|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
7-621 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 572.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 7 DEKTLQALKDIANKLRIHSIRQTCASNSGHPTSCCSAAELMSVLFFHTMRYKAGDPRNPCNDRFILSKGHAAPILYAAWA 86
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 87 EAGY-IKASDLLNLRKIDSDLEGHPTP-KLAFVDVATGSLGQGLGAACGMAYTGKYLDK---------SSYRVYCMLGDG 155
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYgHTPGVETTTGPLGQGLANAVGMALAEKYLAAlfnrpgldiVDHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 156 ECSEGSVWEAMAFASHYKLDNLVAILDVNRLGQSEPAPLQHNVNvYKERCEAFGFNTYVVDGHDVEELCKAMWHAEGVKg 235
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 236 KPTAIVAKTFKGKGLKGIEDQDNWHGKPMPKDRAEELIndllsqiqspnkplypqppKEdappadlspihlltapeykLG 315
Cdd:PRK05899 239 KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAK-------------------KE-------------------LG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 316 dkISTRKAYGVALKRLGDASTRVVALDGDTKNSTFADMF------KKAHPDRYIECFIAEQNMVSVAIGCATRERTVSFA 389
Cdd:PRK05899 281 --WDYRKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFG 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 390 STFAAFLARAYDQIRMAAISQSNVNLVGSHCGVSIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAA-NTK 468
Cdd:PRK05899 359 GTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKD 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 469 GICFIRTSRPDTAVIYNP--EEKFEIGkAKVVRQSSkdQVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDAS 546
Cdd:PRK05899 439 GPSALVLTRQNLPVLERTaqEEGVAKG-GYVLRDDP--DVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 547 tivasaratggrvitvEDHYKEGGLGEAVLSAVGEEPGIV----------VHRLAVSRVPRSGKPQELLDMFGISAKCIV 616
Cdd:PRK05899 516 ----------------DAAYKESVLPAAVTARVAVEAGVAdgwykyvgldGKVLGIDTFGASAPADELFKEFGFTVENIV 579
|
....*
gi 186288308 617 AAVKR 621
Cdd:PRK05899 580 AAAKE 584
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
19-273 |
1.90e-140 |
|
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: 408.82 E-value: 1.90e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 19 NKLRIHSIRQTCASNSGHPTSCCSAAELMSVLFFHTMRYKAGDPRNPCNDRFILSKGHAAPILYAAWAEAGYIKASDLLN 98
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 99 LRKIDSDLEGHPTPKL-AFVDVATGSLGQGLGAACGMAYTGKYLdKSSYRVYCMLGDGECSEGSVWEAMAFASHYKLDNL 177
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 178 VAILDVNRLGQSEPAPLQHNVNVYKERCEAFGFNTYVVDGHDVEELCKAMWHAEGVKGKPTAIVAKTFKGKGLKGIEDQD 257
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*.
gi 186288308 258 NWHGKPMPKDRAEELI 273
Cdd:cd02012 240 KWHGKPLGEEEVELAK 255
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
316-621 |
3.72e-120 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 359.01 E-value: 3.72e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 316 DKISTRKAYGVALKRLGDASTRVVALDGDTKNSTFADMFKKAHPDRYIECFIAEQNMVSVAIGCATRERTVsFASTFAAF 395
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIP-FVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 396 LA-RAYDQIRMA-AISQSNVNLVGSHCGVSIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAANTKGICFI 473
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 474 RTSRPDTAVIYNPEEKFEIGKAKVVRQSSKdqVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASAR 553
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186288308 554 ATgGRVITVEDHYKEGGLGEAVLSAVGEEPGIVVHRLAVS-RVPRSGKPQELLDMFGISAKCIVAAVKR 621
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKE 306
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
7-281 |
3.39e-119 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 355.15 E-value: 3.39e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 7 DEKTLQALKDIANKLRIHSIRQTCASNSGHPTSCCSAAELMSVLFFHTMRYKAGDPRNPCNDRFILSKGHAAPILYAAWA 86
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 87 EAGYIKASDLLNLRKIDSDLEGHPTP-KLAFVDVATGSLGQGLGAACGMAYTGKyLDKSSYRVYCMLGDGECSEGSVWEA 165
Cdd:COG3959 81 EKGYFPKEELATFRKLGSRLQGHPDMkKTPGVEMSTGSLGQGLSVAVGMALAAK-LDGKDYRVYVLLGDGELQEGQVWEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 166 MAFASHYKLDNLVAILDVNRL---GQSE----PAPLqhnvnvyKERCEAFGFNTYVVDGHDVEELCKAMWHAEGVKGKPT 238
Cdd:COG3959 160 AMAAAHYKLDNLIAIVDRNGLqidGPTEdvmsLEPL-------AEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 186288308 239 AIVAKTFKGKGLKGIEDQDNWHGKPMPKDRAEELINDLLSQIQ 281
Cdd:COG3959 233 VIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELG 275
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
15-622 |
1.87e-73 |
|
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: 248.48 E-value: 1.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 15 KDIANKLRIHSIRQTCASNSGHPTSCCSAAELMSVLFFHTMRYkagDPRNPC---NDRFILSKGHAAPILYAAWAEAGYI 91
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKF---NPTNPKwinRDRFVLSNGHGSMLLYSLLHLTGYD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 92 KA-SDLLNLRKIDSDLEGHPT-PKLAFVDVATGSLGQGLGAACGMAYTGKYL---------DKSSYRVYCMLGDGECSEG 160
Cdd:TIGR00232 78 LSiEDLKQFRQLHSKTPGHPEyGHTAGVEATTGPLGQGIANAVGMAIAEKTLaatfnkpgfEIVDHYTYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 161 SVWEAMAFASHYKLDNLVAILDVNRLGQSEPAPLQHNVNVyKERCEAFGFNT-YVVDGHDVEELCKAMWHAEGVKGKPTA 239
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVlEVEDGHDLAAIDAAIEEAKASTDKPTL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 240 IVAKTFKGKGLKGIEDQDNWHGKPMPKD-----------------------------------RAEELINDLLSQIqspn 284
Cdd:TIGR00232 237 IEVKTTIGFGSPNKAGTHGVHGAPLGDEevaltkknlgwnynpfeipqevydhfkktvkergaKAEQEWNELFAAY---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 285 KPLYPQPPKE--DAPPADLSPIHLLTAPEYKLGDK-ISTRKAYGVALKRLGDASTRVVALDGDTKNSTF-----ADMFKK 356
Cdd:TIGR00232 313 KKKYPELAAEftRRLSGELPADWDKQLPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLtkwkgSGDLHE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 357 AHPDRYIECFIAEQNMVSVAIGCATRERTVSFASTFAAFLARAYDQIRMAAISQSNVNLVGSHCGVSIGEDGPSQMALED 436
Cdd:TIGR00232 393 NPLGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 437 LAMFRAIPTCTVFYPSDGVSTERSVELA-ANTKGICFIRTSRPDTAVIyNPEEKFEIGKAKVVRQSSKD-QVTVIGAGVT 514
Cdd:TIGR00232 473 LASLRAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQL-EESSLEKVLKGGYVLKDSKGpDLILIATGSE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 515 LHEALAAHDQLAKEGVNIRV-----IDPFTIKPL--------DASTIVA--SARATGgrvitvedHYKEGGLGEAVLSAv 579
Cdd:TIGR00232 552 VQLAVEAAKKLAAENIKVRVvsmpsFDLFDKQDEeyresvlpANVTRLAieAGAADE--------WYKYAGLVGAILGM- 622
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 186288308 580 geepgivvhrlavSRVPRSGKPQELLDMFGISAKCIVAAVKRT 622
Cdd:TIGR00232 623 -------------DSFGESAPGDKLFEEFGFTVENVVAKAKKL 652
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
322-477 |
3.77e-67 |
|
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: 216.15 E-value: 3.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 322 KAYGVALKRLGDASTRVVALDGDTKNSTFADMFKKAHPDRYIECFIAEQNMVSVAIGCATrERTVSFASTFAAFLARAYD 401
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLAL-HGLKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186288308 402 QIR-MAAISQSNVNLVGSHCGVSIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAANTKGICFIRTSR 477
Cdd:cd07033 80 QIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
17-535 |
1.61e-60 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 213.38 E-value: 1.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 17 IANKLRIHSIRQTCASNSGHPTSCCSAAELMSVLFFHTMRYKAGDPRNPCNDRFILSKGHAAPILYAAWAEAGY-IKASD 95
Cdd:PTZ00089 9 CANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMED 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 96 LLNLRKIDSDLEGHP----TPKlafVDVATGSLGQGLGAACGMAYTGKYLDKSSYR---------VYCMLGDGECSEGSV 162
Cdd:PTZ00089 89 LKNFRQLGSRTPGHPerhiTPG---VEVTTGPLGQGIANAVGLAIAEKHLAAKFNRpghpifdnyVYVICGDGCLQEGVS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 163 WEAMAFASHYKLDNLVAILDVNRLGQSEPAPLQHNVNVYKeRCEAFGFNTYVVD--GHDVEELCKAMWHAEGVKGKPTAI 240
Cdd:PTZ00089 166 QEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEK-KYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 241 VAKTFKGKGLKgIEDQDNWHGKPMpkdrAEELINDLLSQI-QSPNKPLYPQP---------------------------- 291
Cdd:PTZ00089 245 IVKTTIGYGSS-KAGTEKVHGAPL----GDEDIAQVKELFgLDPEKKFHVSEevrqffeqhvekkkenyeawkkrfakyt 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 292 ---PKEDAP-----PADLSPIHLLTAPEYKLGDK-ISTRKAYGVALKRLGDASTRVVALDGDTKNSTF-----ADMFKKA 357
Cdd:PTZ00089 320 aafPKEAQAierrfKGELPPGWEKKLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLtrpkeANDFTKA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 358 HPD-RYIECFIAEQNMVSVAIGCATRERTVSFASTFAAFLARAYDQIRMAAISQSNVNLVGSHCGVSIGEDGPSQMALED 436
Cdd:PTZ00089 400 SPEgRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVET 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 437 LAMFRAIPTCTVFYPSDGVSTERSVELA-ANTKGICFIRTSRPDTAVIYNPEEKFEIGKAKVVRQSSKD-QVTVIGAGVT 514
Cdd:PTZ00089 480 LALLRATPNLLVIRPADGTETSGAYALAlANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFTNSpQLILVASGSE 559
|
570 580
....*....|....*....|.
gi 186288308 515 LHEALAAHDQLAKEgVNIRVI 535
Cdd:PTZ00089 560 VSLCVEAAKALSKE-LNVRVV 579
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
128-623 |
3.25e-58 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 205.32 E-value: 3.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 128 LGAACGMAYTGKYLDKSSYRVYCMLGDGECSEGSVWEAMAFASHYKlDNLVAILDVNRLGQSEP--------APLQHNvN 199
Cdd:PRK05444 123 ISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDNEMSISPNvgalsnylARLRSS-T 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 200 VYkercEAFGFNtYV--VDGHDVEELCKAMWHAEGVKGkPTAIVAKTFKGKGLKGIE-DQDNWHGkpmpkdraeelindl 276
Cdd:PRK05444 201 LF----EELGFN-YIgpIDGHDLDALIETLKNAKDLKG-PVLLHVVTKKGKGYAPAEaDPIKYHG--------------- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 277 lsqiQSPNKPLYPQPPKEDAPPAdlspihlltaPEYKlgdkistrKAYGVALKRLGDASTRVVALDGDTKNSTFADMFKK 356
Cdd:PRK05444 260 ----VGKFDPETGEQPKSSKPGK----------PSYT--------KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 357 AHPDRYIECFIAEQNMVSVAIGCATrERTVSFASTFAAFLARAYDQIRM-AAISQSNVNLVGSHCGVSiGEDGPSQMALE 435
Cdd:PRK05444 318 RFPDRYFDVGIAEQHAVTFAAGLAT-EGLKPVVAIYSTFLQRAYDQVIHdVALQNLPVTFAIDRAGLV-GADGPTHQGAF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 436 DLAMFRAIPTCTVFYPSDGVSTERSVELA-ANTKGICFIRTSR-PDTAVIYNPEEKFEIGKAKVVRQSSKdqVTVIGAGV 513
Cdd:PRK05444 396 DLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRgNGVGVELPELEPLPIGKGEVLREGED--VAILAFGT 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 514 TLHEALAAHDQLAkegvNIRVIDPFTIKPLDASTIVASARaTGGRVITVEDHYKEGGLGEAVLSAVGEE-PGIVVHRLAV 592
Cdd:PRK05444 474 MLAEALKAAERLA----SATVVDARFVKPLDEELLLELAA-KHDLVVTVEEGAIMGGFGSAVLEFLADHgLDVPVLNLGL 548
|
490 500 510
....*....|....*....|....*....|...
gi 186288308 593 --SRVPRsGKPQELLDMFGISAKCIVAAVKRTF 623
Cdd:PRK05444 549 pdEFIDH-GSREELLAELGLDAEGIARRILELL 580
|
|
| PLN02790 |
PLN02790 |
transketolase |
31-535 |
6.55e-58 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 206.03 E-value: 6.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 31 ASNSGHPTSCCSAAELMSVLFFHTMRYKAGDPRNPCNDRFILSKGHAAPILYAAWAEAGY--IKASDLLNLRKIDSDLEG 108
Cdd:PLN02790 11 KANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQFRQWGSRTPG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 109 HP----TPKlafVDVATGSLGQGLGAACGMAYTGKYL---------DKSSYRVYCMLGDGECSEGSVWEAMAFASHYKLD 175
Cdd:PLN02790 91 HPenfeTPG---IEVTTGPLGQGIANAVGLALAEKHLaarfnkpdhKIVDHYTYCILGDGCQMEGISNEAASLAGHWGLG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 176 NLVAILDVNRLGQSEPAPLQHNVNVYKeRCEAFGFNTYVVDG--HDVEELCKAMWHAEGVKGKPTAIVAKTFKGKGLKGI 253
Cdd:PLN02790 168 KLIVLYDDNHISIDGDTEIAFTEDVDK-RYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYGSPNK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 254 EDQDNWHGKPMPKDRAE----------------ELINDLLSQIQSPNKPLYPQPPK-----EDAPPADLSPIHLLTA--- 309
Cdd:PLN02790 247 ANSYSVHGAALGEKEVDatrknlgwpyepfhvpEDVKSHWSKHTKEGAALEAEWNAkfaeyKKKYPEEAAELKSLISgel 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 310 --------PEYKLGDKI-STRKAYGVALKRLGDASTRVVALDGDTKNSTFADM-----FKKAHP-DRYIECFIAEQNMVS 374
Cdd:PLN02790 327 psgwekalPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPeERNVRFGVREHGMGA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 375 VAIGCAT-RERTVSFASTFAAFLARAYDQIRMAAISQSNVNLVGSHCGVSIGEDGPSQMALEDLAMFRAIPTCTVFYPSD 453
Cdd:PLN02790 407 ICNGIALhSSGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNILMLRPAD 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 454 GVSTERSVELA-ANTKG---ICFIRTSRPDTAVIYnpEEKFEIGKAKVVRQSSKDQ--VTVIGAGVTLHEALAAHDQLAK 527
Cdd:PLN02790 487 GNETAGAYKVAvTNRKRptvLALSRQKVPNLPGTS--IEGVEKGGYVISDNSSGNKpdLILIGTGSELEIAAKAAKELRK 564
|
....*...
gi 186288308 528 EGVNIRVI 535
Cdd:PLN02790 565 EGKKVRVV 572
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
15-535 |
1.06e-56 |
|
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: 202.93 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 15 KDIANKLRIHSIRQTCASNSGHPTSCCSAAELMSVLFFHTMRYkagDPRNP--CN-DRFILSKGHAAPILYAAWAEAGY- 90
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKH---NPANPkwPNrDRFVLSAGHGSMLLYSLLHLTGYd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 91 IKASDLLNLRKIDSDLEGHP----TPklaFVDVATGSLGQGLGAACGMAYTGKYL----DKSSY-----RVYCMLGDGEC 157
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPeyghTP---GVETTTGPLGQGIANAVGMAIAERHLaarfNRPGHdivdhYTYVIAGDGDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 158 SEGSVWEAMAFASHYKLDNLVAILDVNR--------LGQSEpaplqhNVnvyKERCEAFGFNTY-VVDGHDVEELCKAMW 228
Cdd:COG0021 159 MEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdLAFSE------DV---AKRFEAYGWHVIrVEDGHDLEAIDAAIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 229 HAEGVKGKPTAIVAKTFKGKGLKGIEDQDNWHGKPMPKD----------------------------------RAEELIN 274
Cdd:COG0021 230 AAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGAPLGAEeiaatkealgwppepfevpdevyahwraagergaAAEAEWN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 275 DLLSQIQSpnkpLYPQPPKE------DAPPADLSPihllTAPEYKLGDK-ISTRKAYGVALKRLGDAstrVVALDG---D 344
Cdd:COG0021 310 ERFAAYAA----AYPELAAElerrlaGELPEDWDA----ALPAFEADAKgVATRKASGKVLNALAPV---LPELIGgsaD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 345 TKNSTFADM-----FKKAHPD-RYIECFIAEQNMVSVAIGCATRERTVSFASTFAAF--LARAydQIRMAAISQSNVNLV 416
Cdd:COG0021 379 LAGSNKTTIkgagsFSPEDPSgRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFsdYMRP--AIRLAALMKLPVIYV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 417 GSHCGVSIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELA-ANTKG-ICFIrTSRPDTAVIYNPEEKFE-IG 493
Cdd:COG0021 457 FTHDSIGLGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLAlERKDGpTALI-LSRQNLPTLDRTAAAAEgVA 535
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 186288308 494 K-AKVVRQSSKD-QVTVIGAGVTLHEALAAHDQLAKEGVNIRVI 535
Cdd:COG0021 536 KgAYVLADAEGTpDVILIATGSEVSLAVEAAELLAAEGIKVRVV 579
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
206-624 |
5.93e-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: 183.29 E-value: 5.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 206 EAFGFNtYV--VDGHDVEELCKAMWHAEGVKGkPTAIVAKTFKGKGLK-GIEDQDNWHGkPMPKDRAE-ELINDllsqiq 281
Cdd:COG1154 242 EELGFK-YIgpIDGHDLDALVETLRNAKDLKG-PVLLHVVTKKGKGYApAEKDPDKFHG-VGPFDPETgEPKKS------ 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 282 SPNKPLYPQppkedappadlspihlltapeyklgdkistrkAYGVALKRLGDASTRVVALdgdtknsTFAdM-------- 353
Cdd:COG1154 313 KSSAPSYTD--------------------------------VFGDTLVELAEKDPRIVAI-------TAA-Mpegtgldk 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 354 FKKAHPDRYIECFIAEQNMVSVAIGCATR-ERTVsFA--STFaafLARAYDQIRM-AAISQSNVN-------LVgshcgv 422
Cdd:COG1154 353 FAERFPDRFFDVGIAEQHAVTFAAGLATEgLKPV-VAiySTF---LQRAYDQVIHdVALQNLPVTfaidragLV------ 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 423 siGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAANTKGICFIRTSR---PDTAvIYNPEEKFEIGKAKVVR 499
Cdd:COG1154 423 --GADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgngPGVE-LPAELEPLPIGKGEVLR 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 500 QSSKdqVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARaTGGRVITVEDHYKEGGLGEAVLSAV 579
Cdd:COG1154 500 EGKD--VAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAR-EHDLVVTVEEGVLAGGFGSAVLEFL 576
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 186288308 580 GEEpGIV--VHRLAvsrVPRS----GKPQELLDMFGISAKCIVAAVKRTFA 624
Cdd:COG1154 577 ADA-GLDvpVLRLG---LPDRfiehGSRAELLAELGLDAEGIARAILELLG 623
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
316-482 |
2.47e-47 |
|
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Pssm-ID: 460692 [Multi-domain] Cd Length: 174 Bit Score: 163.88 E-value: 2.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 316 DKISTRKAYGVALKRLGDASTRVVALDGDTKNSTFADMFKKAHPD---RYIECFIAEQNMVSVAIGCATRER-TVSFAST 391
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 392 FAAFLARAYDQIR-MAAISQSNVNLVGSHCGVSIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAANTKGI 470
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|....
gi 186288308 471 --CFIRTSRPDTAV 482
Cdd:pfam02779 161 kpVVLRLPRQLLRP 174
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
15-267 |
4.78e-40 |
|
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: 149.46 E-value: 4.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 15 KDIANKLRIHSIRQTCASNSGHPTSCCSAAELMSVLFFHTMRYKAGDPRNPCNDRFILSKGHAAPILYAAWAEAGY-IKA 93
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 94 SDLLNLRKIDSDLEGHPTPK-LAFVDVATGSLGQGLGAACGMAYTGKYL---------DKSSYRVYCMLGDGECSEGSVW 163
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPEFGhTAGVEVTTGPLGQGIANAVGMAIAERNLaatynrpgfDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 164 EAMAFASHYKLDNLVAILDVNRL---GQSEPAplqhNVNVYKERCEAFGFNT-YVVDGHDVEELCKAMWHAEGVKGKPTA 239
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQIsidGETKIS----FTEDTAARFEAYGWHViEVEDGHDVEAIAAAIEEAKAEKDKPTL 238
|
250 260
....*....|....*....|....*...
gi 186288308 240 IVAKTFKGKGLKGIEDQDNWHGKPMPKD 267
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAPLGAD 266
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
128-624 |
2.75e-38 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 150.26 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 128 LGAACGMAyTGKYLDKSSYRVYCMLGDGECSEGSVWEAMAFASHYKlDNLVAILDVN----------------------- 184
Cdd:PRK12571 125 ISAALGFA-KARALGQPDGDVVAVIGDGSLTAGMAYEALNNAGAAD-RRLIVILNDNemsiappvgalaaylstlrssdp 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 185 ---------RLGQSEPAPLQHNVNVYKERC----------EAFGFnTYV--VDGHDVEELCKAMWHAEGVKGKPTAIVAK 243
Cdd:PRK12571 203 farlraiakGVEERLPGPLRDGARRARELVtgmigggtlfEELGF-TYVgpIDGHDMEALLSVLRAARARADGPVLVHVV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 244 TFKGKGLKGIE-DQDNWHGKPmpkdraeelINDLLSQIQSPNKPlypqppkedappadlspihllTAPEYKlgdkistrK 322
Cdd:PRK12571 282 TEKGRGYAPAEaDEDKYHAVG---------KFDVVTGLQKKSAP---------------------SAPSYT--------S 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 323 AYGVALKRLGDASTRVVALDGDTKNSTFADMFKKAHPDRYIECFIAEQNMVSVAIGCATrERTVSFASTFAAFLARAYDQ 402
Cdd:PRK12571 324 VFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAA-AGLKPFCAVYSTFLQRGYDQ 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 403 IRM-AAISQSNVNLVGSHCGVsIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSV-ELAANTKGICFIRTSRPDT 480
Cdd:PRK12571 403 LLHdVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEG 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 481 AVIYNPEEK--FEIGKAKVVRQSSKdqVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIvasARATGGR 558
Cdd:PRK12571 482 VGVEIPAEGtiLGIGKGRVPREGPD--VAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALT---DLLVRHH 556
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186288308 559 -VITVEDHYKEGGLGEAVLSAVGEEpGIVVHRLAVS--RVPRS----GKPQELLDMFGISAKCIVAAVKRTFA 624
Cdd:PRK12571 557 iVVIVEEQGAMGGFGAHVLHHLADT-GLLDGGLKLRtlGLPDRfidhASREEMYAEAGLTAPDIAAAVTGALA 628
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
493-615 |
1.54e-36 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 132.72 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 493 GKAKVVRQssKDQVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARATgGRVITVEDHYKEGGLG 572
Cdd:pfam02780 1 GKAEILRE--GDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 186288308 573 EAVLSAVGEE----PGIVVHRLAVSRVPRSGKPQELLDMFGISAKCI 615
Cdd:pfam02780 78 SEVAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
35-309 |
6.69e-32 |
|
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: 127.42 E-value: 6.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 35 GHPTSCCSAAELMSVLFFHTMRYKAGDPRNpcnDRfILSKGHAAPILYA-AWAEaGYIKASDLLNLRKIDSD--LEGHPT 111
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEGGGG---DL-VYFQGHASPGIYArAFLE-GRLTEEQLDNFRQEVGGggLSSYPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 112 PKL--AFVDVATGSLGQGLGAACGMAYTGKYL------DKSSYRVYCMLGDGECSEGSVWEAMAFASHYKLDNLVAILDV 183
Cdd:cd02017 106 PWLmpDFWEFPTVSMGLGPIQAIYQARFNRYLedrglkDTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 184 NRlgQSEPAPLQHNV---------------NVYK-----ERCEAFG---------------------------------- 209
Cdd:cd02017 186 NL--QRLDGPVRGNGkiiqelegifrgagwNVIKviwgsKWDELLAkdgggalrqrmeetvdgdyqtlkakdgayvrehf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 210 FNTYVVD------------------GHDVEELCKAMWHAEGVKGKPTAIVAKTFKGKGLKGIEDQDN-WHG-KPMPKDRA 269
Cdd:cd02017 264 FGKYPELkalvtdlsdedlwalnrgGHDPRKVYAAYKKAVEHKGKPTVILAKTIKGYGLGAAGEGRNhAHQvKKMTEDEL 343
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 186288308 270 EEL---INDLLSQIQSPNKPLYPQPPKEDAPPADLSPIHLLTA 309
Cdd:cd02017 344 KALrdrFGIPVSDEQLEEGPYYKPPEGSEEIKYLHERRHALGG 386
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
317-477 |
2.79e-31 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 118.36 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 317 KISTRKAYGVALKRLGdastrvvaldgdtknstfadmfkkahpdryIECFIAEQNMVSVAIGCATRERTVsFASTFAAFL 396
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGLRP-VVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 397 ARAYDQIRMAAISQSNVNLVGSHCGVSIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAANTKGICFIRTS 476
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 186288308 477 R 477
Cdd:smart00861 131 R 131
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
351-624 |
1.34e-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: 110.88 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 351 ADMFKKAHPDRyieCF---IAEQNMVSVAIGcatrertvsFAST---------FAAFLARAYDQIR--MAAIS-----QS 411
Cdd:COG0022 42 KGLQEKFGPDR---VFdtpISEAGIVGAAIG---------AALAglrpvveiqFADFIYPAFDQIVnqAAKLRymsggQF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 412 NVNLV-----GSHcgvsIGEdGP--SQMaLEdlAMFRAIPTCTVFYPSDgvstersvelAANTKGicFIRTS--RPDTAV 482
Cdd:COG0022 110 KVPMVirtpyGGG----IGA-GAqhSQS-LE--AWFAHIPGLKVVAPST----------PYDAKG--LLKAAirDDDPVI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 483 I------YN-----PEEKFE--IGKAKVVRQSSkdQVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIV 549
Cdd:COG0022 170 FlehkrlYRlkgevPEEDYTvpLGKARVVREGT--DVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETIL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 550 ASARATgGRVITVEDHYKEGGLGEAVLSAVGEE-------PgivVHRLAV--SRVPRSgkpQELLDMFGISAKCIVAAVK 620
Cdd:COG0022 248 ESVKKT-GRLVVVDEAPRTGGFGAEIAARIAEEafdyldaP---VKRVTGpdTPIPYA---PALEKAYLPSADRIVAAVR 320
|
....
gi 186288308 621 RTFA 624
Cdd:COG0022 321 ELLA 324
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
131-622 |
4.57e-25 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 109.71 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 131 ACGMAyTGKYLDKSSYRVYCMLGDGECSEGSVWEAMAFASHYKlDNLVAILDVNRL--------------------GQSE 190
Cdd:PRK12315 122 ATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMsiaenhgglyknlkelrdtnGQSE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 191 paplqhnVNVYKerceAFGFN-TYVVDGHDVEELCKAMwhaEGVK--GKPTAIVAKTFKGKGLK-GIEDQDNWHGKpMPK 266
Cdd:PRK12315 200 -------NNLFK----AMGLDyRYVEDGNDIESLIEAF---KEVKdiDHPIVLHIHTLKGKGYQpAEENKEAFHWH-MPF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 267 DraeelindllsqiqspnkplypqppkedapPADLSPIHLLTAPEYKlgdkiSTRKAYgvaLKRLGDASTRVVALDGDTK 346
Cdd:PRK12315 265 D------------------------------LETGQSKVPASGESYS-----SVTLDY---LLKKIKEGKPVVAINAAIP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 347 NSTFADMFKKAHPDRYIECFIAEQNMVSVAIGCATR-ERTVSFasTFAAFLARAYDQIR--MAAISQSNVNLVGshcGVS 423
Cdd:PRK12315 307 GVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANgARPVIF--VNSTFLQRAYDQLShdLAINNNPAVMIVF---GGS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 424 IGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAAN-TKGICFIRTsrPDTAVIYNPEEKFEIGKAK--VVRQ 500
Cdd:PRK12315 382 ISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTqHEHPVAIRV--PEHGVESGPTVDTDYSTLKyeVTKA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 501 SSKdqVTVIGAGVTLHEALAAHDQLAKE-GVNIRVIDPFTIKPLDASTIvASARATGGRVITVEDHYKEGGLGEAVLSAV 579
Cdd:PRK12315 460 GEK--VAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELL-EKLKEDHELVVTLEDGILDGGFGEKIARYY 536
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 186288308 580 GEEPGIVVH----RLAVSRVPrsgkPQELLDMFGISAKCIVAAVKRT 622
Cdd:PRK12315 537 GNSDMKVLNygakKEFNDRVP----VEELYKRNHLTPEQIVEDILSV 579
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
120-576 |
2.42e-20 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 95.16 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 120 ATGSLGQGLGAACGMAyTGKYLDKSSYRVYCMLGDGECSEGSVWEAMAFAShYKLDNLVAILDVNRL---------GQSE 190
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG-YLHSNMIVILNDNKQvslptanldGPTQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 191 P--------APLQHNVNVYKERC----EAFGFNtYV--VDGHDVEELCKAMWHAEGVKG-KPTAIVAKTFKGKGLKGIED 255
Cdd:PLN02234 253 PvgalscalSRLQSNCGMIRETSstlfEELGFH-YVgpVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAER 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 256 QDNWHGKPMPKDRAeelindllsqiqspnkplypqppkedappadlspihllTAPEYKlgdKISTRKAYGV----ALKRL 331
Cdd:PLN02234 332 ADDKYHGVLKFDPE--------------------------------------TGKQFK---NISKTQSYTScfveALIAE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 332 GDASTRVVALDGDTKNSTFADMFKKAHPDRYIECFIAEQNMVSVAIGCATrERTVSFASTFAAFLARAYDQ-IRMAAISQ 410
Cdd:PLN02234 371 AEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLAC-EGLKPFCTIYSSFMQRAYDQvVHDVDLQK 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 411 SNVNLVGSHCGVsIGEDGPSQMALEDLAMFRAIPTCTVFYPSDGVSTERSVELAA--NTKGICFIRTSRPDTAVIYNPEE 488
Cdd:PLN02234 450 LPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCFRYHRGNGIGVSLPPGN 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 489 K---FEIGKAKVVRQSskDQVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARATgGRVITVEDH 565
Cdd:PLN02234 529 KgvpLQIGRGRILRDG--ERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH-EVLITVEEG 605
|
490
....*....|.
gi 186288308 566 yKEGGLGEAVL 576
Cdd:PLN02234 606 -SIGGFGSHVV 615
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
352-582 |
1.45e-19 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 90.43 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 352 DMFKKAHPDRYIECFIAEQNMVSVAIGCATRERTVSFASTFAAFLARAYDQI-------RMAAISQSNVNLV-GSHCGVS 423
Cdd:PTZ00182 74 GLLDKYGPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIvneaakyRYMSGGQFDCPIViRGPNGAV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 424 iGEDGP--SQmALEdlAMFRAIPTCTVFYPSDGVSTeRSVELAAntkgicfIRTSRP----DTAVIYN------PEEKFE 491
Cdd:PTZ00182 154 -GHGGAyhSQ-SFE--AYFAHVPGLKVVAPSDPEDA-KGLLKAA-------IRDPNPvvffEPKLLYResvevvPEADYT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 492 --IGKAKVVRQSsKDqVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARATgGRVITVEDHYKEG 569
Cdd:PTZ00182 222 lpLGKAKVVREG-KD-VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPTC 298
|
250
....*....|...
gi 186288308 570 GLGEAVLSAVGEE 582
Cdd:PTZ00182 299 GIGAEIAAQIMED 311
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
10-619 |
6.43e-18 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 87.65 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 10 TLQALKDIANKLR---IHSIRQTcasnSGHPTSCCSAAELmSVLFFHTMrykagdprNPCNDRFILSKGHAA-------- 78
Cdd:PLN02582 47 SVKELKQLADELRsdvIFNVSKT----GGHLGSSLGVVEL-TVALHYVF--------NAPQDKILWDVGHQSyphkiltg 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 79 -----PILYAAWAEAGYIKASDllnlRKIDSDLEGHptpklafvdvATGSLGQGLGAACGMAYTGKyldksSYRVYCMLG 153
Cdd:PLN02582 114 rrdkmHTMRQTNGLSGFTKRAE----SEYDCFGTGH----------SSTTISAGLGMAVGRDLKGK-----KNNVVAVIG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 154 DGECSEGSVWEAMAFASHykLD-NLVAILDVNR------LGQSEPAP-----------LQHNVNVYKERCEAFGFNTYVv 215
Cdd:PLN02582 175 DGAMTAGQAYEAMNNAGY--LDsDMIVILNDNKqvslptATLDGPAPpvgalssalsrLQSSRPLRELREVAKGVTKQI- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 216 dGHDVEELC-KAMWHAEGVkgkptaivaktFKGKGLKGIEDQDNWHGKPMPKDRAEELINdLLSQIQSPNK--PL----- 287
Cdd:PLN02582 252 -GGPMHELAaKVDEYARGM-----------ISGSGSTLFEELGLYYIGPVDGHNIDDLVT-ILREVKSTKTtgPVlihvv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 288 ------YPQPPKEDAPPADLSPIHLLTAPEYKLGDKISTRKAY-GVALKRLGDASTRVVALDGDTKNSTFADMFKKAHPD 360
Cdd:PLN02582 319 tekgrgYPYAERAADKYHGVVKFDPATGKQFKVKAKTQSYTTYfAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 361 RYIECFIAEQNMVSVAIGCATrERTVSFASTFAAFLARAYDQ-IRMAAISQSNVNLVGSHCGVsIGEDGPSQMALEDLAM 439
Cdd:PLN02582 399 RCFDVGIAEQHAVTFAAGLAC-EGLKPFCAIYSSFLQRGYDQvVHDVDLQKLPVRFAMDRAGL-VGADGPTHCGAFDVTY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 440 FRAIPTCTVFYPSDGVSTERSVELAA--NTKGICFIRTSRPDTAVIYNPEEK---FEIGKAKVVRQSskDQVTVIGAGVT 514
Cdd:PLN02582 477 MACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCFRYPRGNGIGVQLPPNNKgipIEVGKGRILLEG--ERVALLGYGTA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 515 LHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARaTGGRVITVEDHyKEGGLGEAV---LSAVGEEPGIVVHRLA 591
Cdd:PLN02582 555 VQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAK-SHEVLITVEEG-SIGGFGSHVaqfMALDGLLDGKLKWRPL 632
|
650 660 670
....*....|....*....|....*....|
gi 186288308 592 V--SRVPRSGKPQELLDMFGISAKCIVAAV 619
Cdd:PLN02582 633 VlpDRYIDHGAPADQLAEAGLTPSHIAATV 662
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
120-245 |
3.82e-17 |
|
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: 82.16 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 120 ATGSLGQGLGAACGMAYTGKYLDKSSYrVYCMLGDGECSEGSVWEAMAFASHYKLDNLVAILDvNRLGQSEPAPLQHNVN 199
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPTSRQTAGT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 186288308 200 VYKERCEAFGFNTYVVDGHDVEELCKAM-WHAEGV--KGKPTAIVAKTF 245
Cdd:cd02000 180 SIADRAAAYGIPGIRVDGNDVLAVYEAAkEAVERAraGGGPTLIEAVTY 228
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
492-572 |
8.36e-15 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 77.26 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 492 IGKAKVVRQSsKDqVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARATgGRVITVEDHYKEGGL 571
Cdd:PRK11892 331 IGKARIHREG-KD-VTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGV 407
|
.
gi 186288308 572 G 572
Cdd:PRK11892 408 G 408
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
120-245 |
4.26e-14 |
|
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: 74.02 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 120 ATGSLGQGLGAACGMAYTGKYLDKSsyRV-YCMLGDGECSEGSVWEAMAFASHYKLDNLVAILDvNRLGQSEPAPLQHNV 198
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRGED--EVaVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAISTPVERQTAV 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 186288308 199 -NVYkERCEAFGFNTYVVDGHDVEELCKAMwhAEGVK-----GKPTAIVAKTF 245
Cdd:COG1071 202 eTIA-DRAAGYGIPGVRVDGNDVLAVYAAV--KEAVEraragEGPTLIEAKTY 251
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
487-582 |
6.02e-14 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 73.22 E-value: 6.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 487 EEKFEIGKAKVVRQSSkdQVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARATgGRVITVEDHY 566
Cdd:PRK09212 187 EESIPIGKAAILREGS--DVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGW 263
|
90
....*....|....*.
gi 186288308 567 KEGGLGEAVLSAVGEE 582
Cdd:PRK09212 264 PFAGVGAEIAALIMKE 279
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
476-582 |
1.20e-13 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 72.54 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 476 SRPDTAVIYNPEEKFEIGKAKVVRQSSkdQVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARAT 555
Cdd:PLN02683 203 SFPVSAEVLDSSFVLPIGKAKIEREGK--DVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT 280
|
90 100
....*....|....*....|....*..
gi 186288308 556 gGRVITVEDHYKEGGLGEAVLSAVGEE 582
Cdd:PLN02683 281 -NRLVTVEEGWPQHGVGAEICASVVEE 306
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
354-617 |
1.24e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 73.98 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 354 FKKAHPDRYIECFIAEQNMVSVAIGCATRERTvSFASTFAAFLARAYDQIRMAAISQSN-VNLVGSHCGVsIGEDGPSQM 432
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 433 ALEDLAMFRAIPTCTVFYPSDGVSTERSVELAA--NTKGICF--IRTSRPDTAVIYNPEEKFEIGKAKVVRQSSkdQVTV 508
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCFrfPRGSIVNMNYLVPTGLPIEIGRGRVLVEGQ--DVAL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 509 IGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDAStIVASARATGGRVITVEDHYKeGGLGEAVLSAV---GEEPGI 585
Cdd:PLN02225 573 LGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIK-LVRDLCQNHKFLITVEEGCV-GGFGSHVAQFIaldGQLDGN 650
|
250 260 270
....*....|....*....|....*....|....*.
gi 186288308 586 VVHRLAVsrVP----RSGKPQELLDMFGISAKCIVA 617
Cdd:PLN02225 651 IKWRPIV--LPdgyiEEASPREQLALAGLTGHHIAA 684
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
121-250 |
1.24e-13 |
|
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: 69.88 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 121 TGSLGQGLGAACGMAYTGKYLDKSsYRVYCMLGDGECSEGSVWEAMAFASHYKlDNLVAILDVNRLGQSEPAPLQHNVnv 200
Cdd:cd02007 74 TGHSSTSISAALGMAVARDLKGKK-RKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSISPNVGTPGNL-- 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 186288308 201 ykerCEAFGFN-TYVVDGHDVEELCKAMWHAEGVKGkPTAIVAKTFKGKGL 250
Cdd:cd02007 150 ----FEELGFRyIGPVDGHNIEALIKVLKEVKDLKG-PVLLHVVTKKGKGY 195
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
352-581 |
5.14e-11 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 64.38 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 352 DMFKKAHPDRYIECFIAEQNMVSVAIGCA-TRERTVSFASTFAaFLARAYDQIrmaaisQSNVNLV----GSHCGVSIGE 426
Cdd:CHL00144 43 GLHEKYGDLRVLDTPIAENSFTGMAIGAAmTGLRPIVEGMNMG-FLLLAFNQI------SNNAGMLhytsGGNFTIPIVI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 427 DGPS----QMALEDL----AMFRAIP-----TCTVFYpsdgvstersvelaaNTKGI--CFIRTSRP----DTAVIYN-- 485
Cdd:CHL00144 116 RGPGgvgrQLGAEHSqrleSYFQSVPglqivACSTPY---------------NAKGLlkSAIRSNNPviffEHVLLYNlk 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 486 ---PEEKF--EIGKAKVVRQSSkdQVTVIGAGVTLHEALAAHDQLAKEGVNIRVIDPFTIKPLDASTIVASARATgGRVI 560
Cdd:CHL00144 181 eeiPDNEYllPLEKAEVVRPGN--DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKT-HKVL 257
|
250 260
....*....|....*....|.
gi 186288308 561 TVEDHYKEGGLGEAVLSAVGE 581
Cdd:CHL00144 258 IVEECMKTGGIGAELIAQINE 278
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
35-186 |
3.05e-10 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 63.24 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 35 GHPTSCCSAAELMSVLFFHTMRYK----AGDprnpcndrFILSKGHAAPILYA-AWAEaGYIKASDLLNLRK-IDSD-LE 107
Cdd:PRK09405 108 GHISSFASSATLYEVGFNHFFRAPnephGGD--------LVFFQGHASPGIYArAFLE-GRLTEEQLDNFRQeVDGKgLS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 108 GHPTPKLA--FVDVATGSLGqgLGAACGM--AYTGKYL------DKSSYRVYCMLGDGECSE----GsvweAMAFASHYK 173
Cdd:PRK09405 179 SYPHPWLMpdFWQFPTVSMG--LGPIMAIyqARFLKYLenrglkDTSDQKVWAFLGDGEMDEpeslG----AISLAAREK 252
|
170
....*....|....*
gi 186288308 174 LDNLVAILDVN--RL 186
Cdd:PRK09405 253 LDNLIFVINCNlqRL 267
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
109-244 |
9.92e-09 |
|
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: 54.95 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 109 HPTPKLAFVDVATGSLGQGLGAACGMAYTGKylDKssyRVYCMLGDGECSEGsvWEAMAFASHYKLDNLVAILD------ 182
Cdd:cd00568 33 LRRGRRFLTSTGFGAMGYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNnggygt 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186288308 183 -----VNRLGQSEPAPLQHNVNvYKERCEAFGFNTYVVDghDVEELCKAMWHAEGVKGkPTAIVAKT 244
Cdd:cd00568 106 irmhqEAFYGGRVSGTDLSNPD-FAALAEAYGAKGVRVE--DPEDLEAALAEALAAGG-PALIEVKT 168
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
35-186 |
1.26e-08 |
|
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: 58.16 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 35 GHPTSCCSAAELMSVLFFHTMRYK----AGDprnpcndrFILSKGHAAPILYA-AWAEaGYIKASDLLNLRKidsDLEGH 109
Cdd:COG2609 109 GHISSFASAATLYEVGFNHFFRGPdhpgGGD--------LVYFQGHASPGIYArAFLE-GRLTEEQLDNFRQ---EVDGK 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 110 -----PTPKLA--FVDVATGSLGqgLGAACGM--AYTGKYL------DKSSYRVYCMLGDGECSE----GsvweAMAFAS 170
Cdd:COG2609 177 glssyPHPWLMpdFWQFPTVSMG--LGPINAIyqARFMKYLhnrglkDTSDRKVWAFLGDGEMDEpeslG----AISLAA 250
|
170
....*....|....*...
gi 186288308 171 HYKLDNLVAILDVN--RL 186
Cdd:COG2609 251 REKLDNLIFVINCNlqRL 268
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
35-186 |
2.25e-08 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 57.25 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 35 GHPTSCCSAAELMSVLFFHTMRykAGDPRNPCNDRFIlsKGHAAPILYA-AWAEaGYIKASDLLNLRK-IDSD-LEGHPT 111
Cdd:PRK13012 116 GHIASYASAADLFEVGFNHFFR--GRDDAGGGDLVYF--QPHSAPGIYArAFLE-GRLSEEQLDHFRQeIGGPgLSSYPH 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 112 PKLA--FVDVATGSLGQGLGAACGMAYTGKYL------DKSSYRVYCMLGDGECSEGSVWEAMAFASHYKLDNLVAILDV 183
Cdd:PRK13012 191 PWLMpdFWQFPTGSMGIGPINAIYQARFMRYLqhrglkDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLVFVINC 270
|
....*
gi 186288308 184 N--RL 186
Cdd:PRK13012 271 NlqRL 275
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
124-281 |
5.90e-04 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 42.55 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 124 LGQGLGAACGMAYTGKYL-----DKSSYRVY-CMLGDGECSEGSVWEAMAFASHYKL-------DNLVAILDVNRLGQSE 190
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRqqvlkEVQPLRVTaCFFGDGTTNNGQFFECLNMAVLWKLpiifvveNNQWAIGMAHHRSTSI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 191 PaplqhnvNVYKeRCEAFGFNTYVVDGHDV----EELCKAMWHAEGVKGkPTAIVAKTFKGKG--------LKGIEDQDN 258
Cdd:CHL00149 210 P-------EIHK-KAEAFGLPGIEVDGMDVlavrEVAKEAVERARQGDG-PTLIEALTYRFRGhsladpdeLRSKQEKEA 280
|
170 180
....*....|....*....|....
gi 186288308 259 WHGK-PMPKDRAEELINDLLSQIQ 281
Cdd:CHL00149 281 WVARdPIKKLKSYIIDNELASQKE 304
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
124-249 |
6.21e-04 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 42.62 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 124 LGQGLGAACGMAYTGKYL-----DKSSYRVYC-MLGDGECSEGSVWEAMAFASHYKL-------DNLVAILDVNRLGQSE 190
Cdd:PLN02374 196 IGEGIPVATGAAFSSKYRrevlkEESCDDVTLaFFGDGTCNNGQFFECLNMAALWKLpivfvveNNLWAIGMSHLRATSD 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186288308 191 PaplqhnvNVYKeRCEAFGFNTYVVDGHD---VEELCK-AMWHAEGVKGkPTAIVAKTFKGKG 249
Cdd:PLN02374 276 P-------EIWK-KGPAFGMPGVHVDGMDvlkVREVAKeAIERARRGEG-PTLVECETYRFRG 329
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
108-246 |
7.47e-04 |
|
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: 41.93 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 108 GHPTPKLAFVDVATGSLGQGLGAACGMAYTGKYLDKSSYrVYCMLGDGECSEGSVWEAMAFASHYKLDnLVAILDVNRLG 187
Cdd:pfam00676 87 GYYGAKGNRFYGGNGILGAQVPLGAGIALAAKYRGKKEV-AITLYGDGAANQGDFFEGLNFAALWKLP-VIFVCENNQYG 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186288308 188 QSEPAPLQHNVNVYKERCEAFGFNTYVVDGHDVE---ELCK-AMWHAEGVKGkPTAIVAKTFK 246
Cdd:pfam00676 165 ISTPAERASASTTYADRARGYGIPGLHVDGMDPLavyQASKfAAERARTGKG-PFLIELVTYR 226
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
345-453 |
1.86e-03 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 39.25 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186288308 345 TKNSTFADmFKKAHPDRYIECFIAEQNMVSVAIGCATRERTVSFASTFAAFLARAYDQIRMAAISQSNVNLVGSHCGVSi 424
Cdd:cd06586 21 DEISSLLD-ALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGLADAAAEHLPVVFLIGARGIS- 98
|
90 100
....*....|....*....|....*....
gi 186288308 425 GEDGPSQMALEDLAMFRAIPTCTVFYPSD 453
Cdd:cd06586 99 AQAKQTFQSMFDLGMYRSIPEANISSPSP 127
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
120-185 |
9.21e-03 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 37.57 E-value: 9.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186288308 120 ATGSLGQGLGAACGMAytgkyLDKSSYRVYCMLGDGecseGSVWEAMAF--ASHYKLDNLVAILDvNR 185
Cdd:cd02002 47 RGGGLGWGLPAAVGAA-----LANPDRKVVAIIGDG----SFMYTIQALwtAARYGLPVTVVILN-NR 104
|
|
| |
