|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
1-663 |
0e+00 |
|
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: 1356.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 1 MPSRRERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGY 80
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 81 DLGIEDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMME 160
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 161 GISHEVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDGHDADEIKTAIDTARK-SDQPTL 239
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAeTDKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 240 ICCKTVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWEHAPFEIPAQIYAEWDA-KETGAAQEAEWNKRFAAYQAAHP 318
Cdd:COG0021 241 IICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAaGERGAAAEAEWNERFAAYAAAYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 319 ELAAELLRRLKGELPADFAEKAAAYVADvankGETIASRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGCKGVSAD 398
Cdd:COG0021 321 ELAAELERRLAGELPEDWDAALPAFEAD----AKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 399 DAAGNYVFYGVREFGMSAIMNGVALHGGFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQ 478
Cdd:COG0021 397 DPSGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 479 LASLRLTPNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQARDVAQVADIARGGYVLKDCEGEPELILIATG 558
Cdd:COG0021 477 LASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAEGVAKGAYVLADAEGTPDVILIATG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 559 SEVGLAVQAYDKLSEQGRKVRVVSMPCTSVYEQQDESYKQSVLPVEVGARIAIEAAHADYWYKYVGLDGRIIGMTSFGES 638
Cdd:COG0021 557 SEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGAS 636
|
650 660
....*....|....*....|....*
gi 15595745 639 APAPALFEHFGFTLDNVLAVAEELL 663
Cdd:COG0021 637 APAKVLFEEFGFTVENVVAAAKELL 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
5-663 |
0e+00 |
|
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: 1101.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 5 RERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYDLGI 84
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 85 EDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMMEGISH 164
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 165 EVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDGHDADEIKTAIDTARKS-DQPTLICCK 243
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKAStDKPTLIEVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 244 TVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWEHAPFEIPAQIY--AEWDAKETGAAQEAEWNKRFAAYQAAHPELA 321
Cdd:TIGR00232 241 TTIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYdhFKKTVKERGAKAEQEWNELFAAYKKKYPELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 322 AELLRRLKGELPADFAEKAAAYVAdvanKGETIASRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGcKGVSADDAA 401
Cdd:TIGR00232 321 AEFTRRLSGELPADWDKQLPEFKV----KLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKG-SGDLHENPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 402 GNYVFYGVREFGMSAIMNGVALHGGFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLAS 481
Cdd:TIGR00232 396 GNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 482 LRLTPNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQarDVAQVADIARGGYVLKDCEGePELILIATGSEV 561
Cdd:TIGR00232 476 LRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQL--EESSLEKVLKGGYVLKDSKG-PDLILIATGSEV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 562 GLAVQAYDKLSEQGRKVRVVSMPCTSVYEQQDESYKQSVLPVEVgARIAIEAAHADYWYKYVGLDGRIIGMTSFGESAPA 641
Cdd:TIGR00232 553 QLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPG 631
|
650 660
....*....|....*....|..
gi 15595745 642 PALFEHFGFTLDNVLAVAEELL 663
Cdd:TIGR00232 632 DKLFEEFGFTVENVVAKAKKLL 653
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-663 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 1073.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 1 MPSRRERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGY 80
Cdd:PRK05899 5 MELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 81 DLGIEDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMME 160
Cdd:PRK05899 85 DLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDLME 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 161 GISHEVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRnVDGHDADEIKTAIDTARKSDQPTLI 240
Cdd:PRK05899 165 GISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIE-VDGHDVEAIDAAIEEAKASTKPTLI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 241 CCKTVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWEHapfeipaqiyaewdaketgaaqeaewnkrfaayqaahpel 320
Cdd:PRK05899 244 IAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY---------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 321 aaellrrlkgelpadfaekaaayvadvankgetiasRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGCKGVSADDA 400
Cdd:PRK05899 284 ------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 401 AGNYVFYGVREFGMSAIMNGVALHGGFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLA 480
Cdd:PRK05899 328 SGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 481 SLRLTPNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQARDvAQVADIARGGYVLKDCegePELILIATGSE 560
Cdd:PRK05899 408 SLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERT-AQEEGVAKGGYVLRDD---PDVILIATGSE 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 561 VGLAVQAYDKLSEQGRKVRVVSMPCTSVYEQQDESYKQSVLPVEVGARIAIEAAHADYWYKYVGLDGRIIGMTSFGESAP 640
Cdd:PRK05899 484 VHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASAP 563
|
650 660
....*....|....*....|...
gi 15595745 641 APALFEHFGFTLDNVLAVAEELL 663
Cdd:PRK05899 564 ADELFKEFGFTVENIVAAAKELL 586
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
3-333 |
0e+00 |
|
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: 595.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 3 SRRERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYDL 82
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 83 GIEDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMMEGI 162
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 163 SHEVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDGHDADEIKTAIDTARKS-DQPTLIC 241
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEkDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 242 CKTVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWE-HAPFEIPAQIYAEWDAKE-TGAAQEAEWNKRFAAYQAAHPE 319
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEKVaEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 15595745 320 LAAELLRRLKGELP 333
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
9-273 |
6.35e-144 |
|
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: 418.83 E-value: 6.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 9 NAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYDLgIEDLK 88
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLP-EEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 89 NFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKvlaaqfnrdgHAVVDHYTYAFLGDGCMMEGISHEVAS 168
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEK----------LLGFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 169 LAGTLRLNKLIAFYDDNGISIDGEVHG-WFTDDTPKRFEAYGWQVIRnVDGHDADEIKTAIDTARKS-DQPTLICCKTVI 246
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIE-VDGHDVEEILAALEEAKKSkGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 15595745 247 GFGSPNKQGKEECHGAPLGADEIAATR 273
Cdd:cd02012 229 GKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
407-524 |
8.15e-39 |
|
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: 139.93 E-value: 8.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 407 YGVREFGMSAIMNGVALHGGfIPYGATFLIFMEYARNAVRMSALMkQRVLYVFTHDS-IGLGEDGPTHQPIEQLASLRLT 485
Cdd:smart00861 20 TGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGAS-GNVPVVFRHDGgGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110
....*....|....*....|....*....|....*....
gi 15595745 486 PNLDTWRPADAVESAVAWKHAIERaDGPSALIFSRQNLP 524
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
1-663 |
0e+00 |
|
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: 1356.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 1 MPSRRERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGY 80
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 81 DLGIEDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMME 160
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 161 GISHEVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDGHDADEIKTAIDTARK-SDQPTL 239
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAeTDKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 240 ICCKTVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWEHAPFEIPAQIYAEWDA-KETGAAQEAEWNKRFAAYQAAHP 318
Cdd:COG0021 241 IICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAaGERGAAAEAEWNERFAAYAAAYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 319 ELAAELLRRLKGELPADFAEKAAAYVADvankGETIASRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGCKGVSAD 398
Cdd:COG0021 321 ELAAELERRLAGELPEDWDAALPAFEAD----AKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 399 DAAGNYVFYGVREFGMSAIMNGVALHGGFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQ 478
Cdd:COG0021 397 DPSGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 479 LASLRLTPNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQARDVAQVADIARGGYVLKDCEGEPELILIATG 558
Cdd:COG0021 477 LASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAEGVAKGAYVLADAEGTPDVILIATG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 559 SEVGLAVQAYDKLSEQGRKVRVVSMPCTSVYEQQDESYKQSVLPVEVGARIAIEAAHADYWYKYVGLDGRIIGMTSFGES 638
Cdd:COG0021 557 SEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGAS 636
|
650 660
....*....|....*....|....*
gi 15595745 639 APAPALFEHFGFTLDNVLAVAEELL 663
Cdd:COG0021 637 APAKVLFEEFGFTVENVVAAAKELL 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
5-663 |
0e+00 |
|
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: 1101.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 5 RERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYDLGI 84
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 85 EDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMMEGISH 164
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 165 EVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDGHDADEIKTAIDTARKS-DQPTLICCK 243
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKAStDKPTLIEVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 244 TVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWEHAPFEIPAQIY--AEWDAKETGAAQEAEWNKRFAAYQAAHPELA 321
Cdd:TIGR00232 241 TTIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYdhFKKTVKERGAKAEQEWNELFAAYKKKYPELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 322 AELLRRLKGELPADFAEKAAAYVAdvanKGETIASRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGcKGVSADDAA 401
Cdd:TIGR00232 321 AEFTRRLSGELPADWDKQLPEFKV----KLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKG-SGDLHENPL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 402 GNYVFYGVREFGMSAIMNGVALHGGFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLAS 481
Cdd:TIGR00232 396 GNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 482 LRLTPNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQarDVAQVADIARGGYVLKDCEGePELILIATGSEV 561
Cdd:TIGR00232 476 LRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQL--EESSLEKVLKGGYVLKDSKG-PDLILIATGSEV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 562 GLAVQAYDKLSEQGRKVRVVSMPCTSVYEQQDESYKQSVLPVEVgARIAIEAAHADYWYKYVGLDGRIIGMTSFGESAPA 641
Cdd:TIGR00232 553 QLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPG 631
|
650 660
....*....|....*....|..
gi 15595745 642 PALFEHFGFTLDNVLAVAEELL 663
Cdd:TIGR00232 632 DKLFEEFGFTVENVVAKAKKLL 653
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-663 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 1073.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 1 MPSRRERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGY 80
Cdd:PRK05899 5 MELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 81 DLGIEDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMME 160
Cdd:PRK05899 85 DLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDLME 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 161 GISHEVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRnVDGHDADEIKTAIDTARKSDQPTLI 240
Cdd:PRK05899 165 GISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIE-VDGHDVEAIDAAIEEAKASTKPTLI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 241 CCKTVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWEHapfeipaqiyaewdaketgaaqeaewnkrfaayqaahpel 320
Cdd:PRK05899 244 IAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY---------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 321 aaellrrlkgelpadfaekaaayvadvankgetiasRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGCKGVSADDA 400
Cdd:PRK05899 284 ------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 401 AGNYVFYGVREFGMSAIMNGVALHGGFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLA 480
Cdd:PRK05899 328 SGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 481 SLRLTPNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQARDvAQVADIARGGYVLKDCegePELILIATGSE 560
Cdd:PRK05899 408 SLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERT-AQEEGVAKGGYVLRDD---PDVILIATGSE 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 561 VGLAVQAYDKLSEQGRKVRVVSMPCTSVYEQQDESYKQSVLPVEVGARIAIEAAHADYWYKYVGLDGRIIGMTSFGESAP 640
Cdd:PRK05899 484 VHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASAP 563
|
650 660
....*....|....*....|...
gi 15595745 641 APALFEHFGFTLDNVLAVAEELL 663
Cdd:PRK05899 564 ADELFKEFGFTVENIVAAAKELL 586
|
|
| PLN02790 |
PLN02790 |
transketolase |
11-663 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 924.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 11 IRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYD-LGIEDLKN 89
Cdd:PLN02790 1 IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 90 FRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMMEGISHEVASL 169
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 170 AGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDG-HDADEIKTAIDTARKS-DQPTLICCKTVIG 247
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGnTDYDEIRAAIKEAKAVtDKPTLIKVTTTIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 248 FGSPNKQGKEECHGAPLGADEIAATRAALGWEHAPFEIPAQIYAEW-DAKETGAAQEAEWNKRFAAYQAAHPELAAELLR 326
Cdd:PLN02790 241 YGSPNKANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWsKHTKEGAALEAEWNAKFAEYKKKYPEEAAELKS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 327 RLKGELPADFAEKAAAYVADvaNKGEtiASRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGCKGVSADDAAGNYVF 406
Cdd:PLN02790 321 LISGELPSGWEKALPTFTPE--DPAD--ATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 407 YGVREFGMSAIMNGVALHG-GFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLASLRLT 485
Cdd:PLN02790 397 FGVREHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAM 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 486 PNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQarDVAQVADIARGGYVLKDCEGE--PELILIATGSEVGL 563
Cdd:PLN02790 477 PNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNL--PGTSIEGVEKGGYVISDNSSGnkPDLILIGTGSELEI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 564 AVQAYDKLSEQGRKVRVVSMPCTSVYEQQDESYKQSVLPVEVGARIAIEAAHADYWYKYVGLDGRIIGMTSFGESAPAPA 643
Cdd:PLN02790 555 AAKAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGI 634
|
650 660
....*....|....*....|
gi 15595745 644 LFEHFGFTLDNVLAVAEELL 663
Cdd:PLN02790 635 LYKEFGFTVENVVAAAKSLL 654
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
8-664 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 865.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 8 ANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYDLGIEDL 87
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYDLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 88 KNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMMEGISHEVA 167
Cdd:PTZ00089 90 KNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCLQEGVSQEAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 168 SLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDGH-DADEIKTAIDTARKS-DQPTLICCKTV 245
Cdd:PTZ00089 170 SLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSkGKPKLIIVKTT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 246 IGFGSpNKQGKEECHGAPLGADEIAATRAALGWE-HAPFEIPAQIYAEWDA-KETGAAQEAEWNKRFAAYQAAHPELAAE 323
Cdd:PTZ00089 250 IGYGS-SKAGTEKVHGAPLGDEDIAQVKELFGLDpEKKFHVSEEVRQFFEQhVEKKKENYEAWKKRFAKYTAAFPKEAQA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 324 LLRRLKGELPADFAEKAAAYvadvANKGETIASRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGCKGVSADDAAGN 403
Cdd:PTZ00089 329 IERRFKGELPPGWEKKLPKY----TTNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTKASPEGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 404 YVFYGVREFGMSAIMNGVALHGGFIPYGATFLIFMEYARNAVRMSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLASLR 483
Cdd:PTZ00089 405 YIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 484 LTPNLDTWRPADAVESAVAWKHAIERADGPSALIFSRQNLPHQARDVAQvaDIARGGYVLKDCEGEPELILIATGSEVGL 563
Cdd:PTZ00089 485 ATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSSIE--GVLKGAYIVVDFTNSPQLILVASGSEVSL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 564 AVQAYDKLSEQGRkVRVVSMPCTSVYEQQDESYKQSVLPVEVGARIAIEAAHADYWYKYVGLDgriIGMTSFGESAPAPA 643
Cdd:PTZ00089 563 CVEAAKALSKELN-VRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVH---VGISGFGASAPANA 638
|
650 660
....*....|....*....|.
gi 15595745 644 LFEHFGFTLDNVLAVAEELLE 664
Cdd:PTZ00089 639 LYKHFGFTVENVVEKARALAA 659
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
3-333 |
0e+00 |
|
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: 595.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 3 SRRERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYDL 82
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 83 GIEDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKVLAAQFNRDGHAVVDHYTYAFLGDGCMMEGI 162
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 163 SHEVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFTDDTPKRFEAYGWQVIRNVDGHDADEIKTAIDTARKS-DQPTLIC 241
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEkDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 242 CKTVIGFGSPNKQGKEECHGAPLGADEIAATRAALGWE-HAPFEIPAQIYAEWDAKE-TGAAQEAEWNKRFAAYQAAHPE 319
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEKVaEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 15595745 320 LAAELLRRLKGELP 333
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
9-273 |
6.35e-144 |
|
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: 418.83 E-value: 6.35e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 9 NAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYDLgIEDLK 88
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLP-EEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 89 NFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKvlaaqfnrdgHAVVDHYTYAFLGDGCMMEGISHEVAS 168
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEK----------LLGFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 169 LAGTLRLNKLIAFYDDNGISIDGEVHG-WFTDDTPKRFEAYGWQVIRnVDGHDADEIKTAIDTARKS-DQPTLICCKTVI 246
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIE-VDGHDVEEILAALEEAKKSkGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 15595745 247 GFGSPNKQGKEECHGAPLGADEIAATR 273
Cdd:cd02012 229 GKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
5-277 |
1.72e-82 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 261.55 E-value: 1.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 5 RERANAIRALSMDAVQKANSGHPGAPMGMADIAEVLWRDYMQHNPSNPQWANRDRFVLSNGHGSMLIYSLLHLTGYdLGI 84
Cdd:COG3959 9 EEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKGY-FPK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 85 EDLKNFRQLNSRTPGHPEYGYTAGVETTTGPLGQGIANAVGMALAEKvlaaqfnRDGHavvDHYTYAFLGDGCMMEGISH 164
Cdd:COG3959 88 EELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAK-------LDGK---DYRVYVLLGDGELQEGQVW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 165 EVASLAGTLRLNKLIAFYDDNGISIDGevhgwFTDDT------PKRFEAYGWQVIRnVDGHDADEIKTAIDTARK-SDQP 237
Cdd:COG3959 158 EAAMAAAHYKLDNLIAIVDRNGLQIDG-----PTEDVmsleplAEKWEAFGWHVIE-VDGHDIEALLAALDEAKAvKGKP 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15595745 238 TLICCKTVIGFGSPNKQGKEECHGAPLGADEIAATRAALG 277
Cdd:COG3959 232 TVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELE 271
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
352-524 |
9.33e-60 |
|
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: 198.16 E-value: 9.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 352 ETIASRKASQNALNAFGPLLPELLGGSADLAGSNLTLWKGckgVSADDAAGNYVFYGVREFGMSAIMNGVALHGG-FIPY 430
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKG---LLHPQGAGRVIDTGIAEQAMVGFANGMALHGPlLPPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 431 GATFLIFMEYARNAVR-MSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLASLRLTPNLDTWRPADAVESAVAWKHAIER 509
Cdd:pfam02779 78 EATFSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRR 157
|
170
....*....|....*.
gi 15595745 510 AD-GPSALIFSRQNLP 524
Cdd:pfam02779 158 DGrKPVVLRLPRQLLR 173
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
358-520 |
4.34e-56 |
|
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: 187.65 E-value: 4.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 358 KASQNALNAFGPLLPELLGGSADLAGSNLTLWKgckgvsADDAAGNYVFYGVREFGMSAIMNGVALHGgFIPYGATFLIF 437
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKF------AKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 438 MEYARNAVR-MSALMKQRVLYVFTHDSIGLGEDGPTHQPIEQLASLRLTPNLDTWRPADAVESAVAWKHAIERaDGPSAL 516
Cdd:cd07033 74 LQRAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEY-DGPVYI 152
|
....
gi 15595745 517 IFSR 520
Cdd:cd07033 153 RLPR 156
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
407-524 |
8.15e-39 |
|
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: 139.93 E-value: 8.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 407 YGVREFGMSAIMNGVALHGGfIPYGATFLIFMEYARNAVRMSALMkQRVLYVFTHDS-IGLGEDGPTHQPIEQLASLRLT 485
Cdd:smart00861 20 TGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGAS-GNVPVVFRHDGgGGVGEDGPTHHSIEDEALLRAI 97
|
90 100 110
....*....|....*....|....*....|....*....
gi 15595745 486 PNLDTWRPADAVESAVAWKHAIERaDGPSALIFSRQNLP 524
Cdd:smart00861 98 PGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLY 135
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
540-655 |
1.71e-19 |
|
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: 84.57 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 540 GYVLKDCEGePELILIATGSEVGLAVQAYDKLSEQGRKVRVVSMPCTSVYEQQD-----ESYKQSVLPVEVGARIAIEAA 614
Cdd:pfam02780 1 GKAEILREG-DDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15595745 615 HADYWYK--YVGLDGRIIGMTS--FGESAPAPALFEHFGFTLDNV 655
Cdd:pfam02780 80 VAAALAEeaFDGLDAPVLRVGGpdFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
104-244 |
1.58e-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: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 104 GYTAGVETTTGPLGQGIANAVGMALAEKvlaaqfnrdghavvDHYTYAFLGDGCMMEGIShEVASlAGTLRLNkLIAFYD 183
Cdd:cd00568 36 GRRFLTSTGFGAMGYGLPAAIGAALAAP--------------DRPVVCIAGDGGFMMTGQ-ELAT-AVRYGLP-VIVVVF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595745 184 DNGISIDGEVH------------GWFTDDTPKRFEAYGWQVIRnVDghDADEIKTAIDTARKSDQPTLICCKT 244
Cdd:cd00568 99 NNGGYGTIRMHqeafyggrvsgtDLSNPDFAALAEAYGAKGVR-VE--DPEDLEAALAEALAAGGPALIEVKT 168
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
120-583 |
1.08e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 64.72 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 120 IANAVGMALAekvLAAQFNRDGHAVvdhytyAFLGDGCM---M--EGISHevaslAGTLRlNKLIAFYDDNGISID---G 191
Cdd:PRK05444 123 ISAALGMAKA---RDLKGGEDRKVV------AVIGDGALtggMafEALNN-----AGDLK-SDLIVILNDNEMSISpnvG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 192 EVHGWFTD---DTPkrFEAYGWQVIRNVDGHDADEIKTAIDTARKSDQPTLICCKTVIGFG-SPNKQGKEECHGAPL--- 264
Cdd:PRK05444 188 ALSNYLARlrsSTL--FEELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGyAPAEADPIKYHGVGKfdp 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 265 --GADEIAATRAALGWehapfeipAQIYAEWDAKEtgaaqeAEWNKRFAAYQAAHPE---LAAellrrlkgelpadFAEK 339
Cdd:PRK05444 266 etGEQPKSSKPGKPSY--------TKVFGETLCEL------AEKDPKIVAITAAMPEgtgLVK-------------FSKR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 340 AAAYVADVAnkgetIASrkasQNALnafgpllpellggsadlagsnlTLwkgckgvsaddAAGnyvfygvrefgMSAimn 419
Cdd:PRK05444 319 FPDRYFDVG-----IAE----QHAV----------------------TF-----------AAG-----------LAT--- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 420 gvalhGGFIPYGA---TFL------IFMEyarnaVrmsALMKQRVlyVFTHDSIGL-GEDGPTHQPIEQLASLRLTPNLD 489
Cdd:PRK05444 343 -----EGLKPVVAiysTFLqraydqVIHD-----V---ALQNLPV--TFAIDRAGLvGADGPTHQGAFDLSYLRCIPNMV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 490 TWRPADAVE--SAVAWkhAIERADGPSALIFSRQNLPHQARDVAQVADIARGGyVLKdcEGEpELILIATGSEVGLAVQA 567
Cdd:PRK05444 408 IMAPSDENElrQMLYT--ALAYDDGPIAIRYPRGNGVGVELPELEPLPIGKGE-VLR--EGE-DVAILAFGTMLAEALKA 481
|
490
....*....|....*.
gi 15595745 568 YDKLSEqgrkVRVVSM 583
Cdd:PRK05444 482 AERLAS----ATVVDA 493
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
4-223 |
1.18e-10 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 63.86 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 4 RRERAnAIRALSMDAVQKANS------GHPGAPMGMADIAEVLWrDYMQHNPSNPQWANRdrfVLSNGHGSMLIYSLLHL 77
Cdd:cd02017 5 RRIRS-LIRWNAMAMVHRANKkdlgigGHIATFASAATLYEVGF-NHFFRARGEGGGGDL---VYFQGHASPGIYARAFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 78 TGyDLGIEDLKNFRQ------LNS-----RTPGHPEYgytagvetTTGPLGQGIANAVGMALAEKVLAAQ-FNRDGHAVV 145
Cdd:cd02017 80 EG-RLTEEQLDNFRQevggggLSSyphpwLMPDFWEF--------PTVSMGLGPIQAIYQARFNRYLEDRgLKDTSDQKV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 146 dhytYAFLGDGCMMEGISHEVASLAGTLRLNKLIAFYDDNGISIDGEVHGWFT--DDTPKRFEAYGWQVIRNVDGHDADE 223
Cdd:cd02017 151 ----WAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPVRGNGKiiQELEGIFRGAGWNVIKVIWGSKWDE 226
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
5-628 |
7.31e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 62.05 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 5 RERANAIRALSMDAVQKAnSGHPGAPMGMADIAEVLWRDYmqhnpSNPqwanRDRFVLSNGHGSmliYSLLHLTGYDlgi 84
Cdd:PRK12571 27 EQLADELRAEVISAVSET-GGHLGSSLGVVELTVALHAVF-----NTP----KDKLVWDVGHQC---YPHKILTGRR--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 85 edlKNFRQLnsRTPGHPEyGYTAGVETTTGPLGQG-----IANAVGMALAEKVLaaqfNRDGHAVvdhytyAFLGDGCMM 159
Cdd:PRK12571 91 ---DRFRTL--RQKGGLS-GFTKRSESEYDPFGAAhsstsISAALGFAKARALG----QPDGDVV------AVIGDGSLT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 160 EGISHEVASLAGTLRlNKLIAFYDDNGISID---GEVHGWFTD--------------------------DTPKR------ 204
Cdd:PRK12571 155 AGMAYEALNNAGAAD-RRLIVILNDNEMSIAppvGALAAYLSTlrssdpfarlraiakgveerlpgplrDGARRarelvt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 205 --------FEAYGWQVIRNVDGHDADEIKTAIDTAR-KSDQPTLICCKTVIGFGSPNKQGKEEC-HGapLGADEIAATRA 274
Cdd:PRK12571 234 gmigggtlFEELGFTYVGPIDGHDMEALLSVLRAARaRADGPVLVHVVTEKGRGYAPAEADEDKyHA--VGKFDVVTGLQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 275 ALGWEHAPfeipaqiyaEW-DAKETGAAQEAEWNKRFAAYQAAHPelaaellrrlkgeLPADFAEKAAAYVADVANKGet 353
Cdd:PRK12571 312 KKSAPSAP---------SYtSVFGEELTKEAAEDSDIVAITAAMP-------------LGTGLDKLQKRFPNRVFDVG-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 354 iasrKASQNALnAFgpllpellggSADLAgsnltlwkgckgvsaddaagnyvfygvrefgmsaimngvalHGGFIPYGAT 433
Cdd:PRK12571 368 ----IAEQHAV-TF----------AAGLA-----------------------------------------AAGLKPFCAV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 434 FLIFMEYARNAVRMS-ALMKQRVLYVFthDSIGL-GEDGPTHQPIEQLASLRLTPNLDTWRPADAVESAVAWKHAIERAD 511
Cdd:PRK12571 392 YSTFLQRGYDQLLHDvALQNLPVRFVL--DRAGLvGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDD 469
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 512 GPSALIFSRQNLPHQA-RDVAQVADIARGGYVLKDcegePELILIATGSEVGLAVQAYDKLSEQGRKVRVVSM----PCT 586
Cdd:PRK12571 470 GPIAVRFPRGEGVGVEiPAEGTILGIGKGRVPREG----PDVAILSVGAHLHECLDAADLLEAEGISVTVADPrfvkPLD 545
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 15595745 587 SVYEQQDESYKQSVLPVEVGARIAIEAAHADYWYKYVGLDGR 628
Cdd:PRK12571 546 EALTDLLVRHHIVVIVEEQGAMGGFGAHVLHHLADTGLLDGG 587
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
105-245 |
7.94e-10 |
|
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: 60.59 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 105 YTAGVETTTGPLGQGIANAVGMALAEKvlaaqfnRDGHAVVdhyTYAFLGDGCMMEGISHEVASLAGTLRLNkLIAFYDD 184
Cdd:cd02000 95 KEKNFFGGNGIVGGQVPLAAGAALALK-------YRGEDRV---AVCFFGDGATNEGDFHEALNFAALWKLP-VIFVCEN 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595745 185 NGISIDGEVHGWFTDDTP-KRFEAYGWQVIRnVDGHDADEI----KTAIDTARKSDQPTLICCKTV 245
Cdd:cd02000 164 NGYAISTPTSRQTAGTSIaDRAAAYGIPGIR-VDGNDVLAVyeaaKEAVERARAGGGPTLIEAVTY 228
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
425-583 |
8.88e-10 |
|
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: 61.57 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 425 GGFIPYGA---TFL------IFMEyarnaVrmsALMKQRVlyVFTHDSIGL-GEDGPTHQPIEQLASLRLTPNLDTWRPA 494
Cdd:COG1154 381 EGLKPVVAiysTFLqraydqVIHD-----V---ALQNLPV--TFAIDRAGLvGADGPTHHGVFDLSYLRCIPNMVIMAPK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 495 DAVE------SAVAWkhaieraDGPSALIFSRQNLPHQARDvAQVADIARG-GYVLKdcEGEpELILIATGSEVGLAVQA 567
Cdd:COG1154 451 DENElrhmlyTALAY-------DGPTAIRYPRGNGPGVELP-AELEPLPIGkGEVLR--EGK-DVAILAFGTMVAEALEA 519
|
170
....*....|....*.
gi 15595745 568 YDKLSEQGRKVRVVSM 583
Cdd:COG1154 520 AERLAAEGISATVVDA 535
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
57-249 |
1.76e-08 |
|
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: 54.86 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 57 RDRFVLSNGHGSmliYSLLHLTGYDLGIEDLKNFRQLNsrtpghpeyGYTAGVET-----TTGPLGQGIANAVGMALAEK 131
Cdd:cd02007 25 KDKIIWDVGHQA---YPHKILTGRRDQFHTLRQYGGLS---------GFTKRSESeydafGTGHSSTSISAALGMAVARD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 132 VLaaqfNRDGHAVvdhytyAFLGDGCMMEGISHEVASLAGTLRlNKLIAFYDDNGISIDGEV--HGWFtddtpkrFEAYG 209
Cdd:cd02007 93 LK----GKKRKVI------AVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSISPNVgtPGNL-------FEELG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15595745 210 WQVIRNVDGHDADEIKTAIDTARKSDQPTLICCKTVIGFG 249
Cdd:cd02007 155 FRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGKG 194
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
25-580 |
5.09e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 49.71 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 25 GHPGAPMGMADIAEVLwrDYMQHNPsnpqwanRDRFVLSNGHGSmliYSLLHLTGYDlgiEDLKNFRQLNSRTpghpeyG 104
Cdd:PLN02234 104 GHLGSNLGVVELTVAL--HYIFNTP-------HDKILWDVGHQS---YPHKILTGRR---GKMKTIRQTNGLS------G 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 105 YTAGVETTTGPLGQG-----IANAVGMALAEKVLAaqfnrdghavVDHYTYAFLGDGCMMEGISHEVASLAGTLRLNKLI 179
Cdd:PLN02234 163 YTKRRESEHDSFGTGhssttLSAGLGMAVGRDLKG----------MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 180 AFYDDNGIS-----IDGEVH----------------GWFTDDTPKRFEAYGWQVIRNVDGHDADEIKTAIDTAR--KSDQ 236
Cdd:PLN02234 233 ILNDNKQVSlptanLDGPTQpvgalscalsrlqsncGMIRETSSTLFEELGFHYVGPVDGHNIDDLVSILETLKstKTIG 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 237 PTLICCKTVIGFGSPNKQGKEECHGAPLGADEIAATRaalgwehapFEIPAQIYAEWDAKETGAAQEAEWNKRFAAYQAA 316
Cdd:PLN02234 313 PVLIHVVTEKGRGYPYAERADDKYHGVLKFDPETGKQ---------FKNISKTQSYTSCFVEALIAEAEADKDIVAIHAA 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 317 hpelaaellrrlkgelpadfaekaaayvadvankgetiasrkasqnalnafgpllpelLGGsadlaGSNLTLWKGCKGVS 396
Cdd:PLN02234 384 ----------------------------------------------------------MGG-----GTMLNLFESRFPTR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 397 ADDAagnyvfyGVREFGMSAIMNGVALHgGFIPYGATFLIFMEYARNAVRMSALMkQRVLYVFTHDSIGL-GEDGPTHQP 475
Cdd:PLN02234 401 CFDV-------GIAEQHAVTFAAGLACE-GLKPFCTIYSSFMQRAYDQVVHDVDL-QKLPVRFAIDRAGLmGADGPTHCG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 476 IEQLASLRLTPNLDTWRPADAVE--SAVAWKHAIEraDGPSALIFSRQN-----LPHQARDVAqvADIARgGYVLKDCEg 548
Cdd:PLN02234 472 AFDVTFMACLPNMIVMAPSDEAElfNMVATAAAID--DRPSCFRYHRGNgigvsLPPGNKGVP--LQIGR-GRILRDGE- 545
|
570 580 590
....*....|....*....|....*....|..
gi 15595745 549 epELILIATGSEVGLAVQAYDKLSEQGRKVRV 580
Cdd:PLN02234 546 --RVALLGYGSAVQRCLEAASMLSERGLKITV 575
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
116-244 |
9.75e-06 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 48.40 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 116 LGQGIANAVGMALAEKvlaaqFNRD--GHAVVDHYTYAFLGDGCMMEGISHEVASLAGTLRLNklIAFYDDNGISIDGEV 193
Cdd:PLN02374 196 IGEGIPVATGAAFSSK-----YRREvlKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLP--IVFVVENNLWAIGMS 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15595745 194 HGWFTDDTP--KRFEAYGWQVIrNVDGHDADEI----KTAIDTARKSDQPTLICCKT 244
Cdd:PLN02374 269 HLRATSDPEiwKKGPAFGMPGV-HVDGMDVLKVrevaKEAIERARRGEGPTLVECET 324
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
120-260 |
2.29e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 44.23 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 120 IANAVGMALAEKVlaaqfnRDGHAVVdhytYAFLGDGCMMEGISHEVASLAGTLRLNkLIAFYDDNGISIDGEVHGWFTD 199
Cdd:PRK12315 119 IALATGLAKARDL------KGEKGNI----IAVIGDGSLSGGLALEGLNNAAELKSN-LIIIVNDNQMSIAENHGGLYKN 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595745 200 -----DTPKR-----FEAYGWQVIRNVDGHDadeIKTAIDTARK---SDQPTLICCKTVIGFG-SPNKQGKEECH 260
Cdd:PRK12315 188 lkelrDTNGQsennlFKAMGLDYRYVEDGND---IESLIEAFKEvkdIDHPIVLHIHTLKGKGyQPAEENKEAFH 259
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
114-240 |
3.67e-04 |
|
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: 43.61 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 114 GPLGQGIANAVGMALAekvlaaqfnRDGHAVVdhytyAFLGDGCMMEGIsHEVASLAgTLRLNKLIAFYDDNGIsidGEV 193
Cdd:COG0028 412 GTMGYGLPAAIGAKLA---------RPDRPVV-----AITGDGGFQMNL-QELATAV-RYGLPVKVVVLNNGGL---GMV 472
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595745 194 HGWFTDDTPKRF--------------EAYGWQVIRnVDghDADEIKTAIDTARKSDQPTLI 240
Cdd:COG0028 473 RQWQELFYGGRYsgtdlpnpdfaklaEAFGAKGER-VE--TPEELEAALEEALASDGPALI 530
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
107-245 |
4.94e-03 |
|
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: 39.62 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 107 AGVETTTGPLGQGIANAVGMALAEKvlaaqfnRDGHAVVdhyTYAFLGDGCMMEGISHEVASLAGTLRLnKLIAFYDDNG 186
Cdd:pfam00676 94 NRFYGGNGILGAQVPLGAGIALAAK-------YRGKKEV---AITLYGDGAANQGDFFEGLNFAALWKL-PVIFVCENNQ 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595745 187 ISIDGEV-HGWFTDDTPKRFEAYGWQVIRnVDGHDADEI----KTAIDTARKSDQPTLICCKTV 245
Cdd:pfam00676 163 YGISTPAeRASASTTYADRARGYGIPGLH-VDGMDPLAVyqasKFAAERARTGKGPFLIELVTY 225
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
426-664 |
7.29e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 39.50 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 426 GFIPYGATFLIFMEYARNAVRMSALMkQRVLYVFTHDSIGL-GEDGPTHQPIEQLASLRLTPNLDTWRPADAVE--SAVA 502
Cdd:PLN02582 421 GLKPFCAIYSSFLQRGYDQVVHDVDL-QKLPVRFAMDRAGLvGADGPTHCGAFDVTYMACLPNMVVMAPSDEAElfHMVA 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 503 WKHAIEraDGPSALIFSRQN-----LPHQARDVAqvADIARGGYVLkdcEGEpELILIATGSEVGLAVQAYDKLSEQGRK 577
Cdd:PLN02582 500 TAAAID--DRPSCFRYPRGNgigvqLPPNNKGIP--IEVGKGRILL---EGE-RVALLGYGTAVQSCLAAASLLERHGLS 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595745 578 VRVVSM----PCTSVYEQQDESYKQSVLPVEVGArIAIEAAHAdywYKYVGLDGRIIGMTSF----------GESAPAPA 643
Cdd:PLN02582 572 ATVADArfckPLDRALIRSLAKSHEVLITVEEGS-IGGFGSHV---AQFMALDGLLDGKLKWrplvlpdryiDHGAPADQ 647
|
250 260
....*....|....*....|....*..
gi 15595745 644 LFE------HFGFTLDNVLAVAEELLE 664
Cdd:PLN02582 648 LAEagltpsHIAATVLNVLGQTREALQ 674
|
|
| |
