|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
18-692 |
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: 1212.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 18 TDLDKRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGY 97
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 98 GLEIEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDPeaaPGESPFDHHVFVICSDGD 177
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNR---PGHDIVDHYTYVIAGDGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 178 IEEGVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGGENVSGILDALEAAKAETAR 257
Cdd:COG0021 158 LMEGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 258 PSFILLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPEQtFVVEPEVLKHVREVVARGEAAKAEWQQGFDAWR 337
Cdd:COG0021 238 PTLIICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAAGERGAAAEAEWNERFAAYA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 338 AANPERNALLERAQDYRLPEGLDDALPSWEPDAKGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADSFGPp 417
Cdd:COG0021 317 AAYPELAAELERRLAGELPEDWDAALPAFEADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSP- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 418 saatkhwnTTPYGRTLHFGVREHAMGSILNGIVLHGPTRPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIGLGED 497
Cdd:COG0021 396 --------EDPSGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 498 GPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTKElAREGVAKGGYVLADTEG 577
Cdd:COG0021 468 GPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAA-AAEGVAKGAYVLADAEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 578 EPRVVLIGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKARVVVEAGIAQPWHRFAGDAGE 657
Cdd:COG0021 547 TPDVILIATGSEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGA 626
|
650 660 670
....*....|....*....|....*....|....*
gi 2520578889 658 IVSIEHFGASADYQTLFREFGITTEAVVAAAHRSI 692
Cdd:COG0021 627 VIGIDTFGASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
14-692 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 970.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 14 PSDWTDLDKRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLF 93
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 94 FSGYGLEIEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDPEAApgeSPFDHHVFVIC 173
Cdd:PRK05899 81 LAGYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGL---DIVDHYTYVLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 174 SDGDIEEGVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGgENVSGILDALEAAKA 253
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDG-HDVEAIDAAIEEAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 254 ETaRPSFILLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPeqtfvvepevlkhvrevvargeaakaewqqgf 333
Cdd:PRK05899 237 ST-KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY-------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 334 dawraanpernalleraqdyrlpeglddalpswepdakgvatRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADS 413
Cdd:PRK05899 284 ------------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 414 FGPPSAAtkhwnttpyGRTLHFGVREHAMGSILNGIVLHGPTRPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIG 493
Cdd:PRK05899 322 FAPEDYS---------GRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIG 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 494 LGEDGPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTKelAREGVAKGGYVLA 573
Cdd:PRK05899 393 VGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTA--QEEGVAKGGYVLR 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 574 DtegEPRVVLIGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKARVVVEAGIAQPWHRFAG 653
Cdd:PRK05899 471 D---DPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVG 547
|
650 660 670
....*....|....*....|....*....|....*....
gi 2520578889 654 DAGEIVSIEHFGASADYQTLFREFGITTEAVVAAAHRSI 692
Cdd:PRK05899 548 LDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
22-692 |
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: 820.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 22 KRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYGLEI 101
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 102 EDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDpeaAPGESPFDHHVFVICSDGDIEEG 181
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFN---KPGFEIVDHYTYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 182 VTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGGENVSGILDALEAAKAETARPSFI 261
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 262 LLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPEQtFVVEPEVLKHV-REVVARGEAAKAEWQQGFDAWRAAN 340
Cdd:TIGR00232 238 EVKTTIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFkKTVKERGAKAEQEWNELFAAYKKKY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 341 PERNALLERAQDYRLPEGLDDALPSWEPDAKGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADSFgppsaa 420
Cdd:TIGR00232 317 PELAAEFTRRLSGELPADWDKQLPEFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL------ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 421 tkhwNTTPYGRTLHFGVREHAMGSILNGIVLHGPTRPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIGLGEDGPT 500
Cdd:TIGR00232 391 ----HENPLGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 501 HQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTkelAREGVAKGGYVLADTEGePR 580
Cdd:TIGR00232 467 HQPIEQLASLRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEES---SLEKVLKGGYVLKDSKG-PD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 581 VVLIGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKaRVVVEAGIAQPWHRFAGDAGEIVS 660
Cdd:TIGR00232 543 LILIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILG 621
|
650 660 670
....*....|....*....|....*....|..
gi 2520578889 661 IEHFGASADYQTLFREFGITTEAVVAAAHRSI 692
Cdd:TIGR00232 622 MDSFGESAPGDKLFEEFGFTVENVVAKAKKLL 653
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
21-356 |
2.34e-165 |
|
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: 478.04 E-value: 2.34e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 21 DKRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYGLE 100
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 101 IEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAarrERGLFDPEAAPGESPFDHHVFVICSDGDIEE 180
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIA---ERNLAATYNRPGFDIVDHYTYVFLGDGCLME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 181 GVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGGENVSGILDALEAAKAETARPSF 260
Cdd:pfam00456 159 GVSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 261 ILLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPEQTFVVEPEVLKHVREVVARGEAAKAEWQQGFDAWRAAN 340
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAY 318
|
330
....*....|....*.
gi 2520578889 341 PERNALLERAQDYRLP 356
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
26-294 |
1.19e-120 |
|
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: 360.67 E-value: 1.19e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 26 DTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYgLEIEDIQ 105
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 106 ALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRerglfdpeaapgeSPFDHHVFVICSDGDIEEGVTSE 185
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKL-------------LGFDYRVYVLLGDGELQEGSVWE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 186 ASSLAGRQELGNLTVVYDDNKISIEDDTT-VALSEDTAKRYEAYGWHVQVVEgGENVSGILDALEAAKAETARPSFILLR 264
Cdd:cd02012 147 AASFAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEVD-GHDVEEILAALEEAKKSKGKPTLIIAK 225
|
250 260 270
....*....|....*....|....*....|
gi 2520578889 265 TIIGFPAPTLMNTGKAHGAALGTEEVAAVK 294
Cdd:cd02012 226 TIKGKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
433-552 |
1.06e-35 |
|
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: 131.07 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 433 LHFGVREHAMGSILNGIVLHGPtRPYGGTFLVFSDYMRPAVRLAALSGLpVTYVWTHDS-IGLGEDGPTHQPVEHLAALR 511
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2520578889 512 AIPGLVVLRPGDANETAAAWRAVLgQHEHPVGLALTRQNLP 552
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAI-RDDGPVVIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
18-692 |
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: 1212.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 18 TDLDKRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGY 97
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 98 GLEIEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDPeaaPGESPFDHHVFVICSDGD 177
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNR---PGHDIVDHYTYVIAGDGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 178 IEEGVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGGENVSGILDALEAAKAETAR 257
Cdd:COG0021 158 LMEGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 258 PSFILLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPEQtFVVEPEVLKHVREVVARGEAAKAEWQQGFDAWR 337
Cdd:COG0021 238 PTLIICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAAGERGAAAEAEWNERFAAYA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 338 AANPERNALLERAQDYRLPEGLDDALPSWEPDAKGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADSFGPp 417
Cdd:COG0021 317 AAYPELAAELERRLAGELPEDWDAALPAFEADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSP- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 418 saatkhwnTTPYGRTLHFGVREHAMGSILNGIVLHGPTRPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIGLGED 497
Cdd:COG0021 396 --------EDPSGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 498 GPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTKElAREGVAKGGYVLADTEG 577
Cdd:COG0021 468 GPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAA-AAEGVAKGAYVLADAEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 578 EPRVVLIGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKARVVVEAGIAQPWHRFAGDAGE 657
Cdd:COG0021 547 TPDVILIATGSEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGA 626
|
650 660 670
....*....|....*....|....*....|....*
gi 2520578889 658 IVSIEHFGASADYQTLFREFGITTEAVVAAAHRSI 692
Cdd:COG0021 627 VIGIDTFGASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
14-692 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 970.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 14 PSDWTDLDKRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLF 93
Cdd:PRK05899 1 SMMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 94 FSGYGLEIEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDPEAApgeSPFDHHVFVIC 173
Cdd:PRK05899 81 LAGYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGL---DIVDHYTYVLC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 174 SDGDIEEGVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGgENVSGILDALEAAKA 253
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDG-HDVEAIDAAIEEAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 254 ETaRPSFILLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPeqtfvvepevlkhvrevvargeaakaewqqgf 333
Cdd:PRK05899 237 ST-KPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY-------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 334 dawraanpernalleraqdyrlpeglddalpswepdakgvatRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADS 413
Cdd:PRK05899 284 ------------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 414 FGPPSAAtkhwnttpyGRTLHFGVREHAMGSILNGIVLHGPTRPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIG 493
Cdd:PRK05899 322 FAPEDYS---------GRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIG 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 494 LGEDGPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTKelAREGVAKGGYVLA 573
Cdd:PRK05899 393 VGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTA--QEEGVAKGGYVLR 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 574 DtegEPRVVLIGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKARVVVEAGIAQPWHRFAG 653
Cdd:PRK05899 471 D---DPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVG 547
|
650 660 670
....*....|....*....|....*....|....*....
gi 2520578889 654 DAGEIVSIEHFGASADYQTLFREFGITTEAVVAAAHRSI 692
Cdd:PRK05899 548 LDGKVLGIDTFGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
22-692 |
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: 820.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 22 KRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYGLEI 101
Cdd:TIGR00232 1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 102 EDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDpeaAPGESPFDHHVFVICSDGDIEEG 181
Cdd:TIGR00232 81 EDLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFN---KPGFEIVDHYTYVFVGDGCLQEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 182 VTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGGENVSGILDALEAAKAETARPSFI 261
Cdd:TIGR00232 158 ISYEVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 262 LLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPEQtFVVEPEVLKHV-REVVARGEAAKAEWQQGFDAWRAAN 340
Cdd:TIGR00232 238 EVKTTIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFkKTVKERGAKAEQEWNELFAAYKKKY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 341 PERNALLERAQDYRLPEGLDDALPSWEPDAKGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADSFgppsaa 420
Cdd:TIGR00232 317 PELAAEFTRRLSGELPADWDKQLPEFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL------ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 421 tkhwNTTPYGRTLHFGVREHAMGSILNGIVLHGPTRPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIGLGEDGPT 500
Cdd:TIGR00232 391 ----HENPLGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 501 HQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTkelAREGVAKGGYVLADTEGePR 580
Cdd:TIGR00232 467 HQPIEQLASLRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEES---SLEKVLKGGYVLKDSKG-PD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 581 VVLIGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKaRVVVEAGIAQPWHRFAGDAGEIVS 660
Cdd:TIGR00232 543 LILIATGSEVQLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILG 621
|
650 660 670
....*....|....*....|....*....|..
gi 2520578889 661 IEHFGASADYQTLFREFGITTEAVVAAAHRSI 692
Cdd:TIGR00232 622 MDSFGESAPGDKLFEEFGFTVENVVAKAKKLL 653
|
|
| PLN02790 |
PLN02790 |
transketolase |
29-688 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 818.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 29 RVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGY-GLEIEDIQAL 107
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdSVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 108 RTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDpeaAPGESPFDHHVFVICSDGDIEEGVTSEAS 187
Cdd:PLN02790 82 RQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFN---KPDHKIVDHYTYCILGDGCQMEGISNEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 188 SLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGG-ENVSGILDALEAAKAETARPSFILLRTI 266
Cdd:PLN02790 159 SLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGnTDYDEIRAAIKEAKAVTDKPTLIKVTTT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 267 IGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFdPEQTFVVEPEVLKHVREVVARGEAAKAEWQQGFDAWRAANPERNAL 346
Cdd:PLN02790 239 IGYGSPNKANSYSVHGAALGEKEVDATRKNLGW-PYEPFHVPEDVKSHWSKHTKEGAALEAEWNAKFAEYKKKYPEEAAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 347 LERAQDYRLPEGLDDALPSWEPDAKGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADSFGPPsaatkhwnt 426
Cdd:PLN02790 318 LKSLISGELPSGWEKALPTFTPEDPADATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKD--------- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 427 TPYGRTLHFGVREHAMGSILNGIVLHGPT-RPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIGLGEDGPTHQPVE 505
Cdd:PLN02790 389 TPEERNVRFGVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 506 HLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTkelAREGVAKGGYVLADTEGE--PRVVL 583
Cdd:PLN02790 469 HLASLRAMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGT---SIEGVEKGGYVISDNSSGnkPDLIL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 584 IGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKARVVVEAGIAQPWHRFAGDAGEIVSIEH 663
Cdd:PLN02790 546 IGTGSELEIAAKAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDR 625
|
650 660
....*....|....*....|....*
gi 2520578889 664 FGASADYQTLFREFGITTEAVVAAA 688
Cdd:PLN02790 626 FGASAPAGILYKEFGFTVENVVAAA 650
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
19-688 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 764.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 19 DLDKRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYG 98
Cdd:PTZ00089 4 AIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 99 LEIEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRERGLFDpeaAPGESPFDHHVFVICSDGDI 178
Cdd:PTZ00089 84 LSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFN---RPGHPIFDNYVYVICGDGCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 179 EEGVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGGE-NVSGILDALEAAKAETAR 257
Cdd:PTZ00089 161 QEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSKGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 258 PSFILLRTIIGFpAPTLMNTGKAHGAALGTEEVAAVKRILGFDPEQTFVVEPEVLKHVREVVARGEAAKAEWQQGFDAWR 337
Cdd:PTZ00089 241 PKLIIVKTTIGY-GSSKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 338 AANPERNALLERAQDYRLPEGLDDALPSWEPDAKGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADSFGPP 417
Cdd:PTZ00089 320 AAFPKEAQAIERRFKGELPPGWEKKLPKYTTNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTKA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 418 SaatkhwnttPYGRTLHFGVREHAMGSILNGIVLHGPTRPYGGTFLVFSDYMRPAVRLAALSGLPVTYVWTHDSIGLGED 497
Cdd:PTZ00089 400 S---------PEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGED 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 498 GPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPVLTGTkelAREGVAKGGYVLADTEG 577
Cdd:PTZ00089 471 GPTHQPVETLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGS---SIEGVLKGAYIVVDFTN 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 578 EPRVVLIGTGSELQIAVEAREVLAKDgIAARVVSIPSIEWFDAQDQSYRDSVLPPSVKARVVVEAGIAQPWHRFAGDAge 657
Cdd:PTZ00089 548 SPQLILVASGSEVSLCVEAAKALSKE-LNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVH-- 624
|
650 660 670
....*....|....*....|....*....|.
gi 2520578889 658 iVSIEHFGASADYQTLFREFGITTEAVVAAA 688
Cdd:PTZ00089 625 -VGISGFGASAPANALYKHFGFTVENVVEKA 654
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
21-356 |
2.34e-165 |
|
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: 478.04 E-value: 2.34e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 21 DKRAVDTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYGLE 100
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 101 IEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAarrERGLFDPEAAPGESPFDHHVFVICSDGDIEE 180
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIA---ERNLAATYNRPGFDIVDHYTYVFLGDGCLME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 181 GVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALSEDTAKRYEAYGWHVQVVEGGENVSGILDALEAAKAETARPSF 260
Cdd:pfam00456 159 GVSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 261 ILLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILGFDPEQTFVVEPEVLKHVREVVARGEAAKAEWQQGFDAWRAAN 340
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAY 318
|
330
....*....|....*.
gi 2520578889 341 PERNALLERAQDYRLP 356
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
26-294 |
1.19e-120 |
|
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: 360.67 E-value: 1.19e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 26 DTLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYgLEIEDIQ 105
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 106 ALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARRerglfdpeaapgeSPFDHHVFVICSDGDIEEGVTSE 185
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKL-------------LGFDYRVYVLLGDGELQEGSVWE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 186 ASSLAGRQELGNLTVVYDDNKISIEDDTT-VALSEDTAKRYEAYGWHVQVVEgGENVSGILDALEAAKAETARPSFILLR 264
Cdd:cd02012 147 AASFAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEVD-GHDVEEILAALEEAKKSKGKPTLIIAK 225
|
250 260 270
....*....|....*....|....*....|
gi 2520578889 265 TIIGFPAPTLMNTGKAHGAALGTEEVAAVK 294
Cdd:cd02012 226 TIKGKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
19-298 |
1.86e-73 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 238.82 E-value: 1.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 19 DLDKRAVDtLRVLAADAVQKVGNGHPGTAMSLAPLAYALYQRVMRHDPSDPHWIGRDRFVLSAGHSSLTQYLQLFFSGYg 98
Cdd:COG3959 7 ELEEKARQ-IRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKGY- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 99 LEIEDIQALRTWGSKTPGHPEVNHTKGVEITTGPLGQGLASAVGMAMAARReRGLfdpeaapgespfDHHVFVICSDGDI 178
Cdd:COG3959 85 FPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKL-DGK------------DYRVYVLLGDGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 179 EEGVTSEASSLAGRQELGNLTVVYDDNKISIEDDTTVALS-EDTAKRYEAYGWHVQVVEGGeNVSGILDALEAAKAETAR 257
Cdd:COG3959 152 QEGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSlEPLAEKWEAFGWHVIEVDGH-DIEALLAALDEAKAVKGK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2520578889 258 PSFILLRTIIGFPAPTLMNTGKAHGAALGTEEVAAVKRILG 298
Cdd:COG3959 231 PTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAELE 271
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
377-548 |
2.98e-62 |
|
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: 204.60 E-value: 2.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 377 KASGEVLNAIGDLLPELWGGSADLAESNNTTIKGAdsfGPPsaatkhwnttpyGRTLHFGVREHAMGSILNGIVLHGpTR 456
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAK---KFP------------DRFIDVGIAEQNMVGIAAGLALHG-LK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 457 PYGGTFLVFSDYMRPAVR-LAALSGLPVTYVWTHDSIGLGEDGPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVL 535
Cdd:cd07033 65 PFVSTFSFFLQRAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAAL 144
|
170
....*....|...
gi 2520578889 536 gQHEHPVGLALTR 548
Cdd:cd07033 145 -EYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
371-553 |
2.62e-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: 200.08 E-value: 2.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 371 KGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTIKGADSFgppsaatkhwntTPYGRTLHFGVREHAMGSILNGIV 450
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHP------------QGAGRVIDTGIAEQAMVGFANGMA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 451 LHGP-TRPYGGTFLVFSDYMRPAVR-LAALSGLPVTYVWTHDSIGLGEDGPTHQPVEHLAALRAIPGLVVLRPGDANETA 528
Cdd:pfam02779 69 LHGPlLPPVEATFSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETK 148
|
170 180
....*....|....*....|....*.
gi 2520578889 529 AAWR-AVLGQHEHPVGLALTRQNLPV 553
Cdd:pfam02779 149 GLLRaAIRRDGRKPVVLRLPRQLLRP 174
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
370-692 |
2.71e-37 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 141.38 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 370 AKGVATRKASGEVLNAIGDLLPELWGGSADLAESNNTTiKGADSFGppsaatkhwnttpyGRTLHFGVREHAMGSILNGI 449
Cdd:COG3958 1 MEKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLD-KFAKAFP--------------DRFFNVGIAEQNMVGVAAGL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 450 VLHGpTRPYGGTFLVFSdYMRPA--VRLA-ALSGLPVTYVWTHDSIGLGEDGPTHQPVEHLAALRAIPGLVVLRPGDANE 526
Cdd:COG3958 66 ALAG-KIPFVSTFAPFL-TGRAYeqIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 527 TAAAWRAVLgQHEHPVGLALTRQNLPVLTGTKELAREGvakGGYVLadTEGEpRVVLIGTGSELQIAVEAREVLAKDGIA 606
Cdd:COG3958 144 TEAAVRAAA-EHDGPVYLRLGRGAVPVVYDEDYEFEIG---KARVL--REGK-DVTIIATGIMVAEALEAAELLAKEGIS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 607 ARVVSIPSIEWFDAQD--QSYRDSvlppsvKARVVVEAgiaqpwHRFAGDAGEIVS----------IEH------FGASA 668
Cdd:COG3958 217 ARVINMHTIKPLDEEAilKAARKT------GAVVTAEE------HSIIGGLGSAVAevlaenypvpLRRigvpdrFGESG 284
|
330 340
....*....|....*....|....
gi 2520578889 669 DYQTLFREFGITTEAVVAAAHRSI 692
Cdd:COG3958 285 SPEELLEKYGLDAEGIVAAAKELL 308
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
433-552 |
1.06e-35 |
|
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: 131.07 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 433 LHFGVREHAMGSILNGIVLHGPtRPYGGTFLVFSDYMRPAVRLAALSGLpVTYVWTHDS-IGLGEDGPTHQPVEHLAALR 511
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2520578889 512 AIPGLVVLRPGDANETAAAWRAVLgQHEHPVGLALTRQNLP 552
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAI-RDDGPVVIRLERKSLY 135
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
569-684 |
7.55e-15 |
|
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: 71.47 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 569 GYVLADTEGePRVVLIGTGSELQIAVEAREVLAKDGIAARVVSIPSIEWFDAQD-----QSYRDSVLPPSVKARVVVEAG 643
Cdd:pfam02780 1 GKAEILREG-DDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2520578889 644 IAQPWHRFAGDAGEI----VSIEHFGASADYQTLFREFGITTEAV 684
Cdd:pfam02780 80 VAAALAEEAFDGLDApvlrVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
477-610 |
1.06e-12 |
|
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: 71.20 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 477 ALSGLPVTYVWthDSIGL-GEDGPTHQPVEHLAALRAIPGLVVLRPGDANE------TAAawravlgQHEHPVGLALTRQ 549
Cdd:COG1154 406 ALQNLPVTFAI--DRAGLvGADGPTHHGVFDLSYLRCIPNMVIMAPKDENElrhmlyTAL-------AYDGPTAIRYPRG 476
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2520578889 550 NLPVLTGTKELAREGVAKgGYVLAdtEGEpRVVLIGTGSELQIAVEAREVLAKDGIAARVV 610
Cdd:COG1154 477 NGPGVELPAELEPLPIGK-GEVLR--EGK-DVAILAFGTMVAEALEAAERLAAEGISATVV 533
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
38-252 |
1.24e-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: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 38 KVGnGHPGTAMSLAPLAYALYQRVMRhdpSDPHWIGRDRfVLSAGHSSLTQYLQLFFSGYGLEiEDIQALRTWGSKtPGH 117
Cdd:cd02017 28 GIG-GHIATFASAATLYEVGFNHFFR---ARGEGGGGDL-VYFQGHASPGIYARAFLEGRLTE-EQLDNFRQEVGG-GGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 118 PEVNHTKG----VEITTGPLGQGLASAVGMAMAAR--RERGLFDPEaapgespfDHHVFVICSDGDIEEGVTSEASSLAG 191
Cdd:cd02017 101 SSYPHPWLmpdfWEFPTVSMGLGPIQAIYQARFNRylEDRGLKDTS--------DQKVWAFLGDGEMDEPESLGAIGLAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2520578889 192 RQELGNLTVVYDDNKISIedDTTVALSEDTAKRYEAY----GWHV-QVVEGGEnvsgiLDALEAAK 252
Cdd:cd02017 173 REKLDNLIFVVNCNLQRL--DGPVRGNGKIIQELEGIfrgaGWNViKVIWGSK-----WDELLAKD 231
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
477-602 |
1.36e-08 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 58.17 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 477 ALSGLPVTYVWthDSIGL-GEDGPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNlpvLT 555
Cdd:PRK05444 368 ALQNLPVTFAI--DRAGLvGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGN---GV 442
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2520578889 556 GTKELAREGVAKG-GYVLAdtEGEpRVVLIGTGSELQIAVEAREVLAK 602
Cdd:PRK05444 443 GVELPELEPLPIGkGEVLR--EGE-DVAILAFGTMLAEALKAAERLAS 487
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
477-610 |
3.47e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 53.57 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 477 ALSGLPVTYVWthDSIGL-GEDGPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLPvlt 555
Cdd:PRK12571 408 ALQNLPVRFVL--DRAGLvGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGV--- 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2520578889 556 GTKELAREGVAKGGYVLADTEGePRVVLIGTGSELQIAVEAREVLAKDGIAARVV 610
Cdd:PRK12571 483 GVEIPAEGTILGIGKGRVPREG-PDVAILSVGAHLHECLDAADLLEAEGISVTVA 536
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
129-265 |
1.48e-06 |
|
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: 48.79 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 129 TTGPLGQGLASAVGMAMAARrerglfdpeaapgespfDHHVFVICSDGDIEEGVtSEASSLAgrQELGNLTVVYDDNKIS 208
Cdd:cd00568 44 GFGAMGYGLPAAIGAALAAP-----------------DRPVVCIAGDGGFMMTG-QELATAV--RYGLPVIVVVFNNGGY 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2520578889 209 IE-----------DDTTVALSE-DTAKRYEAYGWHVQVVEGGEnvsGILDALEAAKAETaRPSFILLRT 265
Cdd:cd00568 104 GTirmhqeafyggRVSGTDLSNpDFAALAEAYGAKGVRVEDPE---DLEAALAEALAAG-GPALIEVKT 168
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
561-614 |
2.64e-05 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 47.62 E-value: 2.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2520578889 561 AREGVAKGGYVLADTEGEPRVVLIGTGSELQIAVEAREVLAKD-GIAARVVSIPS 614
Cdd:PRK13012 715 AEEGILKGMYRLAAAAEAPRVQLLGSGAILREVLAAARLLADDwGVDADVWSVTS 769
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
477-621 |
1.39e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 45.00 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 477 ALSGLPVTYVWTHDSIGlGEDgPTHQPVEHLAALRAIPGLVVLRPGDANETAAAWRAVLGQHEHPVGLALTRQNLP---- 552
Cdd:PRK12315 367 AINNNPAVMIVFGGSIS-GND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEHPVAIRVPEHGVEsgpt 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 553 VLTGTKELAREGVAKGgyvladtegePRVVLIGTGSELQIAVEAREVLAKD-GIAARVVSIPSIEWFDAQ 621
Cdd:PRK12315 445 VDTDYSTLKYEVTKAG----------EKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEE 504
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
478-609 |
2.28e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 44.51 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 478 LSGLPVTYvwTHDSIGL-GEDGPTHQPVEHLAALRAIPGLVVLRPGDANE------TAAAWRAVLGQHEHPVGLALTRQn 550
Cdd:PLN02582 446 LQKLPVRF--AMDRAGLvGADGPTHCGAFDVTYMACLPNMVVMAPSDEAElfhmvaTAAAIDDRPSCFRYPRGNGIGVQ- 522
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2520578889 551 LPvlTGTKELAREgVAKGGYVLadtEGEpRVVLIGTGSELQIAVEAREVLAKDGIAARV 609
Cdd:PLN02582 523 LP--PNNKGIPIE-VGKGRILL---EGE-RVALLGYGTAVQSCLAAASLLERHGLSATV 574
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
74-268 |
8.25e-04 |
|
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: 40.99 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 74 RDRFVLSAGHSS-----LTQYLQLFFSgygleiediqaLRTWGSKTpGHPEVNHTKGVEITTGPLGQGLASAVGMAMAAR 148
Cdd:cd02007 25 KDKIIWDVGHQAyphkiLTGRRDQFHT-----------LRQYGGLS-GFTKRSESEYDAFGTGHSSTSISAALGMAVARD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 149 RErglfdpeaapGEspfDHHVFVICSDGDIEEGVTSEASSLAGRQeLGNLTVVYDDNKISIeddttvalSEDTAKR---Y 225
Cdd:cd02007 93 LK----------GK---KRKVIAVIGDGALTGGMAFEALNNAGYL-KSNMIVILNDNEMSI--------SPNVGTPgnlF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2520578889 226 EAYGWHVQVVEGGENVSGILDALEAAKaETARPSFILLRTIIG 268
Cdd:cd02007 151 EELGFRYIGPVDGHNIEALIKVLKEVK-DLKGPVLLHVVTKKG 192
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
431-609 |
1.28e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 42.01 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 431 RTLHFGVREHAMGSILNGIVLHGpTRPYggtFLVFSDYMRPA----VRLAALSGLPVTYVWthDSIGL-GEDGPTHQPVE 505
Cdd:PLN02234 400 RCFDVGIAEQHAVTFAAGLACEG-LKPF---CTIYSSFMQRAydqvVHDVDLQKLPVRFAI--DRAGLmGADGPTHCGAF 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 506 HLAALRAIPGLVVLRPGDANE------TAAAW--RAVLGQHEHPVGLALT----RQNLPVLTGTKELAREGvakggyvla 573
Cdd:PLN02234 474 DVTFMACLPNMIVMAPSDEAElfnmvaTAAAIddRPSCFRYHRGNGIGVSlppgNKGVPLQIGRGRILRDG--------- 544
|
170 180 190
....*....|....*....|....*....|....*.
gi 2520578889 574 dtegePRVVLIGTGSELQIAVEAREVLAKDGIAARV 609
Cdd:PLN02234 545 -----ERVALLGYGSAVQRCLEAASMLSERGLKITV 575
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
130-265 |
6.57e-03 |
|
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: 39.02 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520578889 130 TGPLGQGLASAVGMAMAARRERglfDPEAApgespfdhhvFVICSDGDIEEGVTSEASSLAGRQELGNLTVVYdDNKISI 209
Cdd:cd02000 103 NGIVGGQVPLAAGAALALKYRG---EDRVA----------VCFFGDGATNEGDFHEALNFAALWKLPVIFVCE-NNGYAI 168
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2520578889 210 EDDTTVALSEDT-AKRYEAYGWHVQVVEGGEnvsgILDALEAAK--AETAR----PSFILLRT 265
Cdd:cd02000 169 STPTSRQTAGTSiADRAAAYGIPGIRVDGND----VLAVYEAAKeaVERARagggPTLIEAVT 227
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