|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-620 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 576.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 88 EAGF-LPEEELL**RKITSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCLLGDG 156
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 157 ELSEGSVWEAMAFASIYKLDNLIAILDINRLGQSDPTPLQHQVDvYQKRCEAFGWHTVIVDGHSVEELCKAFGQAKH--Q 234
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 235 PTAIIAKTFKGRGIPGIEDKDAWHGKPLPknmADQIVQeiynqiqsKKKILVTPPqedalsvsitsirmpsppsykvgdk 314
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLG---AEEIAA--------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 315 iatRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIF------RKEHPDRFIECYIAEQNMVSVAVGCATRNRTVPFCSA 388
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 389 FGAFFTRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAA-NTKGI 467
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 468 CFIRTSRPENAIIYNNNEDFQVKQAKVVLKSKDDqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNlile 547
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 548 saratkgriltvEDHYYEGGIGEAVCCALAGEPGITIS----------RLAVGEVPRSGKPAELLKMFGIDRDAIAQAVR 617
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVADGwykyvgldgkVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 2023515869 618 DLV 620
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-270 |
6.33e-136 |
|
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: 397.26 E-value: 6.33e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEEELL* 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 100 *RKITSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNL 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 179 IAILDINRLGQSDPTPLQHQVDVYQKRCEAFGWHTVIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGIPGIEDKD 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*
gi 2023515869 256 AWHGKPLPKNMADQI 270
Cdd:cd02012 240 KWHGKPLGEEEVELA 254
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
313-620 |
3.32e-118 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 353.62 E-value: 3.32e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 313 DKIATRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIFRKEHPDRFIECYIAEQNMVSVAVGCATRNRtVPFCSAFGAF 392
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 393 FT-RAFDQIRMA-AISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAANTKGICFI 470
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 471 RTSRPENAIIYNNNEDFQVKQAKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESAR 550
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023515869 551 ATkGRILTVEDHYYEGGIGEAVCCALAGEPGITISRLAVGEVP-RSGKPAELLKMFGIDRDAIAQAVRDLV 620
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-619 |
4.44e-79 |
|
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: 263.50 E-value: 4.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPE 94
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 95 EELL**RKITSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCLLGDGELSEGSVW 164
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEGISY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 165 EAMAFASIYKLDNLIAILDINRLGQSDPTPLQHQVDVyQKRCEAFGWHTV-IVDGHSVEELCKAFGQAK---HQPTAIIA 240
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTLIEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 241 KTFKGRGIPGIEDKDAWHGKPLPKNMADQ-------------IVQEIY-------------------NQIQSKKKilvTP 288
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGDEEVALtkknlgwnynpfeIPQEVYdhfkktvkergakaeqewnELFAAYKK---KY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 289 PQEDALSVSITSIRMPSP-----PSYKVGDK-IATRKAYGQALAKLGRAHDRIIALDGDTKNSTFS----DIFRKEHP-D 357
Cdd:TIGR00232 317 PELAAEFTRRLSGELPADwdkqlPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTkwkgSGDLHENPlG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 358 RFIECYIAEQNMVSVAVGCATRNRTVPFCSAFGAFFTRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMF 437
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 438 RSIPTATVFYPSDAVSTEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDFQVKQAKVVLKSKDDQVTVIGAGVTLHEAL 516
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 517 AAADLLKKEKINIRVLDPFTIKPLDRN--LILESARATKGRILTVE----DHYYeggigeavccALAGEPGITISRLAVG 590
Cdd:TIGR00232 557 EAAKKLAAENIKVRVVSMPSFDLFDKQdeEYRESVLPANVTRLAIEagaaDEWY----------KYAGLVGAILGMDSFG 626
|
650 660
....*....|....*....|....*....
gi 2023515869 591 EvprSGKPAELLKMFGIDRDAIAQAVRDL 619
Cdd:TIGR00232 627 E---SAPGDKLFEEFGFTVENVVAKAKKL 652
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
313-476 |
8.05e-51 |
|
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: 173.51 E-value: 8.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 313 DKIATRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIFRKEHPD---RFIECYIAEQNMVSVAVGCATRNR-TVPFCSA 388
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 389 FGAFFTRAFDQIR-MAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAANTKGI 467
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 2023515869 468 --CFIRTSRPE 476
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-474 |
6.54e-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: 120.28 E-value: 6.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 314 KIATRKAYGQALAKLGrahdriialdgdtknstfsdifrkehpdrfIECYIAEQNMVSVAVGCATRNRtVPFCSAFGAFF 393
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 394 TRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAANTKGICFIRTS 473
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 2023515869 474 R 474
Cdd:smart00861 131 R 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-620 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 576.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 88 EAGF-LPEEELL**RKITSDLDGHPVPKQA-FTDVATGSLGQGLGAACGMAYTGKY----FDKAS-----YRVYCLLGDG 156
Cdd:PRK05899 81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTpGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 157 ELSEGSVWEAMAFASIYKLDNLIAILDINRLGQSDPTPLQHQVDvYQKRCEAFGWHTVIVDGHSVEELCKAFGQAKH--Q 234
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAstK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 235 PTAIIAKTFKGRGIPGIEDKDAWHGKPLPknmADQIVQeiynqiqsKKKILVTPPqedalsvsitsirmpsppsykvgdk 314
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLG---AEEIAA--------AKKELGWDY------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 315 iatRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIF------RKEHPDRFIECYIAEQNMVSVAVGCATRNRTVPFCSA 388
Cdd:PRK05899 284 ---RKASGKALNALAKALPELVGGSADLAGSNNTKIKgskdfaPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 389 FGAFFTRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAA-NTKGI 467
Cdd:PRK05899 361 FLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKDGP 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 468 CFIRTSRPENAIIYNNNEDFQVKQAKVVLKSKDDqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNlile 547
Cdd:PRK05899 441 SALVLTRQNLPVLERTAQEEGVAKGGYVLRDDPD-VILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ---- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 548 saratkgriltvEDHYYEGGIGEAVCCALAGEPGITIS----------RLAVGEVPRSGKPAELLKMFGIDRDAIAQAVR 617
Cdd:PRK05899 516 ------------DAAYKESVLPAAVTARVAVEAGVADGwykyvgldgkVLGIDTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 2023515869 618 DLV 620
Cdd:PRK05899 584 ELL 586
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
20-270 |
6.33e-136 |
|
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: 397.26 E-value: 6.33e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 20 NRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEEELL* 99
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 100 *RKITSDLDGHPVPKQ-AFTDVATGSLGQGLGAACGMAYTGKYFdKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNL 178
Cdd:cd02012 81 FRQLGSRLPGHPEYGLtPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 179 IAILDINRLGQSDPTPLQHQVDVYQKRCEAFGWHTVIVDGHSVEELCKAFGQAKH---QPTAIIAKTFKGRGIPGIEDKD 255
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKskgKPTLIIAKTIKGKGVPFMENTA 239
|
250
....*....|....*
gi 2023515869 256 AWHGKPLPKNMADQI 270
Cdd:cd02012 240 KWHGKPLGEEEVELA 254
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
313-620 |
3.32e-118 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 353.62 E-value: 3.32e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 313 DKIATRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIFRKEHPDRFIECYIAEQNMVSVAVGCATRNRtVPFCSAFGAF 392
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 393 FT-RAFDQIRMA-AISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAANTKGICFI 470
Cdd:COG3958 81 LTgRAYEQIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 471 RTSRPENAIIYNNNEDFQVKQAKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESAR 550
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLREGKD--VTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023515869 551 ATkGRILTVEDHYYEGGIGEAVCCALAGEPGITISRLAVGEVP-RSGKPAELLKMFGIDRDAIAQAVRDLV 620
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
8-281 |
1.44e-115 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 345.91 E-value: 1.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 8 DQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWA 87
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 88 EAGFLPEEELL**RKITSDLDGHPVPKQafT---DVATGSLGQGLGAACGMAYTGKYfDKASYRVYCLLGDGELSEGSVW 164
Cdd:COG3959 81 EKGYFPKEELATFRKLGSRLQGHPDMKK--TpgvEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQEGQVW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 165 EAMAFASIYKLDNLIAILDINRLGQSDPT-------PLqhqvdvyQKRCEAFGWHTVIVDGHSVEELCKAFGQAKH---Q 234
Cdd:COG3959 158 EAAMAAAHYKLDNLIAIVDRNGLQIDGPTedvmslePL-------AEKWEAFGWHVIEVDGHDIEALLAALDEAKAvkgK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2023515869 235 PTAIIAKTFKGRGIPGIEDKDAWHGKPLPKNMADQIVQEIYNQIQSK 281
Cdd:COG3959 231 PTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELGDY 277
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
16-619 |
4.44e-79 |
|
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: 263.50 E-value: 4.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPE 94
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 95 EELL**RKITSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMAYTGKY----FDKASYRV-----YCLLGDGELSEGSVW 164
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPeYGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatFNKPGFEIvdhytYVFVGDGCLQEGISY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 165 EAMAFASIYKLDNLIAILDINRLGQSDPTPLQHQVDVyQKRCEAFGWHTV-IVDGHSVEELCKAFGQAK---HQPTAIIA 240
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKastDKPTLIEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 241 KTFKGRGIPGIEDKDAWHGKPLPKNMADQ-------------IVQEIY-------------------NQIQSKKKilvTP 288
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGDEEVALtkknlgwnynpfeIPQEVYdhfkktvkergakaeqewnELFAAYKK---KY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 289 PQEDALSVSITSIRMPSP-----PSYKVGDK-IATRKAYGQALAKLGRAHDRIIALDGDTKNSTFS----DIFRKEHP-D 357
Cdd:TIGR00232 317 PELAAEFTRRLSGELPADwdkqlPEFKVKLQaLATRKYSQNVLNAIANVLPELLGGSADLAPSNLTkwkgSGDLHENPlG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 358 RFIECYIAEQNMVSVAVGCATRNRTVPFCSAFGAFFTRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMF 437
Cdd:TIGR00232 397 NYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 438 RSIPTATVFYPSDAVSTEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDFQVKQAKVVLKSKDDQVTVIGAGVTLHEAL 516
Cdd:TIGR00232 477 RAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 517 AAADLLKKEKINIRVLDPFTIKPLDRN--LILESARATKGRILTVE----DHYYeggigeavccALAGEPGITISRLAVG 590
Cdd:TIGR00232 557 EAAKKLAAENIKVRVVSMPSFDLFDKQdeEYRESVLPANVTRLAIEagaaDEWY----------KYAGLVGAILGMDSFG 626
|
650 660
....*....|....*....|....*....
gi 2023515869 591 EvprSGKPAELLKMFGIDRDAIAQAVRDL 619
Cdd:TIGR00232 627 E---SAPGDKLFEEFGFTVENVVAKAKKL 652
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
19-531 |
5.68e-73 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 247.28 E-value: 5.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 19 ANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPEEEL 97
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 98 L**RKITSDLDGHPvpKQAFT---DVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCLLGDGELSEGSVWE 165
Cdd:PTZ00089 90 KNFRQLGSRTPGHP--ERHITpgvEVTTGPLGQGIANAVGLAiaekhlaakFNRPGHPIFDNYVYVICGDGCLQEGVSQE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 166 AMAFASIYKLDNLIAILDINRLGQSDPTPLQHQVDVyQKRCEAFGWHTVIVD-GHS-VEELCKAFGQAKH---QPTAIIA 240
Cdd:PTZ00089 168 ALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDV-EKKYEAYGWHVIEVDnGNTdFDGLRKAIEEAKKskgKPKLIIV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 241 KTFKGRGiPGIEDKDAWHGKPLPKNMADQI-----------------VQEIYNQIQSKKKILVTP------------PQE 291
Cdd:PTZ00089 247 KTTIGYG-SSKAGTEKVHGAPLGDEDIAQVkelfgldpekkfhvseeVRQFFEQHVEKKKENYEAwkkrfakytaafPKE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 292 DALSVSITSIRMPSP-----PSYKVGDK-IATRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDI-----FRKEHPD-RF 359
Cdd:PTZ00089 326 AQAIERRFKGELPPGwekklPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPkeandFTKASPEgRY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 360 IECYIAEQNMVSVAVGCATRNRTVPFCSAFGAFFTRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRS 439
Cdd:PTZ00089 406 IRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRA 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 440 IPTATVFYPSDAVSTEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDfQVKQAKVVLKSKDD--QVTVIGAGVTLHEAL 516
Cdd:PTZ00089 486 TPNLLVIRPADGTETSGAYALAlANAKTPTILCLSRQNTPPLPGSSIE-GVLKGAYIVVDFTNspQLILVASGSEVSLCV 564
|
570
....*....|....*
gi 2023515869 517 AAADLLKKEkINIRV 531
Cdd:PTZ00089 565 EAAKALSKE-LNVRV 578
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
319-474 |
6.53e-69 |
|
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: 220.39 E-value: 6.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 319 KAYGQALAKLGRAHDRIIALDGDTKNSTFSDIFRKEHPDRFIECYIAEQNMVSVAVGCATRNrTVPFCSAFGAFFTRAFD 398
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023515869 399 QIR-MAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAANTKGICFIRTSR 474
Cdd:cd07033 80 QIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PLN02790 |
PLN02790 |
transketolase |
23-531 |
8.96e-64 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 222.20 E-value: 8.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 23 RISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF--LPEEELL** 100
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 101 RKITSDLDGHPvpkQAFT----DVATGSLGQGLGAACGMAYTGKY----FDKA-----SYRVYCLLGDGELSEGSVWEAM 167
Cdd:PLN02790 82 RQWGSRTPGHP---ENFEtpgiEVTTGPLGQGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISNEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 168 AFASIYKLDNLIAILDINRLGQSDPTPLQHQVDVyQKRCEAFGWHTVIVDG--HSVEELCKAFGQAK---HQPTAIIAKT 242
Cdd:PLN02790 159 SLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDV-DKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKavtDKPTLIKVTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 243 FKGRGIPGIEDKDAWHGKPLPKNMADQI----------------VQEIYNQIQS----------------KKKIlvtpPQ 290
Cdd:PLN02790 238 TIGYGSPNKANSYSVHGAALGEKEVDATrknlgwpyepfhvpedVKSHWSKHTKegaaleaewnakfaeyKKKY----PE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 291 EDALSVSITSIRMPSP-----PSYKVGDKI-ATRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDI-----FRKEHP-DR 358
Cdd:PLN02790 314 EAAELKSLISGELPSGwekalPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPeER 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 359 FIECYIAEQNMVSVAVGCATRNRT-VPFCSAFGAFFTRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMF 437
Cdd:PLN02790 394 NVRFGVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 438 RSIPTATVFYPSDAVSTEKAVELA-ANTKGICFIRTSRPENAIIYNNNEDFQVKQAKVVLKSKDDQ---VTVIGAGVTLH 513
Cdd:PLN02790 474 RAMPNILMLRPADGNETAGAYKVAvTNRKRPTVLALSRQKVPNLPGTSIEGVEKGGYVISDNSSGNkpdLILIGTGSELE 553
|
570
....*....|....*...
gi 2023515869 514 EALAAADLLKKEKINIRV 531
Cdd:PLN02790 554 IAAKAAKELRKEGKKVRV 571
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
16-531 |
1.15e-62 |
|
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: 219.11 E-value: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPE 94
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYdLSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 95 EELL**RKITSDLDGHP-------VpkqaftDVATGSLGQGLGAACGMAYTGKY----FDKASY-----RVYCLLGDGEL 158
Cdd:COG0021 85 DDLKNFRQLGSKTPGHPeyghtpgV------ETTTGPLGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGDGDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 159 SEGSVWEAMAFASIYKLDNLIAILDINRLGQSDPTPLQHQVDVyQKRCEAFGWHTV-IVDGHSVEELCKAFGQAKH---Q 234
Cdd:COG0021 159 MEGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDV-AKRFEAYGWHVIrVEDGHDLEAIDAAIEAAKAetdK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 235 PTAIIAKTFKGRGIPGIEDKDAWHGKPLPknmADQI-------------------VQEIYNQIQSKKKILV--------- 286
Cdd:COG0021 238 PTLIICKTIIGYGSPNKQGTAKAHGAPLG---AEEIaatkealgwppepfevpdeVYAHWRAAGERGAAAEaewnerfaa 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 287 ---TPPQEDALSVSITSIRMP-----SPPSYKVGDK-IATRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDI-----FR 352
Cdd:COG0021 315 yaaAYPELAAELERRLAGELPedwdaALPAFEADAKgVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIkgagsFS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 353 KEHPD-RFIECYIAEQNMVSVAVGCATRNRTVPFCSAFGAF--FTRAfdQIRMAAISESNINFCGSHCGVSIGEDGPSQM 429
Cdd:COG0021 395 PEDPSgRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFsdYMRP--AIRLAALMKLPVIYVFTHDSIGLGEDGPTHQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 430 ALEDLAMFRSIPTATVFYPSDAVSTEKAVELA-ANTKG-ICFI----------RTSRPENAIiynnnedfqVKQAKVVLK 497
Cdd:COG0021 473 PVEQLASLRAIPNLDVIRPADANETAAAWKLAlERKDGpTALIlsrqnlptldRTAAAAEGV---------AKGAYVLAD 543
|
570 580 590
....*....|....*....|....*....|....*..
gi 2023515869 498 SKDD-QVTVIGAG--VTLheALAAADLLKKEKINIRV 531
Cdd:COG0021 544 AEGTpDVILIATGseVSL--AVEAAELLAAEGIKVRV 578
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
216-621 |
3.41e-52 |
|
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: 189.45 E-value: 3.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 216 VDGHSVEELCKAFGQAKHQPTAII--AKTFKGRG-IPGIEDKDAWHGkPLPKNMAdqivqeiyNQIQSKKKilvtppqed 292
Cdd:COG1154 252 IDGHDLDALVETLRNAKDLKGPVLlhVVTKKGKGyAPAEKDPDKFHG-VGPFDPE--------TGEPKKSK--------- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 293 alsvsitsirmPSPPSYkvgdkiaTrKAYGQALAKLGRAHDRIIA-----LDGdtknsTFSDIFRKEHPDRFIECYIAEQ 367
Cdd:COG1154 314 -----------SSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERFPDRFFDVGIAEQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 368 NMVSVAVGCATRNrTVPFCSAFGAFFTRAFDQIRM-AAISESNINFCgshcgvsI------GEDGPSQMALEDLAMFRSI 440
Cdd:COG1154 370 HAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHdVALQNLPVTFA-------IdraglvGADGPTHHGVFDLSYLRCI 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 441 PTATVFYPSDAVSTEKAVELAANTKGICFIRTSR--PENAIIYNNNEDFQVKQAKVVLKSKDdqVTVIGAGVTLHEALAA 518
Cdd:COG1154 442 PNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgnGPGVELPAELEPLPIGKGEVLREGKD--VAILAFGTMVAEALEA 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 519 ADLLKKEKINIRVLDPFTIKPLDRNLILESARATKgRILTVEDHYYEGGIGEAVCCALAGEpGITISRLAVGeVPRS--- 595
Cdd:COG1154 520 AERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEFLADA-GLDVPVLRLG-LPDRfie 596
|
410 420
....*....|....*....|....*..
gi 2023515869 596 -GKPAELLKMFGIDRDAIAQAVRDLVA 621
Cdd:COG1154 597 hGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-620 |
6.19e-52 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 187.98 E-value: 6.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 129 LGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKlDNLIAILDINRLGQSDPtplqhqvdV-----YQ 203
Cdd:PRK05444 123 ISAALGMAKARDLKGGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDNEMSISPN--------VgalsnYL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 204 KRC------EAFGWHTV-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGIPGIE-DKDAWHGkplpknmadqivqe 273
Cdd:PRK05444 194 ARLrsstlfEELGFNYIgPIDGHDLDALIETLKNAKdlKGPVLLHVVTKKGKGYAPAEaDPIKYHG-------------- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 274 iynqiqskkkilvtPPQEDALSVSITSIRMPSPPSYKvgdkiatrKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIFRK 353
Cdd:PRK05444 260 --------------VGKFDPETGEQPKSSKPGKPSYT--------KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSK 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 354 EHPDRFIECYIAEQNMVSVAVGCATRNrTVPFCSAFGAFFTRAFDQIRM-AAISESNINFCGSHCGVSiGEDGPSQMALE 432
Cdd:PRK05444 318 RFPDRYFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHdVALQNLPVTFAIDRAGLV-GADGPTHQGAF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 433 DLAMFRSIPTATVFYPSDAVSTEKAVELA-ANTKGICFIRTSRpENAIIYNNNEDFQVKQAKVVLKSKDDQVTVIGAGVT 511
Cdd:PRK05444 396 DLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPR-GNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTM 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 512 LHEALAAADLLKkekiNIRVLDPFTIKPLDRNLILESARATKgRILTVEDHYYEGGIGEAVCCALAGEpGITISRLAVGe 591
Cdd:PRK05444 475 LAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLEFLADH-GLDVPVLNLG- 547
|
490 500 510
....*....|....*....|....*....|...
gi 2023515869 592 VPRS----GKPAELLKMFGIDRDAIAQAVRDLV 620
Cdd:PRK05444 548 LPDEfidhGSREELLAELGLDAEGIARRILELL 580
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
313-476 |
8.05e-51 |
|
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: 173.51 E-value: 8.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 313 DKIATRKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIFRKEHPD---RFIECYIAEQNMVSVAVGCATRNR-TVPFCSA 388
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 389 FGAFFTRAFDQIR-MAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAANTKGI 467
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGR 160
|
170
....*....|.
gi 2023515869 468 --CFIRTSRPE 476
Cdd:pfam02779 161 kpVVLRLPRQL 171
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
16-262 |
1.00e-45 |
|
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: 164.87 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 16 KDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHNDRFVLSKGHAAPILYAVWAEAGF-LPE 94
Cdd:pfam00456 3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 95 EELL**RKITSDLDGHP-VPKQAFTDVATGSLGQGLGAACGMA---------YTGKYFDKASYRVYCLLGDGELSEGSVW 164
Cdd:pfam00456 83 EDLKSFRQLGSKTPGHPeFGHTAGVEVTTGPLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 165 EAMAFASIYKLDNLIAILDINRLGQSDPTPLQHQVDVyQKRCEAFGWHTV-IVDGHSVEELCKAFGQAK---HQPTAIIA 240
Cdd:pfam00456 163 EASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDT-AARFEAYGWHVIeVEDGHDVEAIAAAIEEAKaekDKPTLIKC 241
|
250 260
....*....|....*....|..
gi 2023515869 241 KTFKGRGIPGIEDKDAWHGKPL 262
Cdd:pfam00456 242 RTVIGYGSPNKQGTHDVHGAPL 263
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
129-622 |
2.23e-37 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 147.56 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 129 LGAACGMAyTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASiYKLDNLIAILDIN----------------RLGQSD- 191
Cdd:PRK12571 125 ISAALGFA-KARALGQPDGDVVAVIGDGSLTAGMAYEALNNAG-AADRRLIVILNDNemsiappvgalaaylsTLRSSDp 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 192 ---------------PTPLQ---HQVDVYQKRC-------EAFGWHTV-IVDGHSVEELCKAFGQAKHQ---PTAIIAKT 242
Cdd:PRK12571 203 farlraiakgveerlPGPLRdgaRRARELVTGMigggtlfEELGFTYVgPIDGHDMEALLSVLRAARARadgPVLVHVVT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 243 FKGRGI-PGIEDKDAWHGkplpknmadqiVQEIYnqiqskkkiLVTPPQEDAlsvsitsirMPSPPSYKvgdkiatrKAY 321
Cdd:PRK12571 283 EKGRGYaPAEADEDKYHA-----------VGKFD---------VVTGLQKKS---------APSAPSYT--------SVF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 322 GQALAKLGRAHDRIIALDGDTKNSTFSDIFRKEHPDRFIECYIAEQNMVSVAVGCATRNrTVPFCSAFGAFFTRAFDQIR 401
Cdd:PRK12571 326 GEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 402 M-AAISESNINFCGSHCGVsIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAV-ELAANTKGICFIRTSRPE--N 477
Cdd:PRK12571 405 HdVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEgvG 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 478 AIIYNNNEDFQVKQAKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLIlesARATKGRI- 556
Cdd:PRK12571 484 VEIPAEGTILGIGKGRVPREGPD--VAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALT---DLLVRHHIv 558
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023515869 557 LTVEDHYYEGGIGEAVCCALAGEpGITISRLAV---GEVPR---SGKPAELLKMFGIDRDAIAQAVRDLVAK 622
Cdd:PRK12571 559 VIVEEQGAMGGFGAHVLHHLADT-GLLDGGLKLrtlGLPDRfidHASREEMYAEAGLTAPDIAAAVTGALAR 629
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
492-612 |
6.87e-36 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 130.79 E-value: 6.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 492 AKVVLKSKDDQVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESARATkGRILTVEDHYYEGGIGEA 571
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2023515869 572 VCCALAGE----PGITISRLAVGEVPRSGKPAELLKMFGIDRDAI 612
Cdd:pfam02780 80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-474 |
6.54e-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: 120.28 E-value: 6.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 314 KIATRKAYGQALAKLGrahdriialdgdtknstfsdifrkehpdrfIECYIAEQNMVSVAVGCATRNRtVPFCSAFGAFF 393
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFF 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 394 TRAFDQIRMAAISESNINFCGSHCGVSIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAANTKGICFIRTS 473
Cdd:smart00861 51 DRAKDQIRSAGASGNVPVVFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLE 130
|
.
gi 2023515869 474 R 474
Cdd:smart00861 131 R 131
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
36-269 |
7.43e-24 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 103.92 E-value: 7.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 36 GHPTSCCSAAEIMAVLFFHTMRYKPQDPRNPHndrfVLSKGHAAPILYAVWAEAGFLPEEELL**RKITSD--LDGHPVP 113
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFRARGEGGGGDL----VYFQGHASPGIYARAFLEGRLTEEQLDNFRQEVGGggLSSYPHP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 114 KQ--AFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLIAILDIN 185
Cdd:cd02017 107 WLmpDFWEFPTVSMGLGPIQAIYQARFNRYLedrglkDTSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 186 RlgQSDPTPLQHQVDVYQkRCEAF----GWHTVIV--------------------------------------------- 216
Cdd:cd02017 187 L--QRLDGPVRGNGKIIQ-ELEGIfrgaGWNVIKViwgskwdellakdgggalrqrmeetvdgdyqtlkakdgayvrehf 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 217 ---------------D---------GHSVEELCKAFGQA---KHQPTAIIAKTFKGRGIPgiedkDAWHGkplpKNMADQ 269
Cdd:cd02017 264 fgkypelkalvtdlsDedlwalnrgGHDPRKVYAAYKKAvehKGKPTVILAKTIKGYGLG-----AAGEG----RNHAHQ 334
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
132-572 |
1.35e-22 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 102.01 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 132 ACGMAyTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKlDNLIAILDINRLGQSDptplqHQVDVYQK------- 204
Cdd:PRK12315 122 ATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAE-----NHGGLYKNlkelrdt 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 205 --RCE-----AFGWHTVIV-DGHSVEELCKAFGQAK--HQPTAIIAKTFKGRGI-PGIEDKDAWH---------GKPLPK 264
Cdd:PRK12315 195 ngQSEnnlfkAMGLDYRYVeDGNDIESLIEAFKEVKdiDHPIVLHIHTLKGKGYqPAEENKEAFHwhmpfdletGQSKVP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 265 NMA----DQIVQEIYNQIQSKKKIlvtppqedalsVSITSirmpsppsykvgdkiATRKAYGqalaklgrahdriialdg 340
Cdd:PRK12315 275 ASGesysSVTLDYLLKKIKEGKPV-----------VAINA---------------AIPGVFG------------------ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 341 dtknstFSDiFRKEHPDRFIECYIAEQNMVSVAVGCAtRNRTVPFCSAFGAFFTRAFDQIRM-AAISESNINFCGShcGV 419
Cdd:PRK12315 311 ------LKE-FRKKYPDQYVDVGIAEQESVAFASGIA-ANGARPVIFVNSTFLQRAYDQLSHdLAINNNPAVMIVF--GG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 420 SIGEDGPSQMALEDLAMFRSIPTATVFYPsdavsTEKAVELA------ANTKGICFIRTsrPENAIIYN--NNEDFQVKQ 491
Cdd:PRK12315 381 SISGNDVTHLGIFDIPMISNIPNLVYLAP-----TTKEELIAmlewalTQHEHPVAIRV--PEHGVESGptVDTDYSTLK 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 492 AKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKE-KINIRVLDPFTIKPLDRNLiLESARATKGRILTVEDHYYEGGIGE 570
Cdd:PRK12315 454 YEVTKAGEK--VAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEEL-LEKLKEDHELVVTLEDGILDGGFGE 530
|
..
gi 2023515869 571 AV 572
Cdd:PRK12315 531 KI 532
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
104-569 |
1.82e-22 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 102.10 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 104 TSDLDGHPVPKQAFTD-VATGSLGQGLGAACGMAyTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASiYKLDNLIAIL 182
Cdd:PLN02234 157 TNGLSGYTKRRESEHDsFGTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAG-YLHSNMIVIL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 183 DINR------LGQSDPTP----LQHQVDVYQKRC-----------EAFGWHTV-IVDGHSVEELCKAFGQAKHQ----PT 236
Cdd:PLN02234 235 NDNKqvslptANLDGPTQpvgaLSCALSRLQSNCgmiretsstlfEELGFHYVgPVDGHNIDDLVSILETLKSTktigPV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 237 AIIAKTFKGRGIPGIED-KDAWHGkplpknmadqivqeiynqiqskkkILVTPPQEDALSVSITSIRmpsppSYKvgdki 315
Cdd:PLN02234 315 LIHVVTEKGRGYPYAERaDDKYHG------------------------VLKFDPETGKQFKNISKTQ-----SYT----- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 316 atrKAYGQALAKLGRAHDRIIALDGDTKNSTFSDIFRKEHPDRFIECYIAEQNMVSVAVGCATRNRTvPFCSAFGAFFTR 395
Cdd:PLN02234 361 ---SCFVEALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 396 AFDQ-IRMAAISESNINFCGSHCGVsIGEDGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAA--NTKGICF--- 469
Cdd:PLN02234 437 AYDQvVHDVDLQKLPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCFryh 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 470 ----IRTSRPENaiiyNNNEDFQVKQAKVVlkSKDDQVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLI 545
Cdd:PLN02234 516 rgngIGVSLPPG----NKGVPLQIGRGRIL--RDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALI 589
|
490 500
....*....|....*....|....
gi 2023515869 546 LESARATKgRILTVEdhyyEGGIG 569
Cdd:PLN02234 590 RSLAKSHE-VLITVE----EGSIG 608
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
12-569 |
2.15e-21 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 98.82 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 12 LQALKDTANRLRISSIQATTAAGsGHPTSCCSAAEIMAVLffHTMRYKPQDprnphndRFVLSKGHAApilyavwaeagf 91
Cdd:PLN02582 48 VKELKQLADELRSDVIFNVSKTG-GHLGSSLGVVELTVAL--HYVFNAPQD-------KILWDVGHQS------------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 92 LPEEELL**R------KITSDLDGHPVPKQAFTD-VATGSLGQGLGAACGMAyTGKYFDKASYRVYCLLGDGELSEGSVW 164
Cdd:PLN02582 106 YPHKILTGRRdkmhtmRQTNGLSGFTKRAESEYDcFGTGHSSTTISAGLGMA-VGRDLKGKKNNVVAVIGDGAMTAGQAY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 165 EAMAFASiYKLDNLIAILDIN-------------------------RLGQSDPT-------------------PLQHQVD 200
Cdd:PLN02582 185 EAMNNAG-YLDSDMIVILNDNkqvslptatldgpappvgalssalsRLQSSRPLrelrevakgvtkqiggpmhELAAKVD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 201 VYQKRC---------EAFGWHTV-IVDGHSVEELCKAFGQAKHQ----PTAIIAKTFKGRGIPGIEDK-DAWHGkplpkn 265
Cdd:PLN02582 264 EYARGMisgsgstlfEELGLYYIgPVDGHNIDDLVTILREVKSTkttgPVLIHVVTEKGRGYPYAERAaDKYHG------ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 266 madqivqeiynqiqskkkilvtppqedalsvsITSIRMPSPPSYKVGDKIATRKAY-GQALAKLGRAHDRIIALDGDTKN 344
Cdd:PLN02582 338 --------------------------------VVKFDPATGKQFKVKAKTQSYTTYfAEALIAEAEVDKDVVAIHAAMGG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 345 STFSDIFRKEHPDRFIECYIAEQNMVSVAVGCATRNRTvPFCSAFGAFFTRAFDQ-IRMAAISESNINFCGSHCGVsIGE 423
Cdd:PLN02582 386 GTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQvVHDVDLQKLPVRFAMDRAGL-VGA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 424 DGPSQMALEDLAMFRSIPTATVFYPSDAVSTEKAVELAA--NTKGICF-------IRTSRPENaiiyNNNEDFQVKQAKV 494
Cdd:PLN02582 464 DGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCFryprgngIGVQLPPN----NKGIPIEVGKGRI 539
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023515869 495 VLKSkdDQVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESARATKgRILTVEdhyyEGGIG 569
Cdd:PLN02582 540 LLEG--ERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVE----EGSIG 607
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
349-573 |
3.26e-18 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 86.57 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 349 DIFRKEHPDRFIECYIAEQNMVSVAVGCATrNRTVPFCS-AFGAFFTRAFDQI-RMAAISE--SNINFcgsHCGVSI-GE 423
Cdd:PTZ00182 74 GLLDKYGPDRVFDTPITEQGFAGFAIGAAM-NGLRPIAEfMFADFIFPAFDQIvNEAAKYRymSGGQF---DCPIVIrGP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 424 DGPS-QMALEDL----AMFRSIPTATVFYPSDAVSTeKAVELAAntkgicfIRTSRP----ENAIIYNN------NEDFQ 488
Cdd:PTZ00182 150 NGAVgHGGAYHSqsfeAYFAHVPGLKVVAPSDPEDA-KGLLKAA-------IRDPNPvvffEPKLLYREsvevvpEADYT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 489 VK--QAKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESARATkGRILTVEDHYYEG 566
Cdd:PTZ00182 222 LPlgKAKVVREGKD--VTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPTC 298
|
....*..
gi 2023515869 567 GIGEAVC 573
Cdd:PTZ00182 299 GIGAEIA 305
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
121-243 |
4.42e-16 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 79.08 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 121 ATGSLGQGLGAACGMAYTGKYFDKASYrVYCLLGDGELSEGSVWEAMAFASIYKLDNLIAILDiNRLGQSDPTPLQHQVD 200
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPTSRQTAGT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2023515869 201 VYQKRCEAFGWHTVIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 243
Cdd:cd02000 180 SIADRAAAYGIPGIRVDGNDVLAVYEAAKEAveraraGGGPTLIEAVTY 228
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
351-572 |
1.21e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 80.53 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 351 FRKEHPDRFIECYIAEQNMVSVAVGCATRNRTvPFCSAFGAFFTRAFDQIRMAAISESN-INFCGSHCGVsIGEDGPSQM 429
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 430 ALEDLAMFRSIPTATVFYPSDAVSTEKAVELAA--NTKGICFirtSRPENAIIYNN-----NEDFQVKQAKVVLKSKDdq 502
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCF---RFPRGSIVNMNylvptGLPIEIGRGRVLVEGQD-- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 503 VTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESARATKgRILTVEDHYYeGGIGEAV 572
Cdd:PLN02225 570 VALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHK-FLITVEEGCV-GGFGSHV 637
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
46-242 |
1.69e-13 |
|
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: 68.82 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 46 EIMAVLFFHTmrykpqdprnPHNDRFVLSKGHAAPILYAVWAeagflpeeell**rkitsdldgHPVPKQAFTDVATGSL 125
Cdd:cd00568 1 RVLAALRAAL----------PEDAIVVNDAGNSAYWAYRYLP----------------------LRRGRRFLTSTGFGAM 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 126 GQGLGAACGMAYTGKyfDKasyRVYCLLGDGELSEGsvWEAMAFASIYKLdNLIAILDIN------RLGQSDPTP----- 194
Cdd:cd00568 49 GYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGL-PVIVVVFNNggygtiRMHQEAFYGgrvsg 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2023515869 195 -LQHQVDvYQKRCEAFGWHTVIVDghSVEELCKAFGQAK--HQPTAIIAKT 242
Cdd:cd00568 121 tDLSNPD-FAALAEAYGAKGVRVE--DPEDLEAALAEALaaGGPALIEVKT 168
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
356-572 |
3.86e-13 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 70.91 E-value: 3.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 356 PDRFIECYIAEQNMVSVAVGCATR--NRTVPFCSaFGaFFTRAFDQIRMAAISESNINfcGSHCGVSIGEDGP----SQM 429
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAglRPIVEFMT-FN-FSMQAIDQIVNSAAKTNYMS--GGQLKCPIVFRGPngaaARV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 430 ALEDLAMFRS----IPTATV---FYPSDAvsteKAVELAAntkgicfIRTSRP----ENAIIY-------NNNEDFQVKQ 491
Cdd:PRK09212 126 AAQHSQCYAAwyshIPGLKVvapYFAADC----KGLLKTA-------IRDPNPviflENEILYghshevpEEEESIPIGK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 492 AKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESARATkGRILTVEDHYYEGGIGEA 571
Cdd:PRK09212 195 AAILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAE 271
|
.
gi 2023515869 572 V 572
Cdd:PRK09212 272 I 272
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
121-243 |
1.30e-12 |
|
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: 69.40 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 121 ATGSLGQGLGAACGMAYTGKYF--DKAsyrVYCLLGDGELSEGSVWEAMAFASIYKLDNLIAILDiNRLGQSdpTPLQHQ 198
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAIS--TPVERQ 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2023515869 199 V---DVYQkRCEAFGWHTVIVDGHSVEELCKAFGQA------KHQPTAIIAKTF 243
Cdd:COG1071 199 TaveTIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEAveraraGEGPTLIEAKTY 251
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
122-247 |
7.90e-11 |
|
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: 61.79 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 122 TGSLGQGLGAACGMAYTGKYFDKaSYRVYCLLGDGELSEGSVWEAMAFASiYKLDNLIAILDINRLGqSDPTplqhqVDV 201
Cdd:cd02007 74 TGHSSTSISAALGMAVARDLKGK-KRKVIAVIGDGALTGGMAFEALNNAG-YLKSNMIVILNDNEMS-ISPN-----VGT 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2023515869 202 YQKRCEAFGWHTV-IVDGHSVEELCKAFGQAK--HQPTAIIAKTFKGRG 247
Cdd:cd02007 146 PGNLFEELGFRYIgPVDGHNIEALIKVLKEVKdlKGPVLLHVVTKKGKG 194
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
461-569 |
1.21e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 64.17 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 461 AANTKGI--CFIRTSRP----ENAIIYNNN------EDFQVK--QAKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKEK 526
Cdd:PRK11892 289 AADAKGLlkAAIRDPNPviflENEILYGQSfdvpklDDFVLPigKARIHREGKD--VTIVSFSIGMTYALKAAEELAKEG 366
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2023515869 527 INIRVLDPFTIKPLDRNLILESARATkGRILTVEDHYYEGGIG 569
Cdd:PRK11892 367 IDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVG 408
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
350-576 |
4.14e-10 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 61.76 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 350 IFRKEHPDRFIECYIAEQNMVSVAVGCATRN-RTVPFCSAFGaFFTRAFDQIRMAAISESNINfcGSHCGVSIGEDGP-- 426
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHIINSAAKTNYMS--AGQISVPIVFRGPng 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 427 ------SQMALEDLAMFRSIPTATVFYPSDAvstEKAVEL--AAntkgicfIRTSRP----ENAIIYNNN---------E 485
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYSS---EDARGLlkAA-------IRDPDPvvflENELLYGESfpvsaevldS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 486 DF--QVKQAKVVLKSKDdqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESARATkGRILTVEDHY 563
Cdd:PLN02683 214 SFvlPIGKAKIEREGKD--VTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|...
gi 2023515869 564 YEGGIGEAVCCAL 576
Cdd:PLN02683 291 PQHGVGAEICASV 303
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
36-187 |
3.90e-06 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 50.14 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 36 GHPTSCCSAAEIMAVLFFHTMRykpqDPRNPHNDRFVLSKGHAAPILYA-VWAEaGFLPEEELL**RKitsDLDGH---- 110
Cdd:PRK09405 108 GHISSFASSATLYEVGFNHFFR----APNEPHGGDLVFFQGHASPGIYArAFLE-GRLTEEQLDNFRQ---EVDGKglss 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 111 -PVPK--QAFTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCLLGDGELSE----GsvweAMAFASIYKL 175
Cdd:PRK09405 180 yPHPWlmPDFWQFPTVSMG--LGPIMAIyqARFLKYLenrglkDTSDQKVWAFLGDGEMDEpeslG----AISLAAREKL 253
|
170
....*....|....
gi 2023515869 176 DNLIAILDIN--RL 187
Cdd:PRK09405 254 DNLIFVINCNlqRL 267
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
36-187 |
4.35e-06 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 49.93 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 36 GHPTSCCSAAEIMAVLFFHTMRYKPQDprnpHNDRFVLSKGHAAPILYAVWAEAGFLPEEELL**RKitsDLDG------ 109
Cdd:PRK13012 116 GHIASYASAADLFEVGFNHFFRGRDDA----GGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQ---EIGGpglssy 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 110 -HPVPKQAFTDVATGSLGQGLGAACGMAYTGKYF------DKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLIAIL 182
Cdd:PRK13012 189 pHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLqhrglkDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLVFVI 268
|
....*..
gi 2023515869 183 DIN--RL 187
Cdd:PRK13012 269 NCNlqRL 275
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
358-569 |
8.88e-06 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 48.20 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 358 RFIECYIAEQNMVSVAVGCA-TRNRTVPFCSAFGaFFTRAFDQI--RMAAISESNinfcGSHCGVSIGEDGPS----QMA 430
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAmTGLRPIVEGMNMG-FLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 431 LEDL----AMFRSIPTATVFypsdAVSTekavelAANTKGI--CFIRTSRP----ENAIIYNNNED-------FQVKQAK 493
Cdd:CHL00144 127 AEHSqrleSYFQSVPGLQIV----ACST------PYNAKGLlkSAIRSNNPviffEHVLLYNLKEEipdneylLPLEKAE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2023515869 494 VVLKSKDdqVTVIGAGVTLHEALAAADLLKKEKINIRVLDPFTIKPLDRNLILESARATKgRILTVEDHYYEGGIG 569
Cdd:CHL00144 197 VVRPGND--ITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIG 269
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
121-244 |
4.63e-05 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 45.78 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 121 ATGSLGQGLGAACGMAYTGKYfDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDnLIAILDINRLGQSDPTPLQHQVD 200
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKY-RGKKEVAITLYGDGAANQGDFFEGLNFAALWKLP-VIFVCENNQYGISTPAERASAST 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2023515869 201 VYQKRCEAFGWHTVIVDGHSVEELCKAFGQAK------HQPTAIIAKTFK 244
Cdd:pfam00676 177 TYADRARGYGIPGLHVDGMDPLAVYQASKFAAerartgKGPFLIELVTYR 226
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
125-306 |
6.65e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 45.63 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 125 LGQGLGAACGMAYTGKYF-----DKASYRVY-CLLGDGELSEGSVWEAMAFASIYKLDnLIAILDINR--LGQSDPTPlQ 196
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRqqvlkEVQPLRVTaCFFGDGTTNNGQFFECLNMAVLWKLP-IIFVVENNQwaIGMAHHRS-T 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 197 HQVDVYqKRCEAFGWHTVIVDGHSVEELCKAFGQA------KHQPTAIIAKTFKGRG--------IPGIEDKDAWHGKPL 262
Cdd:CHL00149 208 SIPEIH-KKAEAFGLPGIEVDGMDVLAVREVAKEAverarqGDGPTLIEALTYRFRGhsladpdeLRSKQEKEAWVARDP 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2023515869 263 PKNMADQIV------QEIYNQIQSKKKILVtppqEDALSVSITSirmPSP 306
Cdd:CHL00149 287 IKKLKSYIIdnelasQKELNKIQREVKIEI----EQAVQFAISS---PEP 329
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
319-451 |
7.17e-05 |
|
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: 43.49 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 319 KAYGQALAKLGRAHdrIIALDGDtKNSTFSDiFRKEHPDRFIECYIAEQNMVSVAVGCATRNRTVPFCSAFGAFFTRAFD 398
Cdd:cd06586 1 AAFAEVLTAWGVRH--VFGYPGD-EISSLLD-ALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAIN 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2023515869 399 QIRMAAISESNINFCGSHCGVSiGEDGPSQMALEDLAMFRSIPTATVFYPSDA 451
Cdd:cd06586 77 GLADAAAEHLPVVFLIGARGIS-AQAKQTFQSMFDLGMYRSIPEANISSPSPA 128
|
|
| AceE |
COG2609 |
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ... |
36-187 |
1.30e-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: 45.07 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 36 GHPTSCCSAAEIMAVLFFHTMRykpqDPRNPHNDRFVLSKGHAAPILYAvwaEA---GFLPEEELL**RKitsDLDGH-- 110
Cdd:COG2609 109 GHISSFASAATLYEVGFNHFFR----GPDHPGGGDLVYFQGHASPGIYA---RAfleGRLTEEQLDNFRQ---EVDGKgl 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 111 ---PVPKQA--FTDVATGSLGqgLGAACGM--AYTGKYF------DKASYRVYCLLGDGELSE----GsvweAMAFASIY 173
Cdd:COG2609 179 ssyPHPWLMpdFWQFPTVSMG--LGPINAIyqARFMKYLhnrglkDTSDRKVWAFLGDGEMDEpeslG----AISLAARE 252
|
170
....*....|....*.
gi 2023515869 174 KLDNLIAILDIN--RL 187
Cdd:COG2609 253 KLDNLIFVINCNlqRL 268
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
125-247 |
3.20e-04 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 43.39 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 125 LGQGLGAACGMAYTGKYFDKASYRVYC------LLGDGELSEGSVWEAMAFASIYKL-------DNLIAILDINRLGQSD 191
Cdd:PLN02374 196 IGEGIPVATGAAFSSKYRREVLKEESCddvtlaFFGDGTCNNGQFFECLNMAALWKLpivfvveNNLWAIGMSHLRATSD 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023515869 192 PtplqhqvDVYqKRCEAFGWHTVIVDGH---SVEELCK-AFGQAKH--QPTAIIAKTFKGRG 247
Cdd:PLN02374 276 P-------EIW-KKGPAFGMPGVHVDGMdvlKVREVAKeAIERARRgeGPTLVECETYRFRG 329
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
113-231 |
7.41e-03 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 39.37 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023515869 113 PKQAFTDVATGSLGQGLGAACG--MAYTGKyfdkasyRVYCLLGDG-------ELsegsvweamAFASIYKLDNLIAILD 183
Cdd:COG0028 402 PRRFLTSGGLGTMGYGLPAAIGakLARPDR-------PVVAITGDGgfqmnlqEL---------ATAVRYGLPVKVVVLN 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023515869 184 INRLGqsdpTPLQHQVDVYQKR--------------CEAFGWHTVIVDghSVEELCKAFGQA 231
Cdd:COG0028 466 NGGLG----MVRQWQELFYGGRysgtdlpnpdfaklAEAFGAKGERVE--TPEELEAALEEA 521
|
|
| |
