGLNFA---ALWKLPVIFVCenNQ 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24645119 140 LGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCA---AITKNKPTAIIAKTFK 200
Cdd:pfam00676 163 YGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAaerARTGKGPFLIELVTYR 226
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
74-204 |
1.63e-10 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 60.64 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 74 GTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVIFDVNRLGQSEATSLQHKLd 153
Cdd:cd02007 73 GTGHSSTSISAALGMA-VARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSISPNVGTPGNL- 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24645119 154 vyrdrLEAFGFNAV-VVDGHDVEELSKAFHCAAITKnKPTAIIAKTFKGRDF 204
Cdd:cd02007 150 -----FEELGFRYIgPVDGHNIEALIKVLKEVKDLK-GPVLLHVVTKKGKGY 195
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
309-540 |
1.60e-09 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 59.83 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 309 LKNLDPQRYIECFIAEQNLVGVAVGAACR--RRTVAFVsTFaTFFTRAFDQIRMGAISQTNVNfvGSHCGCSIGEDGP-- 384
Cdd:PLN02683 68 LQKYGPDRVLDTPITEAGFTGIGVGAAYAglKPVVEFM-TF-NFSMQAIDHIINSAAKTNYMS--AGQISVPIVFRGPng 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 385 ------SQMGLEDIAMFRTIPGSTIFYPSDAvSTERAVELAAntkgvcfIRTsrPNTCVIYDNE----EPFT-------- 446
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYSS-EDARGLLKAA-------IRD--PDPVVFLENEllygESFPvsaevlds 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 447 -----IGRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHY 521
Cdd:PLN02683 214 sfvlpIGKAKIEREGK--DVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|....*....
gi 24645119 522 QQGGLGeAVLSALAGERNF 540
Cdd:PLN02683 291 PQHGVG-AEICASVVEESF 308
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
70-198 |
5.61e-08 |
|
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: 52.64 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 70 FIDVGTGSLGQGV--AVGAGMAYvgknfdkADYRTYVVVGDGESAEGsiWESLHFAGHYKLDNLCVIFD----------- 136
Cdd:cd00568 40 LTSTGFGAMGYGLpaAIGAALAA-------PDRPVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNnggygtirmhq 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645119 137 VNRLGQSEATSLQHKLDvYRDRLEAFGFNAVVVDghDVEELSKAFHcAAITKNKPTAIIAKT 198
Cdd:cd00568 111 EAFYGGRVSGTDLSNPD-FAALAEAYGAKGVRVE--DPEDLEAALA-EALAAGGPALIEVKT 168
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
300-409 |
3.82e-06 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 46.95 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 300 TKNSTFSDKLKNLDPQRYIECfIAEQNLVGVAVGAA-CRRRTVAFVsTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCS 378
Cdd:cd06586 21 DEISSLLDALREGDKRIIDTV-IHELGAAGAAAGYArAGGPPVVIV-TSGTGLLNAINGLADAAAEHLPVVFLIGARGIS 98
|
90 100 110
....*....|....*....|....*....|.
gi 24645119 379 iGEDGPSQMGLEDIAMFRTIPGSTIFYPSDA 409
Cdd:cd06586 99 -AQAKQTFQSMFDLGMYRSIPEANISSPSPA 128
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
316-579 |
9.28e-06 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 47.81 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 316 RYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQI--RMGAISQTNvnfvGSHCGCSIGEDGPS----QMGL 389
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLGA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 390 EDI----AMFRTIPGSTIFypsdAVSTeravelAANTKGV--CFIRTSRPntcVIY--------------DNEEPFTIGR 449
Cdd:CHL00144 128 EHSqrleSYFQSVPGLQIV----ACST------PYNAKGLlkSAIRSNNP---VIFfehvllynlkeeipDNEYLLPLEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 450 GKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGeA 529
Cdd:CHL00144 195 AEVVRPGN--DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKT-HKVLIVEECMKTGGIG-A 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24645119 530 VLSALagernfVVKHLY--------------VPTvPRSGPpsvLIDMFGISARHVVNAVNEILK 579
Cdd:CHL00144 271 ELIAQ------INEHLFdeldapivrlssqdVPT-PYNGP---LEEATVIQPAQIIEAVEQIIT 324
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
29-201 |
9.42e-05 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 45.52 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 29 GHAAPILYA-AWAEaGLFPIADLNNLRK-IDSD-LEGHPTPRL--NFIDVGTGSLGQGvAVGA-------------GMAy 90
Cdd:PRK09405 144 GHASPGIYArAFLE-GRLTEEQLDNFRQeVDGKgLSSYPHPWLmpDFWQFPTVSMGLG-PIMAiyqarflkylenrGLK- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 91 vgknfDKADYRTYVVVGDGESAEGsiwESL---HFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRL 159
Cdd:PRK09405 221 -----DTSDQKVWAFLGDGEMDEP---ESLgaiSLAAREKLDNL--IFVIN-------CNLQ-RLDgpV-RgngkiiQEL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 160 EAF----GFNAV--------------------------VVDG-------------------------------------- 171
Cdd:PRK09405 282 EGIfrgaGWNVIkviwgsrwdpllakdtsgklvqlmneTVDGdyqtykakdgayvrehffgkypetkalvadmsdddiwa 361
|
250 260 270
....*....|....*....|....*....|....*
gi 24645119 172 -----HDVEELSKAFHCAAITKNKPTAIIAKTFKG 201
Cdd:PRK09405 362 lnrggHDPRKVYAAYKAAVEHKGQPTVILAKTIKG 396
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
29-201 |
1.13e-04 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 45.31 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 29 GHAAPILYA-AWAEaGLFPIADLNNLRK-IDSD-LEGHPTPRL--NFIDVGTGSLGQGVAVGA----GMAYVGKN--FDK 97
Cdd:PRK13012 152 PHSAPGIYArAFLE-GRLSEEQLDHFRQeIGGPgLSSYPHPWLmpDFWQFPTGSMGIGPINAIyqarFMRYLQHRglKDT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 98 ADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRLEAF----GFN 165
Cdd:PRK13012 231 SGRKVWGFFGDGEMDEPESIAALSLAAREGLDNL--VFVIN-------CNLQ-RLDgpV-RgngriiQELEALfrgaGWN 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 166 --------------------------AVVVD-------------------------------------------GHDVEE 176
Cdd:PRK13012 300 vikvlwgsdwdalfardttgalvrrfAETVDgqfqtfkandgaynrehffgqdpelaalvahlsdedidrlkrgGHDPRK 379
|
250 260
....*....|....*....|....*
gi 24645119 177 LSKAFHCAAITKNKPTAIIAKTFKG 201
Cdd:PRK13012 380 VYAAYAAAVRHKGQPTVILAKTKKG 404
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
29-201 |
1.54e-04 |
|
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]; Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 442021 [Multi-domain] Cd Length: 891 Bit Score: 44.68 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 29 GHAAPILYA-AWAEaGLFPIADLNNLRKidsDLEGH-----PTPRL--NFIDVGTGSLGQGvAVGA-------------G 87
Cdd:COG2609 145 GHASPGIYArAFLE-GRLTEEQLDNFRQ---EVDGKglssyPHPWLmpDFWQFPTVSMGLG-PINAiyqarfmkylhnrG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 88 MAyvgknfDKADYRTYVVVGDGESAEGsiwESL---HFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------ 156
Cdd:COG2609 220 LK------DTSDRKVWAFLGDGEMDEP---ESLgaiSLAAREKLDNL--IFVIN-------CNLQ-RLDgpV-Rgngkii 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 157 DRLEAF----GFNAV--------------------------VVDG----------------------------------- 171
Cdd:COG2609 280 QELEGVfrgaGWNVIkviwgsewdpllakdtdgalvkrmneTVDGdyqtykakdgayvrehffgkypelkalvadmsded 359
|
250 260 270
....*....|....*....|....*....|....*...
gi 24645119 172 --------HDVEELSKAFHCAAITKNKPTAIIAKTFKG 201
Cdd:COG2609 360 iwrlnrggHDPRKVYAAYKAAVEHKGQPTVILAKTIKG 397
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
74-202 |
1.80e-03 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 41.08 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 74 GTGSLGQGVAVGAGMAYVGK------NFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDnlcVIFDV-NRL---GQS 143
Cdd:PLN02374 192 GFAFIGEGIPVATGAAFSSKyrrevlKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLP---IVFVVeNNLwaiGMS 268
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645119 144 EATSLQHKlDVYRdRLEAFGFNAVVVDGHD---VEELSKAFHCAAITKNKPTAIIAKTFKGR 202
Cdd:PLN02374 269 HLRATSDP-EIWK-KGPAFGMPGVHVDGMDvlkVREVAKEAIERARRGEGPTLVECETYRFR 328
|
|
| PLN02269 |
PLN02269 |
Pyruvate dehydrogenase E1 component subunit alpha |
74-135 |
2.90e-03 |
|
Pyruvate dehydrogenase E1 component subunit alpha
Pssm-ID: 215152 [Multi-domain] Cd Length: 362 Bit Score: 40.08 E-value: 2.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24645119 74 GTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGhykLDNLCVIF 135
Cdd:PLN02269 136 GHGIVGAQVPLGAGLAFAQK-YNKEENVAFALYGDGAANQGQLFEALNIAA---LWDLPVIF 193
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
314-409 |
6.66e-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: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24645119 314 PQRYIECFIAEQNLVGVAVGAACR--RRTVAFvsTFATFFTRAFDQIR--------MGAiSQTNVNFV--GShCGCSIGe 381
Cdd:cd07036 43 PDRVIDTPIAEAGIVGLAVGAAMNglRPIVEI--MFADFALPAFDQIVneaaklryMSG-GQFKVPIVirGP-NGGGIG- 117
|
90 100 110
....*....|....*....|....*....|
gi 24645119 382 DGP--SQmGLEdiAMFRTIPGSTIFYPSDA 409
Cdd:cd07036 118 GGAqhSQ-SLE--AWFAHIPGLKVVAPSTP 144
|
|
| |
