|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
4-664 |
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: 1095.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 4 TDLDQLAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGY 83
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 84 DVTMDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAME 163
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 164 GIASEAASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGdNDLEGIEAAIHEAKKVTDKPT 243
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDG-HDLEAIDAAIEAAKAETDKPT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 244 VIRLTTTIGFGS-KLQGTGGVHGNPLKADDCESVKQKFGFDPKQsFVVPQQVYDLYHKHAAEGAAKEQAWNQLLEKYATE 322
Cdd:COG0021 240 LIICKTIIGYGSpNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 323 YKAEHADLVRRLSGKLPEGWEKSLPTYKPTDAAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDFQPPEY 402
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 403 gigewSGRYIRYGVREHAMAAVMNGLAAYGTIIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQP 482
Cdd:COG0021 399 -----SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 483 IETLAHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENS--TIEAALKGAYPVVEAP-NAAITLI 559
Cdd:COG0021 474 VEQLASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTaaAAEGVAKGAYVLADAEgTPDVILI 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 560 STGSEVSICIEAATYLKEKhNIVARVVSVPCFEVFDAQPKDYRLKVLPDGI-PVLSVEALSTMGWERY---SHEQFGLNR 635
Cdd:COG0021 554 ATGSEVSLAVEAAELLAAE-GIKVRVVSMPSWELFEAQDAAYRESVLPPAVrARVAVEAGVTDGWYKYvglDGAVIGIDT 632
|
650 660
....*....|....*....|....*....
gi 2115080454 636 FGASGPYKEVYKKFEFTPEGISKRALATI 664
Cdd:COG0021 633 FGASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
5-667 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 997.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 5 DLDQLAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYD 84
Cdd:PTZ00089 4 AIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 85 VTMDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAMEG 164
Cdd:PTZ00089 84 LSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCLQEG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 165 IASEAASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGDNDLEGIEAAIHEAKKVTDKPTV 244
Cdd:PTZ00089 164 VSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNTDFDGLRKAIEEAKKSKGKPKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 245 IRLTTTIGFGSKLQGTGGVHGNPLKADDCESVKQKFGFDPKQSFVVPQQVYDLYHKHAAEGAAKEQAWNQLLEKYATEYK 324
Cdd:PTZ00089 244 IIVKTTIGYGSSKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYTAAFP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 325 AEHADLVRRLSGKLPEGWEKSLPTYKPTDAAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDFQPPEYgi 404
Cdd:PTZ00089 324 KEAQAIERRFKGELPPGWEKKLPKYTTNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTKASP-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 405 gewSGRYIRYGVREHAMAAVMNGLAAYGTIIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQPIE 484
Cdd:PTZ00089 402 ---EGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 485 TLAHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENSTIEAALKGAYPVVEAPNA-AITLISTGS 563
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFTNSpQLILVASGS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 564 EVSICIEAATYLKEKHNIvaRVVSVPCFEVFDAQPKDYRLKVLP-DGIPVLSVEALSTMGWERYSHEQFGLNRFGASGPY 642
Cdd:PTZ00089 559 EVSLCVEAAKALSKELNV--RVVSMPCWELFDQQSEEYQQSVLPsGGVPVLSVEAYVSFGWEKYSHVHVGISGFGASAPA 636
|
650 660
....*....|....*....|....*
gi 2115080454 643 KEVYKKFEFTPEGISKRALATIDFY 667
Cdd:PTZ00089 637 NALYKHFGFTVENVVEKARALAARF 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
9-664 |
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: 962.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 9 LAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYDVTMD 88
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 89 DLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAMEGIASE 168
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 169 AASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGdNDLEGIEAAIHEAKKVTDKPTVIRLT 248
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDG-HDLAAIDAAIEEAKASTDKPTLIEVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 249 TTIGFGSK-LQGTGGVHGNPLKADDCESVKQKFGFDPKQsFVVPQQVYDLYHKHAAE-GAAKEQAWNQLLEKYATEYKAE 326
Cdd:TIGR00232 241 TTIGFGSPnKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFKKTVKErGAKAEQEWNELFAAYKKKYPEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 327 HADLVRRLSGKLPEGWEKSLPTYKPTDAAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDfqPPEYGige 406
Cdd:TIGR00232 320 AAEFTRRLSGELPADWDKQLPEFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGD--LHENP--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 407 wSGRYIRYGVREHAMAAVMNGLAAYGTIIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQPIETL 486
Cdd:TIGR00232 395 -LGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 487 AHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENSTIEAALKGAYPVVEAPNAAITLISTGSEVS 566
Cdd:TIGR00232 474 ASLRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 567 ICIEAATYLkEKHNIVARVVSVPCFEVFDAQPKDYRLKVLPDGIPVLSVEALSTMGWERYSH---EQFGLNRFGASGPYK 643
Cdd:TIGR00232 554 LAVEAAKKL-AAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVTRLAIEAGAADEWYKYAGlvgAILGMDSFGESAPGD 632
|
650 660
....*....|....*....|.
gi 2115080454 644 EVYKKFEFTPEGISKRALATI 664
Cdd:TIGR00232 633 KLFEEFGFTVENVVAKAKKLL 653
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
7-339 |
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: 551.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 7 DQLAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYDVT 86
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 87 MDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAMEGIA 166
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 167 SEAASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGDnDLEGIEAAIHEAKKVTDKPTVIR 246
Cdd:pfam00456 162 SEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGH-DVEAIAAAIEEAKAEKDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 247 LTTTIGFGSKL-QGTGGVHGNPLKADDCESVKQKFGFDPKQSFVVPQQVYDLYHKHAAEGAAKEQAWNQLLEKYATEYKA 325
Cdd:pfam00456 241 CRTVIGYGSPNkQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 2115080454 326 EHADLVRRLSGKLP 339
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
12-277 |
3.07e-142 |
|
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: 415.36 E-value: 3.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 12 NTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYDvTMDDLK 91
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 92 NFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHtaavfnkpgyDLINNYTYCFFGDGCAMEGIASEAAS 171
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKL----------LGFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 172 MAGHLKLGNLIAIYDDNHISIDGDTK-CAFTEDVMKRFEAYGWHTVWVKdgDNDLEGIEAAIHEAKKVTDKPTVIRLTTT 250
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEVD--GHDVEEILAALEEAKKSKGKPTLIIAKTI 227
|
250 260
....*....|....*....|....*...
gi 2115080454 251 IGFGSK-LQGTGGVHGNPLKADDCESVK 277
Cdd:cd02012 228 KGKGVPfMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
412-531 |
1.68e-33 |
|
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: 124.91 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 412 IRYGVREHAMAAVMNGLAAYGTIiPAGGTFLNFVSYAAGALRLSALSRvRVIHIATHDS-IGLGEDGPTHQPIETLAHFR 490
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLR-PVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2115080454 491 ALPNCMVWRPADGNETSAAYYSAITAKHtPSVLALTRQNLP 531
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDDG-PVVIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
4-664 |
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: 1095.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 4 TDLDQLAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGY 83
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 84 DVTMDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAME 163
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 164 GIASEAASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGdNDLEGIEAAIHEAKKVTDKPT 243
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDG-HDLEAIDAAIEAAKAETDKPT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 244 VIRLTTTIGFGS-KLQGTGGVHGNPLKADDCESVKQKFGFDPKQsFVVPQQVYDLYHKHAAEGAAKEQAWNQLLEKYATE 322
Cdd:COG0021 240 LIICKTIIGYGSpNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 323 YKAEHADLVRRLSGKLPEGWEKSLPTYKPTDAAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDFQPPEY 402
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 403 gigewSGRYIRYGVREHAMAAVMNGLAAYGTIIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQP 482
Cdd:COG0021 399 -----SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 483 IETLAHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENS--TIEAALKGAYPVVEAP-NAAITLI 559
Cdd:COG0021 474 VEQLASLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTaaAAEGVAKGAYVLADAEgTPDVILI 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 560 STGSEVSICIEAATYLKEKhNIVARVVSVPCFEVFDAQPKDYRLKVLPDGI-PVLSVEALSTMGWERY---SHEQFGLNR 635
Cdd:COG0021 554 ATGSEVSLAVEAAELLAAE-GIKVRVVSMPSWELFEAQDAAYRESVLPPAVrARVAVEAGVTDGWYKYvglDGAVIGIDT 632
|
650 660
....*....|....*....|....*....
gi 2115080454 636 FGASGPYKEVYKKFEFTPEGISKRALATI 664
Cdd:COG0021 633 FGASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
5-667 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 997.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 5 DLDQLAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYD 84
Cdd:PTZ00089 4 AIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 85 VTMDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAMEG 164
Cdd:PTZ00089 84 LSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCLQEG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 165 IASEAASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGDNDLEGIEAAIHEAKKVTDKPTV 244
Cdd:PTZ00089 164 VSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNTDFDGLRKAIEEAKKSKGKPKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 245 IRLTTTIGFGSKLQGTGGVHGNPLKADDCESVKQKFGFDPKQSFVVPQQVYDLYHKHAAEGAAKEQAWNQLLEKYATEYK 324
Cdd:PTZ00089 244 IIVKTTIGYGSSKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYTAAFP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 325 AEHADLVRRLSGKLPEGWEKSLPTYKPTDAAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDFQPPEYgi 404
Cdd:PTZ00089 324 KEAQAIERRFKGELPPGWEKKLPKYTTNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTKASP-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 405 gewSGRYIRYGVREHAMAAVMNGLAAYGTIIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQPIE 484
Cdd:PTZ00089 402 ---EGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 485 TLAHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENSTIEAALKGAYPVVEAPNA-AITLISTGS 563
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFTNSpQLILVASGS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 564 EVSICIEAATYLKEKHNIvaRVVSVPCFEVFDAQPKDYRLKVLP-DGIPVLSVEALSTMGWERYSHEQFGLNRFGASGPY 642
Cdd:PTZ00089 559 EVSLCVEAAKALSKELNV--RVVSMPCWELFDQQSEEYQQSVLPsGGVPVLSVEAYVSFGWEKYSHVHVGISGFGASAPA 636
|
650 660
....*....|....*....|....*
gi 2115080454 643 KEVYKKFEFTPEGISKRALATIDFY 667
Cdd:PTZ00089 637 NALYKHFGFTVENVVEKARALAARF 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
9-664 |
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: 962.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 9 LAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYDVTMD 88
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 89 DLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAMEGIASE 168
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 169 AASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGdNDLEGIEAAIHEAKKVTDKPTVIRLT 248
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDG-HDLAAIDAAIEEAKASTDKPTLIEVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 249 TTIGFGSK-LQGTGGVHGNPLKADDCESVKQKFGFDPKQsFVVPQQVYDLYHKHAAE-GAAKEQAWNQLLEKYATEYKAE 326
Cdd:TIGR00232 241 TTIGFGSPnKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFKKTVKErGAKAEQEWNELFAAYKKKYPEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 327 HADLVRRLSGKLPEGWEKSLPTYKPTDAAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDfqPPEYGige 406
Cdd:TIGR00232 320 AAEFTRRLSGELPADWDKQLPEFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGD--LHENP--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 407 wSGRYIRYGVREHAMAAVMNGLAAYGTIIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQPIETL 486
Cdd:TIGR00232 395 -LGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 487 AHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENSTIEAALKGAYPVVEAPNAAITLISTGSEVS 566
Cdd:TIGR00232 474 ASLRAIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQ 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 567 ICIEAATYLkEKHNIVARVVSVPCFEVFDAQPKDYRLKVLPDGIPVLSVEALSTMGWERYSH---EQFGLNRFGASGPYK 643
Cdd:TIGR00232 554 LAVEAAKKL-AAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVTRLAIEAGAADEWYKYAGlvgAILGMDSFGESAPGD 632
|
650 660
....*....|....*....|.
gi 2115080454 644 EVYKKFEFTPEGISKRALATI 664
Cdd:TIGR00232 633 KLFEEFGFTVENVVAKAKKLL 653
|
|
| PLN02790 |
PLN02790 |
transketolase |
14-660 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 958.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 14 IRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYD-VTMDDLKN 92
Cdd:PLN02790 1 IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 93 FRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAMEGIASEAASM 172
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 173 AGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGDNDLEGIEAAIHEAKKVTDKPTVIRLTTTIG 252
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNTDYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 253 FGS-KLQGTGGVHGNPLKADDCESVKQKFGFdPKQSFVVPQQVYDLYHKHAAEGAAKEQAWNQLLEKYATEYKAEHADLV 331
Cdd:PLN02790 241 YGSpNKANSYSVHGAALGEKEVDATRKNLGW-PYEPFHVPEDVKSHWSKHTKEGAALEAEWNAKFAEYKKKYPEEAAELK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 332 RRLSGKLPEGWEKSLPTYKPTDAAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDFQPPEYGigewsGRY 411
Cdd:PLN02790 320 SLISGELPSGWEKALPTFTPEDPADATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPE-----ERN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 412 IRYGVREHAMAAVMNGLAAYGT-IIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQPIETLAHFR 490
Cdd:PLN02790 395 VRFGVREHGMGAICNGIALHSSgLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 491 ALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENSTIEAALKGAYPVVEAPNAA---ITLISTGSEVSI 567
Cdd:PLN02790 475 AMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTSIEGVEKGGYVISDNSSGNkpdLILIGTGSELEI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 568 CIEAATYLkEKHNIVARVVSVPCFEVFDAQPKDYRLKVLPDGIPV-LSVEALSTMGWERYS---HEQFGLNRFGASGPYK 643
Cdd:PLN02790 555 AAKAAKEL-RKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTArVSVEAGSTFGWEKYVgskGKVIGVDRFGASAPAG 633
|
650
....*....|....*..
gi 2115080454 644 EVYKKFEFTPEGISKRA 660
Cdd:PLN02790 634 ILYKEFGFTVENVVAAA 650
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
4-664 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 862.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 4 TDLDQLAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGY 83
Cdd:PRK05899 5 MELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 84 DVTMDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAME 163
Cdd:PRK05899 85 DLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDLME 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 164 GIASEAASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVkDGdNDLEGIEAAIHEAKKVTdKPT 243
Cdd:PRK05899 165 GISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DG-HDVEAIDAAIEEAKAST-KPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 244 VIRLTTTIGFGS-KLQGTGGVHGNPLKADDCESVKQKFGFDPkqsfvvpqqvydlyhkhaaegaakeqawnqllekyate 322
Cdd:PRK05899 242 LIIAKTIIGKGApNKEGTHKVHGAPLGAEEIAAAKKELGWDY-------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 323 ykaehadlvrrlsgklpegwekslptykptdaavasRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDFQPPEY 402
Cdd:PRK05899 284 ------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 403 gigewSGRYIRYGVREHAMAAVMNGLAAYGTIIPAGGTFLNFVSYAAGALRLSALSRVRVIHIATHDSIGLGEDGPTHQP 482
Cdd:PRK05899 328 -----SGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQP 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 483 IETLAHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLEN-STIEAALKGAYPVVEAPnaAITLIST 561
Cdd:PRK05899 403 VEQLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERtAQEEGVAKGGYVLRDDP--DVILIAT 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 562 GSEVSICIEAATYLKEKhNIVARVVSVPCFEVFDAQPKDYRLKVLPDGIPV-LSVEALSTMGWERY---SHEQFGLNRFG 637
Cdd:PRK05899 481 GSEVHLALEAADELEAE-GIKVRVVSMPSTELFDEQDAAYKESVLPAAVTArVAVEAGVADGWYKYvglDGKVLGIDTFG 559
|
650 660
....*....|....*....|....*..
gi 2115080454 638 ASGPYKEVYKKFEFTPEGISKRALATI 664
Cdd:PRK05899 560 ASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
7-339 |
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: 551.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 7 DQLAINTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYDVT 86
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 87 MDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDLINNYTYCFFGDGCAMEGIA 166
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 167 SEAASMAGHLKLGNLIAIYDDNHISIDGDTKCAFTEDVMKRFEAYGWHTVWVKDGDnDLEGIEAAIHEAKKVTDKPTVIR 246
Cdd:pfam00456 162 SEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGH-DVEAIAAAIEEAKAEKDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 247 LTTTIGFGSKL-QGTGGVHGNPLKADDCESVKQKFGFDPKQSFVVPQQVYDLYHKHAAEGAAKEQAWNQLLEKYATEYKA 325
Cdd:pfam00456 241 CRTVIGYGSPNkQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 2115080454 326 EHADLVRRLSGKLP 339
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
12-277 |
3.07e-142 |
|
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: 415.36 E-value: 3.07e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 12 NTIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFGYDvTMDDLK 91
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 92 NFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAHtaavfnkpgyDLINNYTYCFFGDGCAMEGIASEAAS 171
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKL----------LGFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 172 MAGHLKLGNLIAIYDDNHISIDGDTK-CAFTEDVMKRFEAYGWHTVWVKdgDNDLEGIEAAIHEAKKVTDKPTVIRLTTT 250
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEVD--GHDVEEILAALEEAKKSKGKPTLIIAKTI 227
|
250 260
....*....|....*....|....*...
gi 2115080454 251 IGFGSK-LQGTGGVHGNPLKADDCESVK 277
Cdd:cd02012 228 KGKGVPfMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
3-274 |
1.33e-82 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 262.32 E-value: 1.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 3 YTDLDQLAINtIRLLAVDATFKANSGHPGAPMGMAPVAHVLFNKFMNFNPKNPNWLNRDRFVLSNGHGCMLQYALLHLFG 82
Cdd:COG3959 5 IKELEEKARQ-IRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 83 YdVTMDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAqahtAAVFNKPgydlinNYTYCFFGDGCAM 162
Cdd:COG3959 84 Y-FPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALA----AKLDGKD------YRVYVLLGDGELQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 163 EGIASEAASMAGHLKLGNLIAIYDDNHISIDGdtkcaFTEDVM------KRFEAYGWHTVWVkDGdNDLEGIEAAIHEAK 236
Cdd:COG3959 153 EGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDG-----PTEDVMsleplaEKWEAFGWHVIEV-DG-HDIEALLAALDEAK 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 2115080454 237 KVTDKPTVIRLTTTIGFG-SKLQGTGGVHGNPLKADDCE 274
Cdd:COG3959 226 AVKGKPTVIIAHTVKGKGvSFMENRPKWHGKAPNDEELE 264
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
354-532 |
1.13e-56 |
|
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: 190.07 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 354 AAVASRKLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAVDFQPPeygigewsGRYIRYGVREHAMAAVMNGLAAYG- 432
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQGA--------GRVIDTGIAEQAMVGFANGMALHGp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 433 TIIPAGGTFLNFVSYAAGALR-LSALSRVRVIHIATHDSIGLGEDGPTHQPIETLAHFRALPNCMVWRPADGNETSAAYY 511
Cdd:pfam02779 73 LLPPVEATFSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLR 152
|
170 180
....*....|....*....|..
gi 2115080454 512 SAITAKH-TPSVLALTRQNLPQ 532
Cdd:pfam02779 153 AAIRRDGrKPVVLRLPRQLLRP 174
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
360-527 |
8.44e-55 |
|
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: 184.18 E-value: 8.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 360 KLSEAVLEKIHAVVPELMSGSADLTGSNNTRWKNAvdfqppeygigEWSGRYIRYGVREHAMAAVMNGLAAYGtIIPAGG 439
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAK-----------KFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 440 TFLNFVSYAAGALR-LSALSRVRVIHIATHDSIGLGEDGPTHQPIETLAHFRALPNCMVWRPADGNETSAAYYSAITAKH 518
Cdd:cd07033 69 TFSFFLQRAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDG 148
|
....*....
gi 2115080454 519 tPSVLALTR 527
Cdd:cd07033 149 -PVYIRLPR 156
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
412-531 |
1.68e-33 |
|
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: 124.91 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 412 IRYGVREHAMAAVMNGLAAYGTIiPAGGTFLNFVSYAAGALRLSALSRvRVIHIATHDS-IGLGEDGPTHQPIETLAHFR 490
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLR-PVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2115080454 491 ALPNCMVWRPADGNETSAAYYSAITAKHtPSVLALTRQNLP 531
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDDG-PVVIRLERKSLY 135
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
380-664 |
1.29e-27 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 113.64 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 380 SADLTGSNNTrwknaVDFQPpeygigEWSGRYIRYGVREHAMAAVMNGLAAYGtIIPAGGTFLNFVSY-AAGALRLS-AL 457
Cdd:COG3958 28 DADLGGSTKL-----DKFAK------AFPDRFFNVGIAEQNMVGVAAGLALAG-KIPFVSTFAPFLTGrAYEQIRNDiAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 458 SRVRVIHIATHDSIGLGEDGPTHQPIETLAHFRALPNCMVWRPADGNETSAAYYSAITAKHtPSVLALTRQNLPQLENST 537
Cdd:COG3958 96 PNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDG-PVYLRLGRGAVPVVYDED 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 538 IEAALKGAYPVVEapNAAITLISTGSEVSICIEAATYLkEKHNIVARVVSVPCFEVFDaqpKDYRLKVLPDGIPVLSVE- 616
Cdd:COG3958 175 YEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELL-AKEGISARVINMHTIKPLD---EEAILKAARKTGAVVTAEe 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2115080454 617 -------------ALStmgwERYSH--EQFGLN-RFGASGPYKEVYKKFEFTPEGISKRALATI 664
Cdd:COG3958 249 hsiigglgsavaeVLA----ENYPVplRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
548-656 |
2.14e-12 |
|
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: 64.54 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 548 VVEAPNAAITLISTGSEVSICIEAATYLkEKHNIVARVVSVPCFEVFDAQP------KDYRLKVLPDGIPVLSVEA-LST 620
Cdd:pfam02780 4 EILREGDDVTIVAYGSMVEEALEAAELL-AKEGISAEVVDLRTIKPLDKETilesvkKTGRLVTVEEAVPRGGFGSeVAA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2115080454 621 MGWERYSHE------QFGLNRFGASGPYKEVYKKFEFTPEGI 656
Cdd:pfam02780 83 ALAEEAFDGldapvlRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
14-281 |
2.21e-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: 63.09 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 14 IRLLAVDATFKANS------GHPGAPMGMAPVAHVLFNKFmnFNPKNpNWLNRDRfVLSNGHGCMLQYALLHLFGyDVTM 87
Cdd:cd02017 11 IRWNAMAMVHRANKkdlgigGHIATFASAATLYEVGFNHF--FRARG-EGGGGDL-VYFQGHASPGIYARAFLEG-RLTE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 88 DDLKNFRQL--DSITPGHPEAHDTPG-VEVTTGPLGQGFANAVGLAIAQAHTAAVFNKPGYDlinNYTYCFFGDGCAMEG 164
Cdd:cd02017 86 EQLDNFRQEvgGGGLSSYPHPWLMPDfWEFPTVSMGLGPIQAIYQARFNRYLEDRGLKDTSD---QKVWAFLGDGEMDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 165 IASEAASMAGHLKLGNLIAIYDDNHISIDG----DTKCAftEDVMKRFEAYGWHTVWVK--------------------- 219
Cdd:cd02017 163 ESLGAIGLAAREKLDNLIFVVNCNLQRLDGpvrgNGKII--QELEGIFRGAGWNVIKVIwgskwdellakdgggalrqrm 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 220 ----DGD------------------------------------------NDLEGIEAAIHEAKKVTDKPTVIRLTTTIGF 253
Cdd:cd02017 241 eetvDGDyqtlkakdgayvrehffgkypelkalvtdlsdedlwalnrggHDPRKVYAAYKKAVEHKGKPTVILAKTIKGY 320
|
330 340 350
....*....|....*....|....*....|.
gi 2115080454 254 GSKLQGTGGVHGNPLKADDCESVK---QKFG 281
Cdd:cd02017 321 GLGAAGEGRNHAHQVKKMTEDELKalrDRFG 351
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
103-249 |
3.31e-09 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 56.49 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 103 HPEAHDTPGVEVTTGPLGQGFANAVGLAIAQAhtaavfNKPgydlinnyTYCFFGDGCAMEGIAsEAASMAGHlkLGNLI 182
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP------DRP--------VVCIAGDGGFMMTGQ-ELATAVRY--GLPVI 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2115080454 183 AIYDDN--HISIDGDTKCAFTE----------DVMKRFEAYGWHTVWVkdgdNDLEGIEAAIHEAKKvTDKPTVIRLTT 249
Cdd:cd00568 95 VVVFNNggYGTIRMHQEAFYGGrvsgtdlsnpDFAALAEAYGAKGVRV----EDPEDLEAALAEALA-AGGPALIEVKT 168
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
69-249 |
2.95e-08 |
|
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: 55.58 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 69 HGCMLQYALLHLFGydvTMDDLKNFRQLdSITPGHPEAHDTPGvevtTGPLGQGFANAVGLAIAQAhtaavfnkpgYDLI 148
Cdd:cd02000 64 RGVDLKEMLAELFG---KETGPCKGRGG-SMHIGDKEKNFFGG----NGIVGGQVPLAAGAALALK----------YRGE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 149 NNYTYCFFGDGCAMEGIASEAASMAGHLKLgNLIAIYDDNHISIDGDTKCAF-TEDVMKRFEAYGWHTVWVkDGdNDLEG 227
Cdd:cd02000 126 DRVAVCFFGDGATNEGDFHEALNFAALWKL-PVIFVCENNGYAISTPTSRQTaGTSIADRAAAYGIPGIRV-DG-NDVLA 202
|
170 180
....*....|....*....|....*
gi 2115080454 228 IEAAIHEAKK---VTDKPTVIRLTT 249
Cdd:cd02000 203 VYEAAKEAVErarAGGGPTLIEAVT 227
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
124-254 |
9.33e-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: 52.93 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 124 ANAVGLAIAQAHTAAvfnkpgydliNNYTYCFFGDGCAMEGIASEAASMAGHLKlGNLIAIYDDNHISIDGDTKCAFTed 203
Cdd:cd02007 82 SAALGMAVARDLKGK----------KRKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSISPNVGTPGN-- 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2115080454 204 vmkRFEAYGWHTVWVKDGdNDLEGIEAAIHEAKKvTDKPTVIRLTTTIGFG 254
Cdd:cd02007 149 ---LFEELGFRYIGPVDG-HNIEALIKVLKEVKD-LKGPVLLHVVTKKGKG 194
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
126-664 |
2.13e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 50.85 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 126 AVGLAIAQA-------HTAAVfnkpgydlInnytycffGDGcAME-GIASEAASMAGHLKlGNLIAIYDDNHISIDgdtk 197
Cdd:PRK05444 126 ALGMAKARDlkggedrKVVAV--------I--------GDG-ALTgGMAFEALNNAGDLK-SDLIVILNDNEMSIS---- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 198 caftEDV--MKR----------FEAYGWHTVWVKDGdNDLEGIEAAIHEAKKvTDKPTVIRLTTTigfgsklqgtggvhg 265
Cdd:PRK05444 184 ----PNVgaLSNylarlrsstlFEELGFNYIGPIDG-HDLDALIETLKNAKD-LKGPVLLHVVTK--------------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 266 nplkaddcesvKQKfGFDPkqsfvvpqqvydlyhkhaAEGAAkeqawnqllEKYateykaeHA----DLVrrlSGKLPEG 341
Cdd:PRK05444 243 -----------KGK-GYAP------------------AEADP---------IKY-------HGvgkfDPE---TGEQPKS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 342 WEKSLPTYkpTDaaVASRKLSE--AVLEKIHAVVPELMSGSaDLtgsnntrwknaVDFQ---PPEY---GIGEwsgryir 413
Cdd:PRK05444 274 SKPGKPSY--TK--VFGETLCElaEKDPKIVAITAAMPEGT-GL-----------VKFSkrfPDRYfdvGIAE------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 414 ygvrEHA--MAAvmnGLAAygtiipAGG--------TFLNfvsyaagalrlsalsrvR----VIH-IATH--------DS 470
Cdd:PRK05444 331 ----QHAvtFAA---GLAT------EGLkpvvaiysTFLQ-----------------RaydqVIHdVALQnlpvtfaiDR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 471 IGL-GEDGPTHQPIETLAHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQNLPQLENSTIEAALKGAYPVV 549
Cdd:PRK05444 381 AGLvGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNGVGVELPELEPLPIGKGEVL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 550 eAPNAAITLISTGSEVSICIEAATYLKEkhnivARVVSvPCF------EVFDAQPKDYRLKV-LPDGI-------PVLsv 615
Cdd:PRK05444 461 -REGEDVAILAFGTMLAEALKAAERLAS-----ATVVD-ARFvkpldeELLLELAAKHDLVVtVEEGAimggfgsAVL-- 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2115080454 616 EALSTMGWERYSHeQFGL-NRFGASGPYKEVYKKFEFTPEGISKRALATI 664
Cdd:PRK05444 532 EFLADHGLDVPVL-NLGLpDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
157-256 |
1.53e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 48.08 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 157 GDGCAMEGIASEAASMAGHLKlGNLIAIYDDNHISID-----------------GDTKCAFtedvmkrFEAYGWHTVWVK 219
Cdd:PRK12315 143 GDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAenhgglyknlkelrdtnGQSENNL-------FKAMGLDYRYVE 214
|
90 100 110
....*....|....*....|....*....|....*..
gi 2115080454 220 DGdNDLEGIEAAIHEAKKVtDKPTVIRLTTTIGFGSK 256
Cdd:PRK12315 215 DG-NDIESLIEAFKEVKDI-DHPIVLHIHTLKGKGYQ 249
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
97-250 |
2.42e-04 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 43.98 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 97 DSITPGHPEAHDTPGvevtTGPLGQGFANAVGLAIAQAhtaavfnkpgYDLINNYTYCFFGDGCAMEGIASEAASMAGHL 176
Cdd:COG1071 111 GSMHFFDKELNFLGG----SGIVGGQLPHAVGAALAAK----------LRGEDEVAVAFFGDGATSEGDFHEALNFAAVW 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 177 KLGNLIAIYdDNH--IS--IDGDTKCaftEDVMKRFEAYGWHTVWVkDGdNDLEGIEAAIHEAKKV---TDKPTVIRLTT 249
Cdd:COG1071 177 KLPVVFVCE-NNGyaIStpVERQTAV---ETIADRAAGYGIPGVRV-DG-NDVLAVYAAVKEAVERaraGEGPTLIEAKT 250
|
.
gi 2115080454 250 T 250
Cdd:COG1071 251 Y 251
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
2-254 |
7.70e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 42.79 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 2 GYTDLDQLAINTIRLLAVD------ATFKANSGHPGAPMGMAP--VA-HVLFNkfmnfnpkNPnwlnRDRFVLSNGHGCm 72
Cdd:PRK12571 14 GPADLRALSDAELEQLADElraeviSAVSETGGHLGSSLGVVEltVAlHAVFN--------TP----KDKLVWDVGHQC- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 73 lqYALLHLFGydvTMDDLKNFRQLDSITpGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQA------HTAAVFnkpgyd 146
Cdd:PRK12571 81 --YPHKILTG---RRDRFRTLRQKGGLS-GFTKRSESEYDPFGAAHSSTSISAALGFAKARAlgqpdgDVVAVI------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 147 linnytycffGDGCAMEGIASEAASMAGHLKlGNLIAIYDDNHISID---------------GDTKCAF---TEDVMKR- 207
Cdd:PRK12571 149 ----------GDGSLTAGMAYEALNNAGAAD-RRLIVILNDNEMSIAppvgalaaylstlrsSDPFARLraiAKGVEERl 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2115080454 208 ------------------------FEAYGWHTVWVKDGdNDLEGIEAAIHEAKKVTDKPTVIRLTTTIGFG 254
Cdd:PRK12571 218 pgplrdgarrarelvtgmigggtlFEELGFTYVGPIDG-HDMEALLSVLRAARARADGPVLVHVVTEKGRG 287
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
472-586 |
1.05e-03 |
|
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: 42.31 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 472 GL-GEDGPTHQPIETLAHFRALPNCMVWRPADGNETSAAYYSAITAKHtPSVLALTRQNLPQLEnstIEAALKgAYPV-- 548
Cdd:COG1154 420 GLvGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDG-PTAIRYPRGNGPGVE---LPAELE-PLPIgk 494
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2115080454 549 --VEAPNAAITLISTGSEVSICIEAATYLKEkHNIVARVV 586
Cdd:COG1154 495 geVLREGKDVAILAFGTMVAEALEAAERLAA-EGISATVV 533
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
109-249 |
1.79e-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: 40.77 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 109 TPGVEVTT--GPLGQGFANAVGLAIAQAhtaavfnkpgYDLINNYTYCFFGDGCAMEGIASEAASMAGHLKLgNLIAIYD 186
Cdd:pfam00676 91 AKGNRFYGgnGILGAQVPLGAGIALAAK----------YRGKKEVAITLYGDGAANQGDFFEGLNFAALWKL-PVIFVCE 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2115080454 187 DNHISIDGDT-KCAFTEDVMKRFEAYGWHTVWVkDGdNDLEGIEAAIHEAKKVT---DKPTVIRLTT 249
Cdd:pfam00676 160 NNQYGISTPAeRASASTTYADRARGYGIPGLHV-DG-MDPLAVYQASKFAAERArtgKGPFLIELVT 224
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
6-254 |
4.08e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 40.47 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 6 LDQLAINTIRLLA----VDATFKANS--GHPGAPMGMAPVA---HVLFNKfmnfnpknpnwlNRDRFVLSNGHGcmlQYA 76
Cdd:PLN02234 76 MKNLSIKELKVLSdelrSDVIFNVSKtgGHLGSNLGVVELTvalHYIFNT------------PHDKILWDVGHQ---SYP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 77 LLHLFGYDVTMDDLKNFRQLDSITPGHPEAHDTPGVEVTTGPLGQGFANAVGLAIAQahtaavfnkpgydlINNYTYCFF 156
Cdd:PLN02234 141 HKILTGRRGKMKTIRQTNGLSGYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRDLKG--------------MNNSVVSVI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 157 GDGCAMEGIASEAASMAGHLKlGNLIAIYDDNH------ISIDGDTK------CAFTEDVMKR----------FEAYGWH 214
Cdd:PLN02234 207 GDGAMTAGQAYEAMNNAGYLH-SNMIVILNDNKqvslptANLDGPTQpvgalsCALSRLQSNCgmiretsstlFEELGFH 285
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2115080454 215 TVWVKDGDN--DLEGIEAAIHEAKKVtdKPTVIRLTTTIGFG 254
Cdd:PLN02234 286 YVGPVDGHNidDLVSILETLKSTKTI--GPVLIHVVTEKGRG 325
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
469-585 |
8.81e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 39.50 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2115080454 469 DSIGL-GEDGPTHQPIETLAHFRALPNCMVWRPADGNETSAAYYSAITAKHTPSVLALTRQN-----LPQlENSTIEAAL 542
Cdd:PLN02582 456 DRAGLvGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNgigvqLPP-NNKGIPIEV 534
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2115080454 543 KGAYPVVEAPNAAitLISTGSEVSICIEAATYLkEKHNIVARV 585
Cdd:PLN02582 535 GKGRILLEGERVA--LLGYGTAVQSCLAAASLL-ERHGLSATV 574
|
|
| |
