|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-664 |
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: 1244.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 3 DKTDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHLSG 82
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANP-KWPNRDRFVLSAGHGSMLLYSLLHLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 83 YNVTIDDLKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGDLM 162
Cdd:COG0021 80 YDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 163 EGVSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGNDLDEIEAAIEAAKAETDKPT 242
Cdd:COG0021 160 EGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 243 LIEVKTVIGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWEYPDFTVPEEVAARFKETmIDEGQKAEEAWNEMFKNYEHA 321
Cdd:COG0021 240 LIICKTIIGYGSPnKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAA-GERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 322 HPELAKQFKEAFANQLPEGWEQELPKYELGTSA-ASRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPGQY 400
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGvATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 401 EGRNIWFGVREFAMAAAMNGIQLHGGSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQLA 480
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 481 SVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTLEHASDsVQKGAYVLSPQKGeQPAGILIATG 560
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAEG-VAKGAYVLADAEG-TPDVILIATG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 561 SEVNLAVEAQAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTKRVAIEAAASFGWERYVGTEGKTITIDHFGAS 640
Cdd:COG0021 557 SEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGAS 636
|
650 660
....*....|....*....|....
gi 488289091 641 APGGLVLEKFGFTPENVVNTYKSL 664
Cdd:COG0021 637 APAKVLFEEFGFTVENVVAAAKEL 660
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
10-664 |
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: 965.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 10 VNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSRnWVDRDRFVLSAGHGSAMLYSLLHLSGYNVTIDD 89
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPK-WINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 90 LKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGDLMEGVSQEA 169
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 170 SSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGNDLDEIEAAIEAAKAETDKPTLIEVKTV 249
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 250 IGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWEYPDFTVPEEVAARFKETMIDEGQKAEEAWNEMFKNYEHAHPELAKQ 328
Cdd:TIGR00232 243 IGFGSPnKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 329 FKEAFANQLPEGWEQELPKYEL-GTSAASRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPGQYeGRNIWF 407
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHENPL-GNYIHY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 408 GVREFAMAAAMNGIQLHGGSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQLASVRCIPN 487
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 488 VHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTlehASDSVQKGAYVLSpqKGEQPAGILIATGSEVNLAV 567
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEES---SLEKVLKGGYVLK--DSKGPDLILIATGSEVQLAV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 568 EAQAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTkRVAIEAAASFGWERYVGTEGKTITIDHFGASAPGGLVL 647
Cdd:TIGR00232 557 EAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLF 635
|
650
....*....|....*..
gi 488289091 648 EKFGFTPENVVNTYKSL 664
Cdd:TIGR00232 636 EEFGFTVENVVAKAKKL 652
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-664 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 937.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 1 MFDKTDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHL 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNP-KWPNRDRFVLSAGHGSMLLYSLLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 81 SGYNVTIDDLKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGD 160
Cdd:PRK05899 82 AGYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 161 LMEGVSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVkDGNDLDeIEAAIEAAKAETDK 240
Cdd:PRK05899 162 LMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVE-AIDAAIEEAKASTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 241 PTLIEVKTVIGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWEYpdftvpeevaarfketmidegqkaeeawnemfknye 319
Cdd:PRK05899 240 PTLIIAKTIIGKGAPnKEGTHKVHGAPLGAEEIAAAKKELGWDY------------------------------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 320 hahpelakqfkeafanqlpegweqelpkyelgtsaasRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPGQ 399
Cdd:PRK05899 284 -------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPED 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 400 YEGRNIWFGVREFAMAAAMNGIQLHGGSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQL 479
Cdd:PRK05899 327 YSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 480 ASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTleHASDSVQKGAYVLSpqkgEQPAGILIAT 559
Cdd:PRK05899 407 ASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERT--AQEEGVAKGGYVLR----DDPDVILIAT 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 560 GSEVNLAVEAQAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTKRVAIEAAASFGWERYVGTEGKTITIDHFGA 639
Cdd:PRK05899 481 GSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGA 560
|
650 660
....*....|....*....|....*
gi 488289091 640 SAPGGLVLEKFGFTPENVVNTYKSL 664
Cdd:PRK05899 561 SAPADELFKEFGFTVENIVAAAKEL 585
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-338 |
2.65e-174 |
|
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: 499.61 E-value: 2.65e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 5 TDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHLSGYN 84
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDP-KWINRDRFVLSNGHGSMLLYSLLHLTGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 85 VTIDDLKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGDLMEG 164
Cdd:pfam00456 80 LSMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 165 VSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGNDLDEIEAAIEAAKAETDKPTLI 244
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 245 EVKTVIGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWE-YPDFTVPEEVAARFKETmIDEGQKAEEAWNEMFKNYEHAH 322
Cdd:pfam00456 240 KCRTVIGYGSPnKQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEK-VAEGAKAEAEWNELFAAYKKAY 318
|
330
....*....|....*.
gi 488289091 323 PELAKQFKEAFANQLP 338
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-276 |
1.07e-131 |
|
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: 387.63 E-value: 1.07e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 11 NTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHLSGYNVTiDDL 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADP-KWPNRDRFVLSKGHASPALYAVLALAGYLPE-EDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 91 KNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLaatynrdsfpIMDHYTYAICGDGDLMEGVSQEAS 170
Cdd:cd02012 79 KTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 171 SMAGHMKLGKLIVLYDSNDISLDGPTSK-AFTENVGARYEAYGWQHILVkDGNDLDEIEAAIEAAKAETDKPTLIEVKTV 249
Cdd:cd02012 149 SFAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTI 227
|
250 260
....*....|....*....|....*...
gi 488289091 250 IGYGAP-KEGTSSVHGAPIGEEGITAAK 276
Cdd:cd02012 228 KGKGVPfMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
405-524 |
4.94e-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: 123.75 E-value: 4.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 405 IWFGVREFAMAAAMNGIQLHGGsHVYGGTFFVFTDYLRPAIRLAALQKvPVTYVLTHDS-VAVGEDGPTHEPIEQLASVR 483
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488289091 484 CIPNVHVIRPADGNETVAAWKIAMTStETPTILVLSRQNLP 524
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-664 |
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: 1244.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 3 DKTDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHLSG 82
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANP-KWPNRDRFVLSAGHGSMLLYSLLHLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 83 YNVTIDDLKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGDLM 162
Cdd:COG0021 80 YDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 163 EGVSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGNDLDEIEAAIEAAKAETDKPT 242
Cdd:COG0021 160 EGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 243 LIEVKTVIGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWEYPDFTVPEEVAARFKETmIDEGQKAEEAWNEMFKNYEHA 321
Cdd:COG0021 240 LIICKTIIGYGSPnKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAA-GERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 322 HPELAKQFKEAFANQLPEGWEQELPKYELGTSA-ASRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPGQY 400
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGvATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 401 EGRNIWFGVREFAMAAAMNGIQLHGGSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQLA 480
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 481 SVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTLEHASDsVQKGAYVLSPQKGeQPAGILIATG 560
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAEG-VAKGAYVLADAEG-TPDVILIATG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 561 SEVNLAVEAQAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTKRVAIEAAASFGWERYVGTEGKTITIDHFGAS 640
Cdd:COG0021 557 SEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGAS 636
|
650 660
....*....|....*....|....
gi 488289091 641 APGGLVLEKFGFTPENVVNTYKSL 664
Cdd:COG0021 637 APAKVLFEEFGFTVENVVAAAKEL 660
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
10-664 |
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: 965.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 10 VNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSRnWVDRDRFVLSAGHGSAMLYSLLHLSGYNVTIDD 89
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPK-WINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 90 LKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGDLMEGVSQEA 169
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 170 SSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGNDLDEIEAAIEAAKAETDKPTLIEVKTV 249
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 250 IGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWEYPDFTVPEEVAARFKETMIDEGQKAEEAWNEMFKNYEHAHPELAKQ 328
Cdd:TIGR00232 243 IGFGSPnKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 329 FKEAFANQLPEGWEQELPKYEL-GTSAASRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPGQYeGRNIWF 407
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHENPL-GNYIHY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 408 GVREFAMAAAMNGIQLHGGSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQLASVRCIPN 487
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 488 VHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTlehASDSVQKGAYVLSpqKGEQPAGILIATGSEVNLAV 567
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEES---SLEKVLKGGYVLK--DSKGPDLILIATGSEVQLAV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 568 EAQAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTkRVAIEAAASFGWERYVGTEGKTITIDHFGASAPGGLVL 647
Cdd:TIGR00232 557 EAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLF 635
|
650
....*....|....*..
gi 488289091 648 EKFGFTPENVVNTYKSL 664
Cdd:TIGR00232 636 EEFGFTVENVVAKAKKL 652
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-664 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 937.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 1 MFDKTDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHL 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNP-KWPNRDRFVLSAGHGSMLLYSLLHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 81 SGYNVTIDDLKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGD 160
Cdd:PRK05899 82 AGYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 161 LMEGVSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVkDGNDLDeIEAAIEAAKAETDK 240
Cdd:PRK05899 162 LMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVE-AIDAAIEEAKASTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 241 PTLIEVKTVIGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWEYpdftvpeevaarfketmidegqkaeeawnemfknye 319
Cdd:PRK05899 240 PTLIIAKTIIGKGAPnKEGTHKVHGAPLGAEEIAAAKKELGWDY------------------------------------ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 320 hahpelakqfkeafanqlpegweqelpkyelgtsaasRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPGQ 399
Cdd:PRK05899 284 -------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPED 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 400 YEGRNIWFGVREFAMAAAMNGIQLHGGSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQL 479
Cdd:PRK05899 327 YSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 480 ASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTleHASDSVQKGAYVLSpqkgEQPAGILIAT 559
Cdd:PRK05899 407 ASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERT--AQEEGVAKGGYVLR----DDPDVILIAT 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 560 GSEVNLAVEAQAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTKRVAIEAAASFGWERYVGTEGKTITIDHFGA 639
Cdd:PRK05899 481 GSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGA 560
|
650 660
....*....|....*....|....*
gi 488289091 640 SAPGGLVLEKFGFTPENVVNTYKSL 664
Cdd:PRK05899 561 SAPADELFKEFGFTVENIVAAAKEL 585
|
|
| PLN02790 |
PLN02790 |
transketolase |
13-664 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 920.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 13 IRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHLSGYN-VTIDDLK 91
Cdd:PLN02790 1 IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNP-YWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 92 NFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGDLMEGVSQEASS 171
Cdd:PLN02790 80 QFRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 172 MAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGN-DLDEIEAAIEAAKAETDKPTLIEVKTVI 250
Cdd:PLN02790 160 LAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNtDYDEIRAAIKEAKAVTDKPTLIKVTTTI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 251 GYGAPKEGTS-SVHGAPIGEEGITAAKAVYGWEYPDFTVPEEVAARFKEtMIDEGQKAEEAWNEMFKNYEHAHPELAKQF 329
Cdd:PLN02790 240 GYGSPNKANSySVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWSK-HTKEGAALEAEWNAKFAEYKKKYPEEAAEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 330 KEAFANQLPEGWEQELPKYELGTSA-ASRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPGQYEGRNIWFG 408
Cdd:PLN02790 319 KSLISGELPSGWEKALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 409 VREFAMAAAMNGIQLHG-GSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQLASVRCIPN 487
Cdd:PLN02790 399 VREHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 488 VHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTlehASDSVQKGAYVLS-PQKGEQPAGILIATGSEVNLA 566
Cdd:PLN02790 479 ILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGT---SIEGVEKGGYVISdNSSGNKPDLILIGTGSELEIA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 567 VEAQAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTKRVAIEAAASFGWERYVGTEGKTITIDHFGASAPGGLV 646
Cdd:PLN02790 556 AKAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGIL 635
|
650
....*....|....*...
gi 488289091 647 LEKFGFTPENVVNTYKSL 664
Cdd:PLN02790 636 YKEFGFTVENVVAAAKSL 653
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
1-664 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 859.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 1 MFDKTDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSRnWVDRDRFVLSAGHGSAMLYSLLHL 80
Cdd:PTZ00089 1 MDGAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPR-WINRDRFVLSNGHASALLYSMLHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 81 SGYNVTIDDLKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGD 160
Cdd:PTZ00089 80 TGYDLSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 161 LMEGVSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGN-DLDEIEAAIEAAKAETD 239
Cdd:PTZ00089 160 LQEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSKG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 240 KPTLIEVKTVIGYGAPKEGTSSVHGAPIGEEGITAAKAVYGWEyPD--FTVPEEVAARFKEtMIDEGQKAEEAWNEMFKN 317
Cdd:PTZ00089 240 KPKLIIVKTTIGYGSSKAGTEKVHGAPLGDEDIAQVKELFGLD-PEkkFHVSEEVRQFFEQ-HVEKKKENYEAWKKRFAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 318 YEHAHPELAKQFKEAFANQLPEGWEQELPKYELGTSA-ASRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFE 396
Cdd:PTZ00089 318 YTAAFPKEAQAIERRFKGELPPGWEKKLPKYTTNDKAiATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 397 PGQYEGRNIWFGVREFAMAAAMNGIQLHGGSHVYGGTFFVFTDYLRPAIRLAALQKVPVTYVLTHDSVAVGEDGPTHEPI 476
Cdd:PTZ00089 398 KASPEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 477 EQLASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTlehASDSVQKGAYVLSPQKgEQPAGIL 556
Cdd:PTZ00089 478 ETLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGS---SIEGVLKGAYIVVDFT-NSPQLIL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 557 IATGSEVNLAVEAqAKLAEEGIDVSVVSMPSFDLFEKQSAEYKESVLPKAVTKRVAIEAAASFGWERYVgteGKTITIDH 636
Cdd:PTZ00089 554 VASGSEVSLCVEA-AKALSKELNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYS---HVHVGISG 629
|
650 660
....*....|....*....|....*...
gi 488289091 637 FGASAPGGLVLEKFGFTPENVVNTYKSL 664
Cdd:PTZ00089 630 FGASAPANALYKHFGFTVENVVEKARAL 657
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-338 |
2.65e-174 |
|
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: 499.61 E-value: 2.65e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 5 TDQLGVNTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHLSGYN 84
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDP-KWINRDRFVLSNGHGSMLLYSLLHLTGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 85 VTIDDLKNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAATYNRDSFPIMDHYTYAICGDGDLMEG 164
Cdd:pfam00456 80 LSMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 165 VSQEASSMAGHMKLGKLIVLYDSNDISLDGPTSKAFTENVGARYEAYGWQHILVKDGNDLDEIEAAIEAAKAETDKPTLI 244
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 245 EVKTVIGYGAP-KEGTSSVHGAPIGEEGITAAKAVYGWE-YPDFTVPEEVAARFKETmIDEGQKAEEAWNEMFKNYEHAH 322
Cdd:pfam00456 240 KCRTVIGYGSPnKQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEK-VAEGAKAEAEWNELFAAYKKAY 318
|
330
....*....|....*.
gi 488289091 323 PELAKQFKEAFANQLP 338
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-276 |
1.07e-131 |
|
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: 387.63 E-value: 1.07e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 11 NTIRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSrNWVDRDRFVLSAGHGSAMLYSLLHLSGYNVTiDDL 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADP-KWPNRDRFVLSKGHASPALYAVLALAGYLPE-EDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 91 KNFRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLaatynrdsfpIMDHYTYAICGDGDLMEGVSQEAS 170
Cdd:cd02012 79 KTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 171 SMAGHMKLGKLIVLYDSNDISLDGPTSK-AFTENVGARYEAYGWQHILVkDGNDLDEIEAAIEAAKAETDKPTLIEVKTV 249
Cdd:cd02012 149 SFAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTI 227
|
250 260
....*....|....*....|....*...
gi 488289091 250 IGYGAP-KEGTSSVHGAPIGEEGITAAK 276
Cdd:cd02012 228 KGKGVPfMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
13-277 |
5.34e-62 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 207.62 E-value: 5.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 13 IRTLSIEAVQKANSGHPGLPMGAAPMAYALWTKHLKVNPTTSRnWVDRDRFVLSAGHGSAMLYSLLHLSGYnVTIDDLKN 92
Cdd:COG3959 15 IRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPD-WPDRDRFILSKGHAAPALYAVLAEKGY-FPKEELAT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 93 FRQWDSKTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAmaeahLAATYNRDsfpimDHYTYAICGDGDLMEGVSQEASSM 172
Cdd:COG3959 93 FRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMA-----LAAKLDGK-----DYRVYVLLGDGELQEGQVWEAAMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 173 AGHMKLGKLIVLYDSNDISLDGPTSKAF-TENVGARYEAYGWqHILVKDGNDLDEIEAAIEAAKAETDKPTLIEVKTVIG 251
Cdd:COG3959 163 AAHYKLDNLIAIVDRNGLQIDGPTEDVMsLEPLAEKWEAFGW-HVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTVKG 241
|
250 260
....*....|....*....|....*..
gi 488289091 252 YGAPK-EGTSSVHGAPIGEEGITAAKA 277
Cdd:COG3959 242 KGVSFmENRPKWHGKAPNDEELEQALA 268
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
362-520 |
3.74e-57 |
|
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: 190.35 E-value: 3.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 362 ETIQAISKVVPSFWGGSADLSASNNTMVAAEKdfepgqYEGRNIWFGVREFAMAAAMNGIQLHGgSHVYGGTFFVFTDYL 441
Cdd:cd07033 5 EALLELAKKDPRIVALSADLGGSTGLDKFAKK------FPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 442 RPAIR-LAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVAAWKIAMTSTEtPTILVLSR 520
Cdd:cd07033 78 YDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDG-PVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
353-525 |
8.89e-53 |
|
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: 179.28 E-value: 8.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 353 SAASRVTSKETIQAISKVVPSFWGGSADLSASNNTMVAAEKDFEPgqyEGRNIWFGVREFAMAAAMNGIQLHGGS-HVYG 431
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQG---AGRVIDTGIAEQAMVGFANGMALHGPLlPPVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 432 GTFFVFTDYLRPAIR-LAALQKVPVTYVLTHDSVAVGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVAAWKIAM-TS 509
Cdd:pfam02779 79 ATFSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIrRD 158
|
170
....*....|....*.
gi 488289091 510 TETPTILVLSRQNLPV 525
Cdd:pfam02779 159 GRKPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
405-524 |
4.94e-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: 123.75 E-value: 4.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 405 IWFGVREFAMAAAMNGIQLHGGsHVYGGTFFVFTDYLRPAIRLAALQKvPVTYVLTHDS-VAVGEDGPTHEPIEQLASVR 483
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488289091 484 CIPNVHVIRPADGNETVAAWKIAMTStETPTILVLSRQNLP 524
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLY 135
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
378-664 |
5.17e-27 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 111.72 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 378 SADLSASNNTMVAAEKdFePGQYegrnIWFGVREFAM--AAAmnGIQLhGGSHVYGGTFFVFTdYLRPA--IRLA-ALQK 452
Cdd:COG3958 28 DADLGGSTKLDKFAKA-F-PDRF----FNVGIAEQNMvgVAA--GLAL-AGKIPFVSTFAPFL-TGRAYeqIRNDiAYPN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 453 VPVTYVLTHDSVAVGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVAAWKiAMTSTETPTILVLSRQNLPVLegtleH 532
Cdd:COG3958 98 LNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVR-AAAEHDGPVYLRLGRGAVPVV-----Y 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 533 ASDSVQK--GAYVLspQKGEqpAGILIATGSEVNLAVEAQAKLAEEGIDVSVVSMPS---FDlfekqsaeyKESVLpKAV 607
Cdd:COG3958 172 DEDYEFEigKARVL--REGK--DVTIIATGIMVAEALEAAELLAKEGISARVINMHTikpLD---------EEAIL-KAA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488289091 608 --TKR-VAIE----------AAASFGWERY------VGTEgktitiDHFGASAPGGLVLEKFGFTPENVVNTYKSL 664
Cdd:COG3958 238 rkTGAvVTAEehsiigglgsAVAEVLAENYpvplrrIGVP------DRFGESGSPEELLEKYGLDAEGIVAAAKEL 307
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
555-657 |
2.58e-16 |
|
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: 75.71 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 555 ILIATGSEVNLAVEAQAKLAEEGIDVSVVSMPSFDLFEKQS-----AEYKESVLPKAVTKRVAIEAAAS--------FGW 621
Cdd:pfam02780 13 TIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEEAVPRGGFGSEVAaalaeeafDGL 92
|
90 100 110
....*....|....*....|....*....|....*.
gi 488289091 622 ERYVgtegKTITIDHFGASAPGGLVLEKFGFTPENV 657
Cdd:pfam02780 93 DAPV----LRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
13-225 |
7.37e-13 |
|
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: 70.80 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 13 IRTLSIEAVQKANS------GHPGLPMGAAPMAYALWTKHLKvnptTSRNWVDRDRfVLSAGHGSAMLYSLLHLSGyNVT 86
Cdd:cd02017 11 IRWNAMAMVHRANKkdlgigGHIATFASAATLYEVGFNHFFR----ARGEGGGGDL-VYFQGHASPGIYARAFLEG-RLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 87 IDDLKNFRQWDSKtPGHPEVHHT----DGVEATTGPLGQGIAMAVGMAMAEAHLAAT-YNRDSfpimDHYTYAICGDGDL 161
Cdd:cd02017 85 EEQLDNFRQEVGG-GGLSSYPHPwlmpDFWEFPTVSMGLGPIQAIYQARFNRYLEDRgLKDTS----DQKVWAFLGDGEM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488289091 162 MEGVSQEASSMAGHMKLGKLIVLYDSNDISLDGP---TSKAFTEnVGARYEAYGWQHILVKDGNDLD 225
Cdd:cd02017 160 DEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPvrgNGKIIQE-LEGIFRGAGWNVIKVIWGSKWD 225
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
12-659 |
1.76e-12 |
|
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129308 [Multi-domain] Cd Length: 617 Bit Score: 70.57 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 12 TIRTLSIEAVQkANSGHPGLPMGAAPMAYALwtkHLKVNpttsrnwVDRDRFVLSAGHGSamlYSLLHLSGYNvtiDDLK 91
Cdd:TIGR00204 24 ELRRYLLESVS-ASGGHLASGLGTVELTVAL---HYVFN-------TPKDQFIWDVGHQA---YPHKLLTGRR---EKFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 92 NFRQWDSkTPGHPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAHLAAtynrdsfpimDHYTYAICGDGDLMEGVSQEASS 171
Cdd:TIGR00204 87 TLRQKKG-LHGFPKRSESEYDVFSAGHSSTSISAGLGIAVAAEKKGA----------DRKTVCVIGDGAITAGMAFEALN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 172 MAGHMKLGKLIVLYDsNDISLdgptskafTENVGARYEA---------YGWqhilVKDGNdldeieaaieaakaetdKPT 242
Cdd:TIGR00204 156 HAGDLKTDMIVILND-NEMSI--------SENVGALSNHlaqlrsgslYQS----LRDGL-----------------KKI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 243 LIEVKTVIGYGAP--KEGTSS--VHGAPIGEEGITAAKAVYGWEYpdftvpeevaarfkETMIDEGQKAEEAWNEMFKny 318
Cdd:TIGR00204 206 FSKLPPIKNYLAKrtEESMKGlvVPGTFFEELGFNYIGPVDGHDL--------------LELIETLKNAKKLKGPVFL-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 319 eHAHPELAKQFKEAFANqlPEGWeQELPKYELGTSAAsrVTSKETIQAISKVvpsFWGGSADLSASNNTMVAAEKDFEPG 398
Cdd:TIGR00204 270 -HIQTKKGKGYKPAEKD--PIGW-HGVGPFDLSTGCL--PKSKSALPSYSKI---FSDTLCELAKKDNKIVGITPAMPEG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 399 --------QYEGRNIWFGVRE-----FAMAAAMNGiqlhggshvYGGTFFVFTDYLRPA----IRLAALQKVPVTYVLTH 461
Cdd:TIGR00204 341 sgldkfsrKFPDRYFDVAIAEqhavtFAAGMAIEG---------YKPFVAIYSTFLQRAydqvVHDVCIQKLPVLFAIDR 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 462 DSVaVGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTLEHASDSVQKGA 541
Cdd:TIGR00204 412 AGI-VGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTPEPEKLPIGKSE 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 542 YVlspQKGEQPAgiLIATGSEVNLAVEAQAKLAEEGIDVSVVSM----PsfdLFEKQSAEYKESVLPKAVTKRVAIEAAA 617
Cdd:TIGR00204 491 VL---RKGEKIL--ILGFGTLVPEALEVAESLNEKGIEATVVDArfvkP---LDEELILEIAASHEKLVTVEENAIMGGA 562
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 488289091 618 SFGWERYVGTEGKTITIDHFG------ASAPGGLVLEKFGFTPENVVN 659
Cdd:TIGR00204 563 GSAVLEFLMDQNKLVPVKRLGipdffiPHGTQEEVLAELGLDTAGMEA 610
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
449-585 |
2.21e-11 |
|
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: 66.96 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 449 ALQKVPVTYVLthDSvA--VGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVaawkiAMTST----ETPTILVLSRQN 522
Cdd:COG1154 406 ALQNLPVTFAI--DR-AglVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELR-----HMLYTalayDGPTAIRYPRGN 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488289091 523 LPVLEgtLEHASDSVQKG-AYVLspQKGEQPAgiLIATGSEVNLAVEAQAKLAEEGIDVSVVSM 585
Cdd:COG1154 478 GPGVE--LPAELEPLPIGkGEVL--REGKDVA--ILAFGTMVAEALEAAERLAAEGISATVVDA 535
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
13-585 |
7.79e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 65.13 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 13 IRTLSIEAVQKAnSGHPGLPMGAAPMAYALwtkHLKVNPTtsrnwvdRDRFVLSAGHGSamlYSLLHLSGYNvtiDDLKN 92
Cdd:PRK12571 33 LRAEVISAVSET-GGHLGSSLGVVELTVAL---HAVFNTP-------KDKLVWDVGHQC---YPHKILTGRR---DRFRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 93 FRQWD--SKTPGHPEVHHtDGVEAttGPLGQGIAMAVGMAMAEAHLAAtynrdsfpimDHYTYAICGDGDLMEGVSQEAS 170
Cdd:PRK12571 96 LRQKGglSGFTKRSESEY-DPFGA--AHSSTSISAALGFAKARALGQP----------DGDVVAVIGDGSLTAGMAYEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 171 SMAGHMKlGKLIVLYDSNDISLDGPTS------------------KAFTENVGAR------------------------- 207
Cdd:PRK12571 163 NNAGAAD-RRLIVILNDNEMSIAPPVGalaaylstlrssdpfarlRAIAKGVEERlpgplrdgarrarelvtgmigggtl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 208 YEAYGWQHILVKDGNDLDEIEAAIEAAKAETDKPTLIEVKTVIGYG-APKE-------GTSSVHGApIGEEGITAAKAvy 279
Cdd:PRK12571 242 FEELGFTYVGPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGyAPAEadedkyhAVGKFDVV-TGLQKKSAPSA-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 280 gweyPDFTvpeevaARFKETMIDEGQKAEEAwnemfknyehahpelakqfkeafanqlpegweqelpkyeLGTSAASRvt 359
Cdd:PRK12571 319 ----PSYT------SVFGEELTKEAAEDSDI---------------------------------------VAITAAMP-- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 360 SKETIQAISKVVPsfwggsadlsasnntmvaaEKDFEPGQYEGRNIWFgvrefamAAAMngiqLHGGSHVYggtFFVFTD 439
Cdd:PRK12571 348 LGTGLDKLQKRFP-------------------NRVFDVGIAEQHAVTF-------AAGL----AAAGLKPF---CAVYST 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 440 YLRPA----IRLAALQKVPVTYVLTHDSVaVGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTI 515
Cdd:PRK12571 395 FLQRGydqlLHDVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIA 473
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 516 LVLSRQNLPVLEGTLEHASDSVQKGAYVlspqkGEQPAGILIATGSEVNLAVEAQAKLAEEGIDVSVVSM 585
Cdd:PRK12571 474 VRFPRGEGVGVEIPAEGTILGIGKGRVP-----REGPDVAILSVGAHLHECLDAADLLEAEGISVTVADP 538
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
103-248 |
1.46e-08 |
|
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: 54.57 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 103 HPEVHHTDGVEATTGPLGQGIAMAVGMAMAEAhlaatynrdsfpimDHYTYAICGDGDLMEGVsQEASSMAGHMklGKLI 182
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP--------------DRPVVCIAGDGGFMMTG-QELATAVRYG--LPVI 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488289091 183 VLYDSNDISLDGPTS--KAFTENVGARY----------EAYGWQHILVKDGNDLDeieaAIEAAKAETDKPTLIEVKT 248
Cdd:cd00568 95 VVVFNNGGYGTIRMHqeAFYGGRVSGTDlsnpdfaalaEAYGAKGVRVEDPEDLE----AALAEALAAGGPALIEVKT 168
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
449-585 |
5.00e-08 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 56.24 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 449 ALQKVPVTYVLthDSvA--VGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNlpvL 526
Cdd:PRK05444 368 ALQNLPVTFAI--DR-AglVGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGN---G 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289091 527 EGTLEHASDSVQKGayvlspqKGE---QPAGILI-ATGSEVNLAVEAQAKLAEegidVSVVSM 585
Cdd:PRK05444 442 VGVELPELEPLPIG-------KGEvlrEGEDVAIlAFGTMLAEALKAAERLAS----ATVVDA 493
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
123-583 |
3.81e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 53.09 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 123 IAMAVGMAMAEAHLAATYNrdsfpIMdhytyAICGDGDLMEGVSQEASSMAGHMKlGKLIVLYDSNDISLDgptskaftE 202
Cdd:PRK12315 119 IALATGLAKARDLKGEKGN-----II-----AVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIA--------E 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 203 NVGARYE------------------AYGWQHILVKDGNDLdEIEAAIEAAKAETDKPTLIEVKTVIGYG-APKEgtssvh 263
Cdd:PRK12315 180 NHGGLYKnlkelrdtngqsennlfkAMGLDYRYVEDGNDI-ESLIEAFKEVKDIDHPIVLHIHTLKGKGyQPAE------ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 264 gapigeegitAAKAVYGWEYPdFTVpeevaarfkETMIDEGQKAEEAWNEMFKNYehahpeLAKQFKEafanqlpegweq 343
Cdd:PRK12315 253 ----------ENKEAFHWHMP-FDL---------ETGQSKVPASGESYSSVTLDY------LLKKIKE------------ 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 344 elpkyelgtsaasrvtsKETIQAISKVVPSFWGgsadlsasnntmVAAEKDFEPGQYEGRNIwfgVREFAMAAAmNGIQL 423
Cdd:PRK12315 295 -----------------GKPVVAINAAIPGVFG------------LKEFRKKYPDQYVDVGI---AEQESVAFA-SGIAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 424 HGGSHVYggtfFVFTDYLRPA----IRLAALQKVPVTYVLTHDSvaVGEDGPTHEPIEQLASVRCIPNVHVIRPADGNET 499
Cdd:PRK12315 342 NGARPVI----FVNSTFLQRAydqlSHDLAINNNPAVMIVFGGS--ISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEEL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 500 VAAWKIAMTSTETPTILVLSRQNLPVLEGTLEHASDSVQKGAyvlspQKGEQPAgiLIATGSEVNLAVEAQAKLAEE-GI 578
Cdd:PRK12315 416 IAMLEWALTQHEHPVAIRVPEHGVESGPTVDTDYSTLKYEVT-----KAGEKVA--ILALGDFYELGEKVAKKLKEElGI 488
|
....*
gi 488289091 579 DVSVV 583
Cdd:PRK12315 489 DATLI 493
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
115-253 |
9.27e-06 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 46.77 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 115 TTGPLGQGIAMAVGMAMAEAHLAAtynrdsfpimDHYTYAICGDGDLMEGVSQEASSMAGHMKlGKLIVLYDSNDISLDg 194
Cdd:cd02007 73 GTGHSSTSISAALGMAVARDLKGK----------KRKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSIS- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488289091 195 ptskaftENVGAR---YEAYGWQHILVKDGNDLDeIEAAIEAAKAETDKPTLIEVKTVIGYG 253
Cdd:cd02007 141 -------PNVGTPgnlFEELGFRYIGPVDGHNIE-ALIKVLKEVKDLKGPVLLHVVTKKGKG 194
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
27-582 |
3.89e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 47.01 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 27 GHPGLPMGAAPMAYALwtkHLKVNpttsrnwVDRDRFVLSAGHGSamlYSLLHLSGYNVTIDDLKNFRQWDSKTPGHPEV 106
Cdd:PLN02234 104 GHLGSNLGVVELTVAL---HYIFN-------TPHDKILWDVGHQS---YPHKILTGRRGKMKTIRQTNGLSGYTKRRESE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 107 HHTDGVEATTGPLGQGIAMAVGmamaeahlaatynRDsFPIMDHYTYAICGDGDLMEGVSQEASSMAGHMKLGKLIVLYD 186
Cdd:PLN02234 171 HDSFGTGHSSTTLSAGLGMAVG-------------RD-LKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILND 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 187 SNDIS-----LDGPT----------------SKAFTENVGARYEAYGWQHILVKDGNDLDE-IEAAIEAAKAETDKPTLI 244
Cdd:PLN02234 237 NKQVSlptanLDGPTqpvgalscalsrlqsnCGMIRETSSTLFEELGFHYVGPVDGHNIDDlVSILETLKSTKTIGPVLI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 245 EVKTVIGYGAPKegtssvhgapigeegitaakavygweypdftvpeevaarfketmideGQKAEEAWNEMFKnyehAHPE 324
Cdd:PLN02234 317 HVVTEKGRGYPY-----------------------------------------------AERADDKYHGVLK----FDPE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 325 LAKQFKeafanqlpegweqELPKYELGTS--AASRVTSKETIQAISKVVPSFWGGsadlsasnnTMVaaekdfepGQYEG 402
Cdd:PLN02234 346 TGKQFK-------------NISKTQSYTScfVEALIAEAEADKDIVAIHAAMGGG---------TML--------NLFES 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 403 RniwFGVREFAMA-AAMNGIQLHGGSHVYGGTFF--VFTDYLRPA----IRLAALQKVPVTYVLTHDSVaVGEDGPTHEP 475
Cdd:PLN02234 396 R---FPTRCFDVGiAEQHAVTFAAGLACEGLKPFctIYSSFMQRAydqvVHDVDLQKLPVRFAIDRAGL-MGADGPTHCG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 476 IEQLASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQNLPVLEGTLEHASDSVQKG-AYVLspQKGEQPAg 554
Cdd:PLN02234 472 AFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPPGNKGVPLQIGrGRIL--RDGERVA- 548
|
570 580
....*....|....*....|....*...
gi 488289091 555 iLIATGSEVNLAVEAQAKLAEEGIDVSV 582
Cdd:PLN02234 549 -LLGYGSAVQRCLEAASMLSERGLKITV 575
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
114-249 |
5.36e-05 |
|
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: 45.56 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 114 ATTGPLGQGIAMAVGMAMaeahlAATYNRDsfpimDHYTYAICGDGDLMEGVSQEASSMAGHMKLGKLIVLYDsNDISLD 193
Cdd:cd02000 101 GGNGIVGGQVPLAAGAAL-----ALKYRGE-----DRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAIS 169
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 194 GPTSKAF-TENVGARYEAYGWQHILVkDGNDLDEIEAAIEAAKA---ETDKPTLIEVKTV 249
Cdd:cd02000 170 TPTSRQTaGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVErarAGGGPTLIEAVTY 228
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
114-186 |
1.35e-04 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 42.97 E-value: 1.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488289091 114 ATTGPLGQGIAMAVGMAMAeahlaatyNRDSFPImdhytyAICGDGDLMEGVsQEASSMAgHMKLGKLIVLYD 186
Cdd:cd02002 46 LRGGGLGWGLPAAVGAALA--------NPDRKVV------AIIGDGSFMYTI-QALWTAA-RYGLPVTVVILN 102
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
450-582 |
2.34e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 44.51 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488289091 450 LQKVPVTYVLTHDSVaVGEDGPTHEPIEQLASVRCIPNVHVIRPADGNETVAAWKIAMTSTETPTILVLSRQN---LPVL 526
Cdd:PLN02582 446 LQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNgigVQLP 524
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 488289091 527 EGTlEHASDSVQKGAYVLspqKGEQPAgiLIATGSEVNLAVEAQAKLAEEGIDVSV 582
Cdd:PLN02582 525 PNN-KGIPIEVGKGRILL---EGERVA--LLGYGTAVQSCLAAASLLERHGLSATV 574
|
|
| |
