|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
17-588 |
1.72e-132 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 399.51 E-value: 1.72e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 17 DRGTLQVLQDMASRLRIHSIRATCST------SSGSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------ 78
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKAnsghpgMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 79 ----------------------------RLSFVDVATGWLGQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDG 121
Cdd:PRK05899 81 lagydlsiddlknfrqlgsktpghpeygHTPGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 122 ESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPaEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKh 201
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTE-GWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 202 KPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIesqiqtsrNLDPqppiedspevnitdvrmtsppdyrvgd 281
Cdd:PRK05899 239 KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL--------GWDY--------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 282 kiatRKACGLALAKLGYANNRVVVLDGD------TRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFAS 355
Cdd:PRK05899 284 ----RKASGKALNALAKALPELVGGSADlagsnnTKIKGSKDFAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 356 TFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAK-G 434
Cdd:PRK05899 360 TFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 435 MCFIRTTRPETMVIY-TPQERFEIGQAKVLRHCvsDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVAti 513
Cdd:PRK05899 440 PSALVLTRQNLPVLErTAQEEGVAKGGYVLRDD--PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ-- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 514 vssakategriitvEDHYPQGGIGEAVCAAVSMDPDI----------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVA 583
Cdd:PRK05899 516 --------------DAAYKESVLPAAVTARVAVEAGVadgwykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAA 581
|
....*
gi 225637461 584 VKCML 588
Cdd:PRK05899 582 AKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
281-585 |
1.66e-110 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 332.82 E-value: 1.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 281 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 360
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 361 LT-RAFDHIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFI 438
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 439 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAK 518
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225637461 519 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 585
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
30-239 |
1.38e-77 |
|
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: 246.26 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 30 RLRIHSIRATCST------SSGSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------- 78
Cdd:cd02012 2 RIRRLSIDMVQKAgsghpgGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 79 -----RL---------SFVDVATGWLGQGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLV 144
Cdd:cd02012 82 rqlgsRLpghpeygltPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 145 AIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAES 224
Cdd:cd02012 161 AIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAK 240
|
250
....*....|....*
gi 225637461 225 WHAKPMPRERADAII 239
Cdd:cd02012 241 WHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
281-447 |
2.39e-46 |
|
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: 160.79 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 281 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 356
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 357 FAAFLTRAFDHIRIG-GLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAV--ALAANAK 433
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAIRRDGR 160
|
170
....*....|....
gi 225637461 434 GMCFIRTTRPETMV 447
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-442 |
2.19e-28 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 110.27 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 314 TFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDG 393
Cdd:smart00861 4 ATRKAFGEALAELAIDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 225637461 394 ASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR 442
Cdd:smart00861 83 PTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
17-588 |
1.72e-132 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 399.51 E-value: 1.72e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 17 DRGTLQVLQDMASRLRIHSIRATCST------SSGSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------ 78
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKAnsghpgMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAghgsmllysllh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 79 ----------------------------RLSFVDVATGWLGQGLGVACGMAYTGKY----FDRAS-----YRVFCLMSDG 121
Cdd:PRK05899 81 lagydlsiddlknfrqlgsktpghpeygHTPGVETTTGPLGQGLANAVGMALAEKYlaalFNRPGldivdHYTYVLCGDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 122 ESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPaEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKh 201
Cdd:PRK05899 161 DLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTE-GWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKAST- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 202 KPTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIesqiqtsrNLDPqppiedspevnitdvrmtsppdyrvgd 281
Cdd:PRK05899 239 KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL--------GWDY--------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 282 kiatRKACGLALAKLGYANNRVVVLDGD------TRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFAS 355
Cdd:PRK05899 284 ----RKASGKALNALAKALPELVGGSADlagsnnTKIKGSKDFAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 356 TFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAK-G 434
Cdd:PRK05899 360 TFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 435 MCFIRTTRPETMVIY-TPQERFEIGQAKVLRHCvsDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVAti 513
Cdd:PRK05899 440 PSALVLTRQNLPVLErTAQEEGVAKGGYVLRDD--PDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ-- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 514 vssakategriitvEDHYPQGGIGEAVCAAVSMDPDI----------QVHSLAVSGVPQSGKSEELLDMYGISARHIIVA 583
Cdd:PRK05899 516 --------------DAAYKESVLPAAVTARVAVEAGVadgwykyvglDGKVLGIDTFGASAPADELFKEFGFTVENIVAA 581
|
....*
gi 225637461 584 VKCML 588
Cdd:PRK05899 582 AKELL 586
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
281-585 |
1.66e-110 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 332.82 E-value: 1.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 281 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAF 360
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGK-IPFVSTFAPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 361 LT-RAFDHIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFI 438
Cdd:COG3958 81 LTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 439 RTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAK 518
Cdd:COG3958 161 RLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAAR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225637461 519 ATeGRIITVEDHYPQGGIGEAVCAAVSMDPDIQVHSLAVSGVP-QSGKSEELLDMYGISARHIIVAVK 585
Cdd:COG3958 239 KT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFgESGSPEELLEKYGLDAEGIVAAAK 305
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
30-239 |
1.38e-77 |
|
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: 246.26 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 30 RLRIHSIRATCST------SSGSSSEIMSVLFFYIMRYKQSDPENPDNDRFVLAK------------------------- 78
Cdd:cd02012 2 RIRRLSIDMVQKAgsghpgGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKghaspalyavlalagylpeedlktf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 79 -----RL---------SFVDVATGWLGQGLGVACGMAYTGKYFdRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLV 144
Cdd:cd02012 82 rqlgsRLpghpeygltPGVEVTTGSLGQGLSVAVGMALAEKLL-GFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 145 AIFDVNRLGHSGALPAEHCINIYQRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAES 224
Cdd:cd02012 161 AIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTAK 240
|
250
....*....|....*
gi 225637461 225 WHAKPMPRERADAII 239
Cdd:cd02012 241 WHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
17-247 |
2.25e-62 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 206.85 E-value: 2.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 17 DRGTLQVLQDMASRLRIHSIRAT-------------CStssgsssEIMSVLFFYIMRYKQSDPENPDNDRFVLAK----- 78
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIyaagsghpggslsAA-------DILAALYFKVMNIDPKNPDWPDRDRFILSKghaap 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 79 -------RLSF---------------------------VDVATGWLGQGLGVACGMAYTGKYfDRASYRVFCLMSDGESS 124
Cdd:COG3959 74 alyavlaEKGYfpkeelatfrklgsrlqghpdmkktpgVEMSTGSLGQGLSVAVGMALAAKL-DGKDYRVYVLLGDGELQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 125 EGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGalPAEHCINIY--QRRCEAFGWNTYVVDGRDVEALCQVFWQASQVKHK 202
Cdd:COG3959 153 EGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDG--PTEDVMSLEplAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 225637461 203 PTAVVAKTFKGRGTPSIEDAESWHAKPMPRERADAIIKLIESQIQ 247
Cdd:COG3959 231 PTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELEAELG 275
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
287-442 |
3.32e-59 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 194.20 E-value: 3.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 287 KACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFD 366
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225637461 367 HIRI-GGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR 442
Cdd:cd07033 80 QIRHdVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
281-447 |
2.39e-46 |
|
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: 160.79 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 281 DKIATRKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPE---RFIECFMAEQNMVSVALGCASRGR-TIAFAST 356
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 357 FAAFLTRAFDHIRIG-GLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAV--ALAANAK 433
Cdd:pfam02779 81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAIRRDGR 160
|
170
....*....|....
gi 225637461 434 GMCFIRTTRPETMV 447
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
172-588 |
2.83e-42 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 160.25 E-value: 2.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 172 EAFGWNtYV--VDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWHAkpmpreradaiikliesqiqt 248
Cdd:PRK05444 203 EELGFN-YIgpIDGHDLDALIETLKNAKDLKG-PVLLHVVTKKGKGyAPAEADPIKYHG--------------------- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 249 srnldpqppiedspevnitdvrmTSPPDYRVGDKIATRKAC--------GLALAKLGYANNRVVVLDGDTRYSTFSEIFN 320
Cdd:PRK05444 260 -----------------------VGKFDPETGEQPKSSKPGkpsytkvfGETLCELAEKDPKIVAITAAMPEGTGLVKFS 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 321 KEYPERFIECFMAEQNMVSVALGCASRGrTIAFASTFAAFLTRAFDHI----------------RiGGLaesniniigsh 384
Cdd:PRK05444 317 KRFPDRYFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVihdvalqnlpvtfaidR-AGL----------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 385 cgvsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANA-KGMCFIRTTRPE-TMVIYTPQERFEIGQAKV 462
Cdd:PRK05444 384 ----VGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYdDGPIAIRYPRGNgVGVELPELEPLPIGKGEV 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 463 LRHcvSDKVTVIGAGITVYEALAAADELSKqdifIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCA 542
Cdd:PRK05444 460 LRE--GEDVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAKHD-LVVTVEEGAIMGGFGSAVLE 532
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 225637461 543 AVS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 588
Cdd:PRK05444 533 FLAdHGLDVPVLNL---GLPDEfidhGSREELLAELGLDAEGIARRILELL 580
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
172-588 |
9.01e-42 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 159.41 E-value: 9.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 172 EAFGWNtYV--VDGRDVEALCQVFWQASQVKhKPTAVVAKTFKGRG-TPSIEDAESWHAkpmpreradaiikliesqiqt 248
Cdd:COG1154 242 EELGFK-YIgpIDGHDLDALVETLRNAKDLK-GPVLLHVVTKKGKGyAPAEKDPDKFHG--------------------- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 249 srnldpQPPIEdsPEVNITDVRMTSPPDYrvgdkiaTrKACGLALAKLGYANNRVVV-----LDGdtrysTFSEIFNKEY 323
Cdd:COG1154 299 ------VGPFD--PETGEPKKSKSSAPSY-------T-DVFGDTLVELAEKDPRIVAitaamPEG-----TGLDKFAERF 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 324 PERFIECFMAEQNMVSVALGCASRGRTIAFA--STFaafLTRAFDHI----------------RiGGLaesniniigshc 385
Cdd:COG1154 358 PDRFFDVGIAEQHAVTFAAGLATEGLKPVVAiySTF---LQRAYDQVihdvalqnlpvtfaidR-AGL------------ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 386 gvsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR-PETMV-IYTPQERFEIGQAKVL 463
Cdd:COG1154 422 ---VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRgNGPGVeLPAELEPLPIGKGEVL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 464 RHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCAA 543
Cdd:COG1154 499 RE--GKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHD-LVVTVEEGVLAGGFGSAVLEF 575
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 225637461 544 VS-MDPDIQVHSLavsGVPQS----GKSEELLDMYGISARHIIVAVKCML 588
Cdd:COG1154 576 LAdAGLDVPVLRL---GLPDRfiehGSRAELLAELGLDAEGIARAILELL 622
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
458-580 |
1.04e-35 |
|
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.
Pssm-ID: 460693 [Multi-domain] Cd Length: 124 Bit Score: 130.02 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 458 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIG 537
Cdd:pfam02780 1 GKAEILRE--GDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKT-GRLVTVEEAVPRGGFG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 225637461 538 EAVCAAVS----MDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHI 580
Cdd:pfam02780 78 SEVAAALAeeafDGLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
49-588 |
1.60e-34 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 138.65 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 49 EIMSVLFFYIMRYKQSDPENPDNDRFVL----AKRLSF------------------------------------VDVATG 88
Cdd:PTZ00089 37 PIAHILWSEVMKYNPKDPRWINRDRFVLsnghASALLYsmlhltgydlsmedlknfrqlgsrtpghperhitpgVEVTTG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 89 WLGQGLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALP 159
Cdd:PTZ00089 117 PLGQGIANAVGLAIAEKHlaakFNRPGHpifdnYVYVICGDGCLQEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 160 AEHCINIyQRRCEAFGWNTYVVD--GRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTpSIEDAESWHAKPMPRERADA 237
Cdd:PTZ00089 197 LSFTEDV-EKKYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLIIVKTTIGYGS-SKAGTEKVHGAPLGDEDIAQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 238 IIKLIesqiqtsrNLDPQPPIEDSPEV--------------------NITDVRMTSP----------------------P 275
Cdd:PTZ00089 275 VKELF--------GLDPEKKFHVSEEVrqffeqhvekkkenyeawkkRFAKYTAAFPkeaqaierrfkgelppgwekklP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 276 DYRVGDK-IATRKACGLALAKLGYANNRVVVLDGD------TRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRG 348
Cdd:PTZ00089 347 KYTTNDKaIATRKASENVLNPLFQILPELIGGSADltpsnlTRPKEANDFTKASPEGRYIRFGVREHAMCAIMNGIAAHG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 349 RTIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVAL 428
Cdd:PTZ00089 427 GFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYAL 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 429 A-ANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHC-VSDKVTVIGAGITVYEALAAADELSKqDIFIRVI-----D 501
Cdd:PTZ00089 507 AlANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFtNSPQLILVASGSEVSLCVEAAKALSK-ELNVRVVsmpcwE 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 502 LFTIKPLDVATIVssakategriitvedhYPQGGIGE-AVCAAVSMDPDIQVH-SLAVSGVPQSGKSEELLDMYGISARH 579
Cdd:PTZ00089 586 LFDQQSEEYQQSV----------------LPSGGVPVlSVEAYVSFGWEKYSHvHVGISGFGASAPANALYKHFGFTVEN 649
|
....*....
gi 225637461 580 IIVAVKCML 588
Cdd:PTZ00089 650 VVEKARALA 658
|
|
| PLN02790 |
PLN02790 |
transketolase |
49-502 |
2.37e-29 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 123.21 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 49 EIMSVLFFYIMRYKQSDPENPDNDRFVLA-------------------------KRL------------SF----VDVAT 87
Cdd:PLN02790 25 PMGHVLYDEVMKYNPKNPYWFNRDRFVLSaghgcmlqyallhlagydsvqmedlKQFrqwgsrtpghpeNFetpgIEVTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 88 GWLGQGLGVACGMAYTGKY----FDRA-----SYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRL---GHS 155
Cdd:PLN02790 105 GPLGQGIANAVGLALAEKHlaarFNKPdhkivDHYTYCILGDGCQMEGISNEAASLAGHWGLGKLIVLYDDNHIsidGDT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 156 GALPAEHCIniyqRRCEAFGWNTYVVDG--RDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRE 233
Cdd:PLN02790 185 EIAFTEDVD----KRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIGYGSPNKANSYSVHGAALGEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 234 RADAiikliesqiqTSRNLD-PQPPIEDSPEVN--------------------------------------ITDVRMT-- 272
Cdd:PLN02790 261 EVDA----------TRKNLGwPYEPFHVPEDVKshwskhtkegaaleaewnakfaeykkkypeeaaelkslISGELPSgw 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 273 --SPPDYRVGDKI-ATRK---ACGLALAKL------GYAN----NRVVVLD-GDtrystfseiFNKEYP-ERFIECFMAE 334
Cdd:PLN02790 331 ekALPTFTPEDPAdATRNlsqKCLNALAKVlpgligGSADlassNMTLLKDfGD---------FQKDTPeERNVRFGVRE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 335 QNMVSVALGCASRGRT-IAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTI 413
Cdd:PLN02790 402 HGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNILM 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 414 FYPTDAVSTEHAVALA-ANAKG---MCFIRTTRPETMViyTPQERFEIGQAKVLRHCVSDK--VTVIGAGITVYEALAAA 487
Cdd:PLN02790 482 LRPADGNETAGAYKVAvTNRKRptvLALSRQKVPNLPG--TSIEGVEKGGYVISDNSSGNKpdLILIGTGSELEIAAKAA 559
|
570
....*....|....*
gi 225637461 488 DELSKQDIFIRVIDL 502
Cdd:PLN02790 560 KELRKEGKKVRVVSM 574
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
314-442 |
2.19e-28 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 110.27 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 314 TFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRtIAFASTFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDG 393
Cdd:smart00861 4 ATRKAFGEALAELAIDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGNVPVVFRHDGGGGVGEDG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 225637461 394 ASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAANAKGMCFIRTTR 442
Cdd:smart00861 83 PTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
333-545 |
1.79e-25 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 107.41 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 333 AEQNMVSVALGCASRG-RTIAFAsTFAAFLTRAFDHI---------RIGGLAESNInIIGSHCGVSVGDdGA--SQMaLE 400
Cdd:COG0022 59 SEAGIVGAAIGAALAGlRPVVEI-QFADFIYPAFDQIvnqaaklryMSGGQFKVPM-VIRTPYGGGIGA-GAqhSQS-LE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 401 diAMFRTIPKCTIFYPtdavSTehavalAANAKGM---CfIRTTRP----ETMVIYT-----PQERFE--IGQAKVLRHc 466
Cdd:COG0022 135 --AWFAHIPGLKVVAP----ST------PYDAKGLlkaA-IRDDDPviflEHKRLYRlkgevPEEDYTvpLGKARVVRE- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225637461 467 vSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVCAAVS 545
Cdd:COG0022 201 -GTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEIAARIA 277
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
178-588 |
3.99e-25 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 110.20 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 178 TYV--VDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAEswhakpmprERADAIIKLiesQIQTSRNLDPQ 255
Cdd:PRK12571 248 TYVgpIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEADE---------DKYHAVGKF---DVVTGLQKKSA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 256 PpiedspevnitdvrmtSPPDYRvgdkiatrKACGLALAKLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQ 335
Cdd:PRK12571 316 P----------------SAPSYT--------SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 336 NMVSVALGCASRGrTIAFASTFAAFLTRAFDHIRIG-GLAESNINIIGSHCGVsVGDDGASQMALEDIAMFRTIPKCTIF 414
Cdd:PRK12571 372 HAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLHDvALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVM 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 415 YPTDAVSTEHAVALA-ANAKGMCFIRTTRPETMVIYTPqERFEIGQAKVLRHCVSDK-VTVIGAGITVYEALAAADELSK 492
Cdd:PRK12571 450 APRDEAELRHMLRTAaAHDDGPIAVRFPRGEGVGVEIP-AEGTILGIGKGRVPREGPdVAILSVGAHLHECLDAADLLEA 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 493 QDIFIRVIDLFTIKPLDVATIvssAKATEGRI-ITVEDHYPQGGIGEAVCAAVS----MDPDIQVHSLavsGVP----QS 563
Cdd:PRK12571 529 EGISVTVADPRFVKPLDEALT---DLLVRHHIvVIVEEQGAMGGFGAHVLHHLAdtglLDGGLKLRTL---GLPdrfiDH 602
|
410 420
....*....|....*....|....*
gi 225637461 564 GKSEELLDMYGISARHIIVAVKCML 588
Cdd:PRK12571 603 ASREEMYAEAGLTAPDIAAAVTGAL 627
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
49-503 |
4.39e-22 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 100.47 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 49 EIMSVLFFYIMRYkqsDPENP---DNDRFVLA------------------------KRL----------------SFVDV 85
Cdd:COG0021 35 PIAYVLWTKFLKH---NPANPkwpNRDRFVLSaghgsmllysllhltgydlslddlKNFrqlgsktpghpeyghtPGVET 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 86 ATGWLGQGLGVACGMAYTGKY----FDRASY-----RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRlghsg 156
Cdd:COG0021 112 TTGPLGQGIANAVGMAIAERHlaarFNRPGHdivdhYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNG----- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 157 alpaehcINI-----------YQRRCEAFGWNTY-VVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAES 224
Cdd:COG0021 187 -------ISIdgdtdlafsedVAKRFEAYGWHVIrVEDGHDLEAIDAAIEAAKAETDKPTLIICKTIIGYGSPNKQGTAK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 225 WHAKPMPrerADAIIKLIEsqiqtsrNLD-PQPPIEDSPEV-NITD-------------------------------VRM 271
Cdd:COG0021 260 AHGAPLG---AEEIAATKE-------ALGwPPEPFEVPDEVyAHWRaagergaaaeaewnerfaayaaaypelaaelERR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 272 TSP----------PDYRVGDK-IATRKACGLALAKLGYANNRVVV----LDGdtrySTFSEI-----FNKEYPE-RFIEC 330
Cdd:COG0021 330 LAGelpedwdaalPAFEADAKgVATRKASGKVLNALAPVLPELIGgsadLAG----SNKTTIkgagsFSPEDPSgRNIHF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 331 FMAEQNMVSVALGCASRGRTIAFASTFAAFltraFDH----IRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFR 406
Cdd:COG0021 406 GVREHAMGAIMNGIALHGGLRPYGGTFLVF----SDYmrpaIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASLR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 407 TIPKCTIFYPTDAVSTEHAVALAANakgmcfiRTTRPeTMVIYT----PQERFEIGQAK-------VLRHCVSD-KVTVI 474
Cdd:COG0021 482 AIPNLDVIRPADANETAAAWKLALE-------RKDGP-TALILSrqnlPTLDRTAAAAEgvakgayVLADAEGTpDVILI 553
|
570 580 590
....*....|....*....|....*....|....
gi 225637461 475 GAGITVYEALAAADELSKQDIFIRVI-----DLF 503
Cdd:COG0021 554 ATGSEVSLAVEAAELLAAEGIKVRVVsmpswELF 587
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
324-544 |
1.63e-21 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 96.20 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 324 PERFIECFMAEQNMVSVALGCASRG-RTIAfASTFAAFLTRAFDHI---------RIGGLAESNInIIGSHCGVsVGDDG 393
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNGlRPIA-EFMFADFIFPAFDQIvneaakyryMSGGQFDCPI-VIRGPNGA-VGHGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 394 A--SQmALEdiAMFRTIPKCTIFYPTDAVstehavalaaNAKGMCF--IRTTRP----ETMVIY------TPQERFE--I 457
Cdd:PTZ00182 158 AyhSQ-SFE--AYFAHVPGLKVVAPSDPE----------DAKGLLKaaIRDPNPvvffEPKLLYresvevVPEADYTlpL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 458 GQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIG 537
Cdd:PTZ00182 225 GKAKVVRE--GKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPTCGIG 301
|
....*..
gi 225637461 538 EAVCAAV 544
Cdd:PTZ00182 302 AEIAAQI 308
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
49-264 |
2.19e-19 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 89.75 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 49 EIMSVLFFYIMRYKQSDPENPDNDRFVL----------------------AKRLSF------------------VDVATG 88
Cdd:pfam00456 33 PIAEVLFKRFLKHNPNDPKWINRDRFVLsnghgsmllysllhltgydlsmEDLKSFrqlgsktpghpefghtagVEVTTG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 89 WLGQGLGVACGMA---------YTGKYFDRASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALP 159
Cdd:pfam00456 113 PLGQGIANAVGMAiaernlaatYNRPGFDIVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFYDDNQISIDGETK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 160 AEHCINIyQRRCEAFGWNT-YVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMpreRADAI 238
Cdd:pfam00456 193 ISFTEDT-AARFEAYGWHViEVEDGHDVEAIAAAIEEAKAEKDKPTLIKCRTVIGYGSPNKQGTHDVHGAPL---GADEV 268
|
250 260
....*....|....*....|....*.
gi 225637461 239 iklieSQIQTSRNLDPQPPIEDSPEV 264
Cdd:pfam00456 269 -----AALKQKLGWDPYKPFEIPAEV 289
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
90-547 |
4.44e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 90.93 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 90 LGQGLGVACGMAYTGkyfdrASYRVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFD--------VNRLGHSGALPAE 161
Cdd:PLN02234 183 LSAGLGMAVGRDLKG-----MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDnkqvslptANLDGPTQPVGAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 162 HC-INIYQRRC-----------EAFGWNtYV--VDGRDVEALCQVFWQASQVKH-KPTAVVAKTFKGRGTPSIEDAEswh 226
Cdd:PLN02234 258 SCaLSRLQSNCgmiretsstlfEELGFH-YVgpVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERAD--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 227 akpmprERADAIIKLiesqiqtsrnlDPQppiedspevnitdvrmtSPPDYRVGDKIATRKACGL-ALAKLGYANNRVVV 305
Cdd:PLN02234 334 ------DKYHGVLKF-----------DPE-----------------TGKQFKNISKTQSYTSCFVeALIAEAEADKDIVA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 306 LDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDHI-RIGGLAESNINIIGSH 384
Cdd:PLN02234 380 IHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQVvHDVDLQKLPVRFAIDR 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 385 CGVsVGDDGASQMALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMCFiRTTRPETMVIYTPQER----FEIG 458
Cdd:PLN02234 459 AGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSLPPGNkgvpLQIG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 459 QAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHyPQGGIGE 538
Cdd:PLN02234 537 RGRILRD--GERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHE-VLITVEEG-SIGGFGS 612
|
....*....
gi 225637461 539 AVCAAVSMD 547
Cdd:PLN02234 613 HVVQFLALD 621
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
429-544 |
1.55e-18 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 88.44 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 429 AANAKGM--CFIRTTRPetmVIYTPQE-----RFE----------IGQAKVLRhcVSDKVTVIGAGITVYEALAAADELS 491
Cdd:PRK11892 289 AADAKGLlkAAIRDPNP---VIFLENEilygqSFDvpklddfvlpIGKARIHR--EGKDVTIVSFSIGMTYALKAAEELA 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 225637461 492 KQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVCAAV 544
Cdd:PRK11892 364 KEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVGAEIAARV 415
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
324-544 |
1.14e-16 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 81.31 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 324 PERFIECFMAEQNMVSVALGCASRG-RTIAFASTFAaFLTRAFDHIrIGGLAESNInIIGSHCGVSV---GDDGA----- 394
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAGlRPIVEFMTFN-FSMQAIDQI-VNSAAKTNY-MSGGQLKCPIvfrGPNGAaarva 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 395 SQMALEDIAMFRTIPKCTIFYPtdavstehavALAANAKGM--CFIRTTRP----ETMVIY-----TPQERF--EIGQAK 461
Cdd:PRK09212 127 AQHSQCYAAWYSHIPGLKVVAP----------YFAADCKGLlkTAIRDPNPviflENEILYghsheVPEEEEsiPIGKAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 462 VLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHYPQGGIGEAVC 541
Cdd:PRK09212 197 ILRE--GSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGVGAEIA 273
|
...
gi 225637461 542 AAV 544
Cdd:PRK09212 274 ALI 276
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
318-547 |
4.87e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 81.49 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 318 IFNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDHIRIG-GLAESNINIIGSHCGVsVGDDGASQ 396
Cdd:PLN02582 391 LFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQVVHDvDLQKLPVRFAMDRAGL-VGADGPTH 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 397 MALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMCFiRTTRPETMVIYTPQER----FEIGQAKVLRHcvSDK 470
Cdd:PLN02582 469 CGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNNkgipIEVGKGRILLE--GER 545
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225637461 471 VTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHyPQGGIGEAVCAAVSMD 547
Cdd:PLN02582 546 VALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHE-VLITVEEG-SIGGFGSHVAQFMALD 620
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
179-540 |
5.39e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 81.21 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 179 YVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG-TPSIEDAESWHAKpMPReradaiikliesqiqtsrNLDPQPP 257
Cdd:PRK12315 212 YVEDGNDIESLIEAFKEVKDIDH-PIVLHIHTLKGKGyQPAEENKEAFHWH-MPF------------------DLETGQS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 258 IEDSPEVNITDVRMtsppDYrVGDKIATRKacglalaklgyannRVVVLDGDTRySTFS-EIFNKEYPERFIECFMAEQN 336
Cdd:PRK12315 272 KVPASGESYSSVTL----DY-LLKKIKEGK--------------PVVAINAAIP-GVFGlKEFRKKYPDQYVDVGIAEQE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 337 MVSVALGCASRG-RTIAFasTFAAFLTRAFDHIrIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIFY 415
Cdd:PRK12315 332 SVAFASGIAANGaRPVIF--VNSTFLQRAYDQL-SHDLAINNNPAVMIVFGGSISGNDVTHLGIFDIPMISNIPNLVYLA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 416 PTDA-----------VSTEHAVAlaanakgmcfIRTtrPETMVIYTPQE-------RFEIGQAkvlrhcvSDKVTVIGAG 477
Cdd:PRK12315 409 PTTKeeliamlewalTQHEHPVA----------IRV--PEHGVESGPTVdtdystlKYEVTKA-------GEKVAILALG 469
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225637461 478 iTVYE-ALAAADELSKQD-IFIRVIDLFTIKPLDVATIvSSAKATEGRIITVEDHYPQGGIGEAV 540
Cdd:PRK12315 470 -DFYElGEKVAKKLKEELgIDATLINPKFITGLDEELL-EKLKEDHELVVTLEDGILDGGFGEKI 532
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
318-547 |
7.37e-15 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 76.40 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 318 IFNKEYPERFIECFMAEQNMVSVALGCASRG-RTIAFASTFAaFLTRAFDHIrIGGLAESNINIIGShcgVSV-----GD 391
Cdd:PLN02683 67 LLQKYGPDRVLDTPITEAGFTGIGVGAAYAGlKPVVEFMTFN-FSMQAIDHI-INSAAKTNYMSAGQ---ISVpivfrGP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 392 DGAS-----QMALEDIAMFRTIPKCTIFYPTDAvstEHAVALAANAkgmcfIRTTRP----ETMVIY-----------TP 451
Cdd:PLN02683 142 NGAAagvgaQHSQCFAAWYSSVPGLKVLAPYSS---EDARGLLKAA-----IRDPDPvvflENELLYgesfpvsaevlDS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 452 QERFEIGQAKVLRHcvSDKVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATeGRIITVEDHY 531
Cdd:PLN02683 214 SFVLPIGKAKIERE--GKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
|
250
....*....|....*.
gi 225637461 532 PQGGIGEAVCAAVSMD 547
Cdd:PLN02683 291 PQHGVGAEICASVVEE 306
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
319-588 |
3.51e-12 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 69.36 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 319 FNKEYPERFIECFMAEQNMVSVALGCASRGRTiAFASTFAAFLTRAFDH-IRIGGLAESNINIIGSHCGVsVGDDGASQM 397
Cdd:PLN02225 417 FQERFPDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQvVHDVDRQRKAVRFVITSAGL-VGSDGPVQC 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 398 ALEDIAMFRTIPKCTIFYPTDAVSTEHAVALAA--NAKGMC--FIRTTRPETMVIYTPQERFEIGQAKVLRHcvSDKVTV 473
Cdd:PLN02225 495 GAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEIGRGRVLVE--GQDVAL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 474 IGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVaTIVSSAKATEGRIITVEDHYpQGGIGEAVCAAVS----MDPD 549
Cdd:PLN02225 573 LGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDI-KLVRDLCQNHKFLITVEEGC-VGGFGSHVAQFIAldgqLDGN 650
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 225637461 550 IQVHSLAV-SGVPQSGKSEELLDMYGISARHIIVAVKCML 588
Cdd:PLN02225 651 IKWRPIVLpDGYIEEASPREQLALAGLTGHHIAATALSLL 690
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
86-211 |
4.20e-11 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 64.05 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 86 ATGWLGQGLGVACGMAYTGKYFDRASYrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGALP-AEH 162
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALKYRGEDRV-AVCFFGDGATNEGDFHEALNFA---ALWKLPVIFVCenNGYAISTPTSrQTA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 225637461 163 CINIYQrRCEAFGWNTYVVDGRDVEALCQVFWQASQ---VKHKPTAVVAKTF 211
Cdd:cd02000 178 GTSIAD-RAAAYGIPGIRVDGNDVLAVYEAAKEAVErarAGGGPTLIEAVTY 228
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
90-260 |
1.03e-10 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 63.62 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 90 LGQGLGVACGMAYTGKYF--DRAsyrVFCLMSDGESSEGSVWEAMAFAsyySLDNLVAIFDV--NRLGHSGalPAEH--- 162
Cdd:COG1071 129 VGGQLPHAVGAALAAKLRgeDEV---AVAFFGDGATSEGDFHEALNFA---AVWKLPVVFVCenNGYAIST--PVERqta 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 163 CINIYQrRCEAFGWNTYVVDGRDVEALCQVFWQAsqVKH-----KPTAVVAKTFKGRG-----TPSI----EDAESWHAK 228
Cdd:COG1071 201 VETIAD-RAAGYGIPGVRVDGNDVLAVYAAVKEA--VERarageGPTLIEAKTYRLGGhstsdDPTRyrtkEEVEEWRER 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 225637461 229 -PMPR-------------ERADAIIKLIESQIQTSRNL---DPQPPIED 260
Cdd:COG1071 278 dPIERlraylleegllteEELEAIEAEAKAEVEEAVEFaeaSPEPDPEE 326
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
87-215 |
1.10e-06 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 49.47 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 87 TGWLGQGLGVACGMAytgKYFDRA--SYRVFCLMSDGESSEGSVWEAMAFASYYsLDNLVAIFDVNRlgHSGALPAEHCI 164
Cdd:cd02007 74 TGHSSTSISAALGMA---VARDLKgkKRKVIAVIGDGALTGGMAFEALNNAGYL-KSNMIVILNDNE--MSISPNVGTPG 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 225637461 165 NIYqrrcEAFGWN-TYVVDGRDVEALCQVFWQASQVKHkPTAVVAKTFKGRG 215
Cdd:cd02007 148 NLF----EELGFRyIGPVDGHNIEALIKVLKEVKDLKG-PVLLHVVTKKGKG 194
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
403-590 |
1.55e-06 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 50.51 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 403 AMFRTIPKCTIFyptdAVSTEHavalaaNAKGM--CFIRTTRP----ETMVIYT-----PQERF--EIGQAKVLRHcvSD 469
Cdd:CHL00144 135 SYFQSVPGLQIV----ACSTPY------NAKGLlkSAIRSNNPviffEHVLLYNlkeeiPDNEYllPLEKAEVVRP--GN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 470 KVTVIGAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEgRIITVEDHYPQGGIGEAVCAAV----- 544
Cdd:CHL00144 203 DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTH-KVLIVEECMKTGGIGAELIAQInehlf 281
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 225637461 545 -SMDPDIQVHSLAVSGVPQSGKSEELLDmygISARHIIVAVKCMLLN 590
Cdd:CHL00144 282 dELDAPIVRLSSQDVPTPYNGPLEEATV---IQPAQIIEAVEQIITN 325
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
82-189 |
4.08e-06 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 49.23 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 82 FVDVATGWLGQGLGVACGMAYTGKYFDRASY------RVFCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNR---- 151
Cdd:cd02017 112 FWEFPTVSMGLGPIQAIYQARFNRYLEDRGLkdtsdqKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLqrld 191
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 225637461 152 ---LGHSGAlpaehcINIYQRRCEAFGWN-TYVVDGRDVEAL 189
Cdd:cd02017 192 gpvRGNGKI------IQELEGIFRGAGWNvIKVIWGSKWDEL 227
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
74-210 |
3.71e-05 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 44.55 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 74 FVLAKRLSFVdVATGW--LGQGLGVACGMAYTGKyfDRasyRVFCLMSDGESSEGsvWEAMAFASYYSLDNLVAIFDVNR 151
Cdd:cd00568 31 LPLRRGRRFL-TSTGFgaMGYGLPAAIGAALAAP--DR---PVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNNGG 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225637461 152 LG---------HSGALPAEHCINI-YQRRCEAFGWNTYVVDgrDVEALCQVFWQASQvKHKPTAVVAKT 210
Cdd:cd00568 103 YGtirmhqeafYGGRVSGTDLSNPdFAALAEAYGAKGVRVE--DPEDLEAALAEALA-AGGPALIEVKT 168
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
89-270 |
4.79e-05 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 45.63 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 89 WLGQGLGVACGMAYTGKYF-----DRASYRV-FCLMSDGESSEGSVWEAMAFASYYsldNLVAIFDVNR------LGH-- 154
Cdd:CHL00149 129 FIGEGIPIALGAAFQSIYRqqvlkEVQPLRVtACFFGDGTTNNGQFFECLNMAVLW---KLPIIFVVENnqwaigMAHhr 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225637461 155 SGALPAEHciniyqRRCEAFGWNTYVVDGRDVEALCQVFWQA---SQVKHKPTAVVAKTFKGRGTP--------SIEDAE 223
Cdd:CHL00149 206 STSIPEIH------KKAEAFGLPGIEVDGMDVLAVREVAKEAverARQGDGPTLIEALTYRFRGHSladpdelrSKQEKE 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225637461 224 SWHAKpmpreraDAIIKL----IESQIQTSRNLDP-----QPPIED-------SPEVNITDVR 270
Cdd:CHL00149 280 AWVAR-------DPIKKLksyiIDNELASQKELNKiqrevKIEIEQavqfaisSPEPNISDLK 335
|
|
| |
