|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-662 |
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: 1203.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 3 NEKDQLAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSG- 81
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 82 SLELEELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDLME 161
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 162 GISHEAASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEG-PTI 240
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDkPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 241 IEVKTTIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPEKrFNVSEEVYEIFQNTmLKRANEDESQWNSLLEKYAET 320
Cdd:COG0021 241 IICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAA-GERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 321 YPELAEEFKLAISGKLPKNYKDELPRFELGHNG-ASRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSSETP 399
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGvATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 400 EGKNVWFGVREFAMGAAVNGMAAHGGLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLA 479
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 480 GLRAIPNMNVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLDvPEDVVEEGVRKGAYTVYGSEETPEFLLLASGS 559
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLD-RTAAAAEGVAKGAYVLADAEGTPDVILIATGS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 560 EVSLAVEAAKDLEKQGKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTKRVAIEMASPLGWHKYVGTAGKVIAIDGFGASA 639
Cdd:COG0021 558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
|
650 660
....*....|....*....|...
gi 446403588 640 PGDLVVEKYGFTKENILNQVMSL 662
Cdd:COG0021 638 PAKVLFEEFGFTVENVVAAAKEL 660
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
8-662 |
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: 939.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 8 LAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSG-SLELE 86
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGyDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 87 ELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDLMEGISHE 166
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 167 AASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEG-PTIIEVKT 245
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDkPTLIEVKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 246 TIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPEKrFNVSEEVYEIFQNTMLKRANEDESQWNSLLEKYAETYPELA 325
Cdd:TIGR00232 242 TIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 326 EEFKLAISGKLPKNYKDELPRFEL-GHNGASRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSsETPEGKNV 404
Cdd:TIGR00232 321 AEFTRRLSGELPADWDKQLPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLH-ENPLGNYI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 405 WFGVREFAMGAAVNGMAAHGGLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLAGLRAI 484
Cdd:TIGR00232 400 HYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 485 PNMNVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLDvPEDVveEGVRKGAYTVYGSEEtPEFLLLASGSEVSLA 564
Cdd:TIGR00232 480 PNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLE-ESSL--EKVLKGGYVLKDSKG-PDLILIATGSEVQLA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 565 VEAAKDLEKQGKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTkRVAIEMASPLGWHKYVGTAGKVIAIDGFGASAPGDLV 644
Cdd:TIGR00232 556 VEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKL 634
|
650
....*....|....*...
gi 446403588 645 VEKYGFTKENILNQVMSL 662
Cdd:TIGR00232 635 FEEFGFTVENVVAKAKKL 652
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-662 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 938.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 1 MFNEKDQLAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVS 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 81 G-SLELEELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDL 159
Cdd:PRK05899 83 GyDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 160 MEGISHEAASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVkDGNDLEEIDKAITTAKSQEGPT 239
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKASTKPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 240 IIEVKTTIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPekrfnvseevyeifqntmlkranedesqwnsllekyae 319
Cdd:PRK05899 242 LIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY-------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 320 typelaeefklaisgklpknykdelprfelghngasRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSSETP 399
Cdd:PRK05899 284 ------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 400 EGKNVWFGVREFAMGAAVNGMAAHGGLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLA 479
Cdd:PRK05899 328 SGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 480 GLRAIPNMNVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLDVPEDvvEEGVRKGAYTVygsEETPEFLLLASGS 559
Cdd:PRK05899 408 SLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTAQ--EEGVAKGGYVL---RDDPDVILIATGS 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 560 EVSLAVEAAKDLEKQGKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTKRVAIEMASPLGWHKYVGTAGKVIAIDGFGASA 639
Cdd:PRK05899 483 EVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASA 562
|
650 660
....*....|....*....|...
gi 446403588 640 PGDLVVEKYGFTKENILNQVMSL 662
Cdd:PRK05899 563 PADELFKEFGFTVENIVAAAKEL 585
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
6-337 |
5.07e-172 |
|
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: 493.83 E-value: 5.07e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 6 DQLAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSG-SLE 84
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGyDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 85 LEELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDLMEGIS 164
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 165 HEAASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEG-PTIIEV 243
Cdd:pfam00456 162 SEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDkPTLIKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 244 KTTIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPEKRFNVSEEVYEIFQNTmLKRANEDESQWNSLLEKYAETYPE 323
Cdd:pfam00456 242 RTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEK-VAEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 446403588 324 LAEEFKLAISGKLP 337
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-273 |
1.24e-133 |
|
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: 392.64 E-value: 1.24e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 11 DTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSGSLELEELKQ 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 91 FRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLagkfnkegynVVDHYTYVLASDGDLMEGISHEAASF 170
Cdd:cd02012 81 FRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAASF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 171 AGHNKLSKLVVLYDSNDISLDGELNK-AFSENTKARFEAYGWNYLLVkDGNDLEEIDKAITTAKSQEG-PTIIEVKTTIG 248
Cdd:cd02012 151 AGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGkPTLIIAKTIKG 229
|
250 260
....*....|....*....|....*
gi 446403588 249 FGSPNKAGTNGVHGAPLGEVERKLT 273
Cdd:cd02012 230 KGVPFMENTAKWHGKPLGEEEVELA 254
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
404-523 |
1.67e-37 |
|
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: 136.08 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 404 VWFGVREFAMGAAVNGMAAHGgLHPYGATFFVFSDYLKPALRLSSIMGlNATFIFTHDS-IAVGEDGPTHEPIEQLAGLR 482
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHG-LRPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446403588 483 AIPNMNVIRPADGNETRVAWEVALESEsTPTSLVLTRQNLP 523
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDD-GPVVIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-662 |
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: 1203.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 3 NEKDQLAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSG- 81
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 82 SLELEELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDLME 161
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 162 GISHEAASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEG-PTI 240
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDkPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 241 IEVKTTIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPEKrFNVSEEVYEIFQNTmLKRANEDESQWNSLLEKYAET 320
Cdd:COG0021 241 IICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAA-GERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 321 YPELAEEFKLAISGKLPKNYKDELPRFELGHNG-ASRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSSETP 399
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGvATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 400 EGKNVWFGVREFAMGAAVNGMAAHGGLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLA 479
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 480 GLRAIPNMNVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLDvPEDVVEEGVRKGAYTVYGSEETPEFLLLASGS 559
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLD-RTAAAAEGVAKGAYVLADAEGTPDVILIATGS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 560 EVSLAVEAAKDLEKQGKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTKRVAIEMASPLGWHKYVGTAGKVIAIDGFGASA 639
Cdd:COG0021 558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
|
650 660
....*....|....*....|...
gi 446403588 640 PGDLVVEKYGFTKENILNQVMSL 662
Cdd:COG0021 638 PAKVLFEEFGFTVENVVAAAKEL 660
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
8-662 |
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: 939.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 8 LAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSG-SLELE 86
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGyDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 87 ELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDLMEGISHE 166
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 167 AASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEG-PTIIEVKT 245
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDkPTLIEVKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 246 TIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPEKrFNVSEEVYEIFQNTMLKRANEDESQWNSLLEKYAETYPELA 325
Cdd:TIGR00232 242 TIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 326 EEFKLAISGKLPKNYKDELPRFEL-GHNGASRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSsETPEGKNV 404
Cdd:TIGR00232 321 AEFTRRLSGELPADWDKQLPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLH-ENPLGNYI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 405 WFGVREFAMGAAVNGMAAHGGLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLAGLRAI 484
Cdd:TIGR00232 400 HYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 485 PNMNVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLDvPEDVveEGVRKGAYTVYGSEEtPEFLLLASGSEVSLA 564
Cdd:TIGR00232 480 PNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLE-ESSL--EKVLKGGYVLKDSKG-PDLILIATGSEVQLA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 565 VEAAKDLEKQGKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTkRVAIEMASPLGWHKYVGTAGKVIAIDGFGASAPGDLV 644
Cdd:TIGR00232 556 VEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKL 634
|
650
....*....|....*...
gi 446403588 645 VEKYGFTKENILNQVMSL 662
Cdd:TIGR00232 635 FEEFGFTVENVVAKAKKL 652
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-662 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 938.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 1 MFNEKDQLAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVS 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 81 G-SLELEELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDL 159
Cdd:PRK05899 83 GyDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 160 MEGISHEAASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVkDGNDLEEIDKAITTAKSQEGPT 239
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKASTKPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 240 IIEVKTTIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPekrfnvseevyeifqntmlkranedesqwnsllekyae 319
Cdd:PRK05899 242 LIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY-------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 320 typelaeefklaisgklpknykdelprfelghngasRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSSETP 399
Cdd:PRK05899 284 ------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDY 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 400 EGKNVWFGVREFAMGAAVNGMAAHGGLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLA 479
Cdd:PRK05899 328 SGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 480 GLRAIPNMNVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLDVPEDvvEEGVRKGAYTVygsEETPEFLLLASGS 559
Cdd:PRK05899 408 SLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTAQ--EEGVAKGGYVL---RDDPDVILIATGS 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 560 EVSLAVEAAKDLEKQGKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTKRVAIEMASPLGWHKYVGTAGKVIAIDGFGASA 639
Cdd:PRK05899 483 EVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASA 562
|
650 660
....*....|....*....|...
gi 446403588 640 PGDLVVEKYGFTKENILNQVMSL 662
Cdd:PRK05899 563 PADELFKEFGFTVENIVAAAKEL 585
|
|
| PLN02790 |
PLN02790 |
transketolase |
14-662 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 897.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 14 RALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSG--SLELEELKQF 91
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGydSVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 92 RQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDLMEGISHEAASFA 171
Cdd:PLN02790 82 RQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 172 GHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGN-DLEEIDKAITTAK-SQEGPTIIEVKTTIGF 249
Cdd:PLN02790 162 GHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNtDYDEIRAAIKEAKaVTDKPTLIKVTTTIGY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 250 GSPNKAGTNGVHGAPLGEVERKLTFENYGLDPEKrFNVSEEVYEIFQnTMLKRANEDESQWNSLLEKYAETYPELAEEFK 329
Cdd:PLN02790 242 GSPNKANSYSVHGAALGEKEVDATRKNLGWPYEP-FHVPEDVKSHWS-KHTKEGAALEAEWNAKFAEYKKKYPEEAAELK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 330 LAISGKLPKNYKDELPRFELGHNG-ASRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSSETPEGKNVWFGV 408
Cdd:PLN02790 320 SLISGELPSGWEKALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 409 REFAMGAAVNGMAAHG-GLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLAGLRAIPNM 487
Cdd:PLN02790 400 REHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 488 NVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLDVPEdvvEEGVRKGAYTVYG--SEETPEFLLLASGSEVSLAV 565
Cdd:PLN02790 480 LMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTS---IEGVEKGGYVISDnsSGNKPDLILIGTGSELEIAA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 566 EAAKDLEKQGKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTKRVAIEMASPLGWHKYVGTAGKVIAIDGFGASAPGDLVV 645
Cdd:PLN02790 557 KAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGILY 636
|
650
....*....|....*..
gi 446403588 646 EKYGFTKENILNQVMSL 662
Cdd:PLN02790 637 KEFGFTVENVVAAAKSL 653
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
1-662 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 819.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 1 MFNEKDQLAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVS 80
Cdd:PTZ00089 1 MDGAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 81 G-SLELEELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDL 159
Cdd:PTZ00089 81 GyDLSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 160 MEGISHEAASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGN-DLEEIDKAITTAKSQEG- 237
Cdd:PTZ00089 161 QEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSKGk 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 238 PTIIEVKTTIGFGSpNKAGTNGVHGAPLGEVERKLTFENYGLDPEKRFNVSEEVYEIFQNTMLKRANEDEsQWNSLLEKY 317
Cdd:PTZ00089 241 PKLIIVKTTIGYGS-SKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQHVEKKKENYE-AWKKRFAKY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 318 AETYPELAEEFKLAISGKLPKNYKDELPRFEL-GHNGASRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDYSS 396
Cdd:PTZ00089 319 TAAFPKEAQAIERRFKGELPPGWEKKLPKYTTnDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 397 ETPEGKNVWFGVREFAMGAAVNGMAAHGGLHPYGATFFVFSDYLKPALRLSSIMGLNATFIFTHDSIAVGEDGPTHEPIE 476
Cdd:PTZ00089 399 ASPEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 477 QLAGLRAIPNMNVIRPADGNETRVAWEVALESESTPTSLVLTRQNLPVLdvpEDVVEEGVRKGAYTVYGSEETPEFLLLA 556
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPL---PGSSIEGVLKGAYIVVDFTNSPQLILVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 557 SGSEVSLAVEAAKDLEKQgKSVRVVSMPNWNAFEQQSEEYKESVIPSSVTKRVAIEMASPLGWHKYvgtAGKVIAIDGFG 636
Cdd:PTZ00089 556 SGSEVSLCVEAAKALSKE-LNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKY---SHVHVGISGFG 631
|
650 660
....*....|....*....|....*.
gi 446403588 637 ASAPGDLVVEKYGFTKENILNQVMSL 662
Cdd:PTZ00089 632 ASAPANALYKHFGFTVENVVEKARAL 657
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
6-337 |
5.07e-172 |
|
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: 493.83 E-value: 5.07e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 6 DQLAVDTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSG-SLE 84
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGyDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 85 LEELKQFRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLAGKFNKEGYNVVDHYTYVLASDGDLMEGIS 164
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 165 HEAASFAGHNKLSKLVVLYDSNDISLDGELNKAFSENTKARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEG-PTIIEV 243
Cdd:pfam00456 162 SEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDkPTLIKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 244 KTTIGFGSPNKAGTNGVHGAPLGEVERKLTFENYGLDPEKRFNVSEEVYEIFQNTmLKRANEDESQWNSLLEKYAETYPE 323
Cdd:pfam00456 242 RTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEK-VAEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 446403588 324 LAEEFKLAISGKLP 337
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-273 |
1.24e-133 |
|
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: 392.64 E-value: 1.24e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 11 DTLRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSGSLELEELKQ 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 91 FRQWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDHLagkfnkegynVVDHYTYVLASDGDLMEGISHEAASF 170
Cdd:cd02012 81 FRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAASF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 171 AGHNKLSKLVVLYDSNDISLDGELNK-AFSENTKARFEAYGWNYLLVkDGNDLEEIDKAITTAKSQEG-PTIIEVKTTIG 248
Cdd:cd02012 151 AGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGkPTLIIAKTIKG 229
|
250 260
....*....|....*....|....*
gi 446403588 249 FGSPNKAGTNGVHGAPLGEVERKLT 273
Cdd:cd02012 230 KGVPFMENTAKWHGKPLGEEEVELA 254
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
13-250 |
1.40e-65 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 217.25 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 13 LRALSIDTIEKANSGHPGLPMGAAPMAYTLWTRHLNFNPQSKDYFNRDRFVLSAGHGSALLYSLLHVSGSLELEELKQFR 92
Cdd:COG3959 15 IRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKGYFPKEELATFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 93 QWGSKTPGHPEYRHTDGVEVTTGPLGQGFAMSVGLAlaedhLAGKFNKEGYNVvdhytYVLASDGDLMEGISHEAASFAG 172
Cdd:COG3959 95 KLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMA-----LAAKLDGKDYRV-----YVLLGDGELQEGQVWEAAMAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 173 HNKLSKLVVLYDSNDISLDGELNKAFS-ENTKARFEAYGWNYLLVkDGNDLEEIDKAITTAKSQEG-PTIIEVKTTIGFG 250
Cdd:COG3959 165 HYKLDNLIAIVDRNGLQIDGPTEDVMSlEPLAEKWEAFGWHVIEV-DGHDIEALLAALDEAKAVKGkPTVIIAHTVKGKG 243
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
359-519 |
4.11e-61 |
|
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: 200.75 E-value: 4.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 359 SGTVIQAISKTVPSFFGGSADLAGSNKsnvndaTDYSSETPEGKNVWFGVREFAMGAAVNGMAAHGgLHPYGATFFVFSD 438
Cdd:cd07033 3 FGEALLELAKKDPRIVALSADLGGSTG------LDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 439 YLKPALR-LSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLAGLRAIPNMNVIRPADGNETRVAWEVALESEStPTSLVL 517
Cdd:cd07033 76 RAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDG-PVYIRL 154
|
..
gi 446403588 518 TR 519
Cdd:cd07033 155 PR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
354-524 |
1.67e-52 |
|
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: 178.51 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 354 ASRADSGTVIQAISKTVPSFFGGSADLAGSNKSNVNDATDyssETPEGKNVWFGVREFAMGAAVNGMAAHGG-LHPYGAT 432
Cdd:pfam02779 4 ATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLH---PQGAGRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 433 FFVFSDYLKPALR-LSSIMGLNATFIFTHDSIAVGEDGPTHEPIEQLAGLRAIPNMNVIRPADGNETRVAWEVALESES- 510
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|....
gi 446403588 511 TPTSLVLTRQNLPV 524
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
404-523 |
1.67e-37 |
|
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: 136.08 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 404 VWFGVREFAMGAAVNGMAAHGgLHPYGATFFVFSDYLKPALRLSSIMGlNATFIFTHDS-IAVGEDGPTHEPIEQLAGLR 482
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHG-LRPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446403588 483 AIPNMNVIRPADGNETRVAWEVALESEsTPTSLVLTRQNLP 523
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDD-GPVVIRLERKSLY 135
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
360-662 |
2.78e-28 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 115.57 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 360 GTVIQAISKTVPSFFGGSADLAGSNKSN----------VNdatdyssetpegknvwFGVREFAM-GAAVnGMAAhGGLHP 428
Cdd:COG3958 11 GEALVELAEEDPDIVVLDADLGGSTKLDkfakafpdrfFN----------------VGIAEQNMvGVAA-GLAL-AGKIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 429 YGATFFVFSdYLKPA--LRLS-SIMGLNATFIFTHDSIAVGEDGPTHEPIEQLAGLRAIPNMNVIRPADGNETRVAWEVA 505
Cdd:COG3958 73 FVSTFAPFL-TGRAYeqIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 506 LESEStPTSLVLTRQNLPVLDVPEDVVEEG----VRKGAytvygseetpEFLLLASGSEVSLAVEAAKDLEKQGKSVRVV 581
Cdd:COG3958 152 AEHDG-PVYLRLGRGAVPVVYDEDYEFEIGkarvLREGK----------DVTIIATGIMVAEALEAAELLAKEGISARVI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 582 SMP-----NWNAFEQQSEEYK-----E--SVI---PSSVTKRVAIEMASPLgwhKYVGTAgkviaiDGFGASAPGDLVVE 646
Cdd:COG3958 221 NMHtikplDEEAILKAARKTGavvtaEehSIIgglGSAVAEVLAENYPVPL---RRIGVP------DRFGESGSPEELLE 291
|
330
....*....|....*.
gi 446403588 647 KYGFTKENILNQVMSL 662
Cdd:COG3958 292 KYGLDAEGIVAAAKEL 307
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
3-583 |
9.36e-18 |
|
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: 87.14 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 3 NEKDQLA--VDTLRALSIDTIEkANSGHPGLPMGAAPMAYTLwtrHLNFNPQskdyfnRDRFVLSAGHgSALLYSLLHVS 80
Cdd:TIGR00204 13 LSIDELEklCDELRRYLLESVS-ASGGHLASGLGTVELTVAL---HYVFNTP------KDQFIWDVGH-QAYPHKLLTGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 81 GslelEELKQFRQW----GSKTPGHPEYRHtdgveVTTGPLGQGFAMSVGLALAEDhlagkfnKEGynvVDHYTYVLASD 156
Cdd:TIGR00204 82 R----EKFSTLRQKkglhGFPKRSESEYDV-----FSAGHSSTSISAGLGIAVAAE-------KKG---ADRKTVCVIGD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 157 GDLMEGISHEAASFAGHNKLSKLVVLYDsNDISLD---GELNKAFS------------------------------ENTK 203
Cdd:TIGR00204 143 GAITAGMAFEALNHAGDLKTDMIVILND-NEMSISenvGALSNHLAqlrsgslyqslrdglkkifsklppiknylaKRTE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 204 ----------ARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEGPTIIEVKTTIGFG-SPNKAGTNGVHGAPLGEVERKL 272
Cdd:TIGR00204 222 esmkglvvpgTFFEELGFNYIGPVDGHDLLELIETLKNAKKLKGPVFLHIQTKKGKGyKPAEKDPIGWHGVGPFDLSTGC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 273 TFENYGLDPEKRfnvseevyEIFQNTMLKRANEDESQwnsllekyaetypelaeefkLAISGKLPknykdelprfelghn 352
Cdd:TIGR00204 302 LPKSKSALPSYS--------KIFSDTLCELAKKDNKI--------------------VGITPAMP--------------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 353 gasradSGTVIQAISKTVP-SFFggsaDLAGSNKSNVNDATdyssetpegknvwfgvrefamgaavnGMAAhGGLHPYGA 431
Cdd:TIGR00204 339 ------EGSGLDKFSRKFPdRYF----DVAIAEQHAVTFAA--------------------------GMAI-EGYKPFVA 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 432 tffVFSDYLKPA----LRLSSIMGLNATFIFTHDSIaVGEDGPTHEPIEQLAGLRAIPNMNVIRPADGNETRVAWEVALE 507
Cdd:TIGR00204 382 ---IYSTFLQRAydqvVHDVCIQKLPVLFAIDRAGI-VGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYH 457
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446403588 508 SESTPTSLVLTRQNlpVLDVPEDVVEEGVRKGAYTVYGSEEtpEFLLLASGSEVSLAVEAAKDLEKQGKSVRVVSM 583
Cdd:TIGR00204 458 YDDGPIAVRYPRGN--AVGVELTPEPEKLPIGKSEVLRKGE--KILILGFGTLVPEALEVAESLNEKGIEATVVDA 529
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
125-583 |
7.15e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 81.28 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 125 VGLALAEDHLagkfNKEGYNVVdhytyVLASDGDLMEGISHEAASFAGHNKLSKLVVLYDsNDISLD---GELNKAFSEN 201
Cdd:PRK05444 127 LGMAKARDLK----GGEDRKVV-----AVIGDGALTGGMAFEALNNAGDLKSDLIVILND-NEMSISpnvGALSNYLARL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 202 -TKARFEAYGWNYLLVKDGNDLEEIDKAITTAKSQEGPTIIEVKTTIGFG-SPNKAGTNGVHGAPLGEVErklTFEnygl 279
Cdd:PRK05444 197 rSSTLFEELGFNYIGPIDGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGyAPAEADPIKYHGVGKFDPE---TGE---- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 280 dPEKRFNVSEEVY-EIFQNTMLKRANEDEsqwnsllekyaetypelaeefKL-AISGKLPknykdelprfelghngasra 357
Cdd:PRK05444 270 -QPKSSKPGKPSYtKVFGETLCELAEKDP---------------------KIvAITAAMP-------------------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 358 dSGTVIQAISKTVPS-FFggsaDLAGSnksnvndatdyssetpEGKNVWFgvrefamgAAvnGMAAhGGLHPYGA---TF 433
Cdd:PRK05444 308 -EGTGLVKFSKRFPDrYF----DVGIA----------------EQHAVTF--------AA--GLAT-EGLKPVVAiysTF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 434 F------VFSDYlkpalrlsSIMGLNATF------IfthdsiaVGEDGPTHEPIEQLAGLRAIPNMNVIRPADGNETR-- 499
Cdd:PRK05444 356 LqraydqVIHDV--------ALQNLPVTFaidragL-------VGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRqm 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 500 VAWevALESESTPTSLVLTRQNLPVLDVPE-DVVEEGvrKGAYTVYGSeetpEFLLLASGSEVSLAVEAAKDLEkqgkSV 578
Cdd:PRK05444 421 LYT--ALAYDDGPIAIRYPRGNGVGVELPElEPLPIG--KGEVLREGE----DVAILAFGTMLAEALKAAERLA----SA 488
|
....*
gi 446403588 579 RVVSM 583
Cdd:PRK05444 489 TVVDA 493
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
3-611 |
5.27e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 72.06 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 3 NEKDQLAvDTLRALSIDTIEKAnSGHPGLPMGAAPMAYTLwtrHLNFN-PqskdyfnRDRFVLSAGHGSaLLYSLLHVSG 81
Cdd:PRK12571 24 AELEQLA-DELRAEVISAVSET-GGHLGSSLGVVELTVAL---HAVFNtP-------KDKLVWDVGHQC-YPHKILTGRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 82 slelEELKQFRQWG--SKTPGHPEYRHtDGVEV--TTGPLGQGFAMSVGLALAEDhlagkfnkegynvVDHYTYVLAsDG 157
Cdd:PRK12571 91 ----DRFRTLRQKGglSGFTKRSESEY-DPFGAahSSTSISAALGFAKARALGQP-------------DGDVVAVIG-DG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 158 DLMEGISHEAASFAGHNKlSKLVVLYDSNDISLD---GELNKAFSE--------NTKAR--------------------- 205
Cdd:PRK12571 152 SLTAGMAYEALNNAGAAD-RRLIVILNDNEMSIAppvGALAAYLSTlrssdpfaRLRAIakgveerlpgplrdgarrare 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 206 -----------FEAYGWNYLLVKDGNDLEEIDKAITTAKSQ-EGPTIIEVKTTIGFG-SPNKAGTNGVHGAPLGEVERKL 272
Cdd:PRK12571 231 lvtgmigggtlFEELGFTYVGPIDGHDMEALLSVLRAARARaDGPVLVHVVTEKGRGyAPAEADEDKYHAVGKFDVVTGL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 273 tfenygldPEKRFNVSEEVYEIFQNTMLKRANEDESqwnsllekyaetypelaeefKLAISGKLPknykdelprfelghn 352
Cdd:PRK12571 311 --------QKKSAPSAPSYTSVFGEELTKEAAEDSD--------------------IVAITAAMP--------------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 353 gasradSGTVIQAISKTVPSffggsadlagsnksNVNDAtdyssetpegknvwfGVREFAMGAAVNGMAAhGGLHPYGAt 432
Cdd:PRK12571 348 ------LGTGLDKLQKRFPN--------------RVFDV---------------GIAEQHAVTFAAGLAA-AGLKPFCA- 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 433 ffVFSDYLKPA----LRLSSIMGLNATFIFTHDSIaVGEDGPTHEPIEQLAGLRAIPNMNVIRPADGNETRVAWEVALES 508
Cdd:PRK12571 391 --VYSTFLQRGydqlLHDVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAH 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 509 ESTPTSLVLTRQNLPVLDVPEDVVEEGVRKGaytvYGSEETPEFLLLASGSEVSLAVEAAKDLEKQGKSVRVVSmPNWna 588
Cdd:PRK12571 468 DDGPIAVRFPRGEGVGVEIPAEGTILGIGKG----RVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVAD-PRF-- 540
|
650 660
....*....|....*....|...
gi 446403588 589 feqqSEEYKESVIPSSVTKRVAI 611
Cdd:PRK12571 541 ----VKPLDEALTDLLVRHHIVV 559
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
415-583 |
6.66e-12 |
|
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440768 [Multi-domain] Cd Length: 623 Bit Score: 68.50 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 415 AAvnGMAAhGGLHPYGA---TFF------VFSDYlkpalrlsSIMGLNATFifthdsiA------VGEDGPTHEPIEQLA 479
Cdd:COG1154 375 AA--GLAT-EGLKPVVAiysTFLqraydqVIHDV--------ALQNLPVTF-------AidraglVGADGPTHHGVFDLS 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 480 GLRAIPNMNVIRPADGNETRVAWEVALESEStPTSLVLTRQNLPVLDVPEDVVE------EGVRKGAytvygseetpEFL 553
Cdd:COG1154 437 YLRCIPNMVIMAPKDENELRHMLYTALAYDG-PTAIRYPRGNGPGVELPAELEPlpigkgEVLREGK----------DVA 505
|
170 180 190
....*....|....*....|....*....|
gi 446403588 554 LLASGSEVSLAVEAAKDLEKQGKSVRVVSM 583
Cdd:COG1154 506 ILAFGTMVAEALEAAERLAAEGISATVVDA 535
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
548-655 |
2.18e-11 |
|
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: 61.46 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 548 ETPEFLLLASGSEVSLAVEAAKDLEKQGKSVRVVSMP-----NWNAFEQQSEEYKESVIPSSVTKRVAI--EMASPLGWH 620
Cdd:pfam02780 8 EGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRtikplDKETILESVKKTGRLVTVEEAVPRGGFgsEVAAALAEE 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 446403588 621 KYVGTAGKVIAIDG--FGASAPGDLVVEKYGFTKENI 655
Cdd:pfam02780 88 AFDGLDAPVLRVGGpdFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
125-250 |
7.59e-11 |
|
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: 61.79 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 125 VGLALAEDhLAGKfnkeGYNVVdhytyVLASDGDLMEGISHEAASFAGHNKlSKLVVLYDSNDISLdgelnkafSENTKA 204
Cdd:cd02007 85 LGMAVARD-LKGK----KRKVI-----AVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSI--------SPNVGT 145
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446403588 205 R---FEAYGWNYLLVKDGNDLEEIDKAITTAKSQEGPTIIEVKTTIGFG 250
Cdd:cd02007 146 PgnlFEELGFRYIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGKG 194
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
67-224 |
7.25e-09 |
|
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: 58.08 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 67 GHGSALLYSLLHVSGSLELEELKQFRQWGSKtPGHPEYRHT----DGVEVTTGPLGQGFAMSVGLALAEDHLAGKfnkeG 142
Cdd:cd02017 67 GHASPGIYARAFLEGRLTEEQLDNFRQEVGG-GGLSSYPHPwlmpDFWEFPTVSMGLGPIQAIYQARFNRYLEDR----G 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 143 YNV-VDHYTYVLASDGDLMEGISHEAASFAGHNKLSKLVVLYDSNDISLDGELnkafSENTK------ARFEAYGWNYLL 215
Cdd:cd02017 142 LKDtSDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPV----RGNGKiiqeleGIFRGAGWNVIK 217
|
....*....
gi 446403588 216 VKDGNDLEE 224
Cdd:cd02017 218 VIWGSKWDE 226
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
105-245 |
1.29e-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: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 105 RHTDGVEVTTGPLGQGFAMSVGLALAEDhlagkfnkegynvvDHYTYVLASDGDLMEGIShEAASFAGHNklSKLVVLYD 184
Cdd:cd00568 36 GRRFLTSTGFGAMGYGLPAAIGAALAAP--------------DRPVVCIAGDGGFMMTGQ-ELATAVRYG--LPVIVVVF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446403588 185 SND--ISLDGELNKAFSENT----------KARFEAYGWNYLLVkdgNDLEEIDKAITTAKSQEGPTIIEVKT 245
Cdd:cd00568 99 NNGgyGTIRMHQEAFYGGRVsgtdlsnpdfAALAEAYGAKGVRV---EDPEDLEAALAEALAAGGPALIEVKT 168
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
114-245 |
4.48e-07 |
|
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: 52.11 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 114 TGPLGQGFAMSVGLALAeDHLAGKfnkegynvvDHYTYVLASDGDLMEGISHEAASFAGHNKLSKLVVLYDsNDISLDGE 193
Cdd:cd02000 103 NGIVGGQVPLAAGAALA-LKYRGE---------DRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTP 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446403588 194 LNKAFSENT-KARFEAYGWNYLLVkDGNDLEEI----DKAITTAKSQEGPTIIEVKT 245
Cdd:cd02000 172 TSRQTAGTSiADRAAAYGIPGIRV-DGNDVLAVyeaaKEAVERARAGGGPTLIEAVT 227
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-574 |
6.09e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 52.70 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 122 AMSVGLALAEDhlagkFNKEGYNVVdhytyVLASDGDLMEGISHEAASFAGHNKlSKLVVLYDSNDISLD---GELNKAF 198
Cdd:PRK12315 120 ALATGLAKARD-----LKGEKGNII-----AVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAenhGGLYKNL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 199 SE--NTKAR-----FEAYGWNYLLVKDGNDLEEIDKAITTAKSQEGPTIIEVKTTIGFG-SPNKAGTNGVH-GAPL---- 265
Cdd:PRK12315 189 KElrDTNGQsennlFKAMGLDYRYVEDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKGyQPAEENKEAFHwHMPFdlet 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 266 GEVERKLTFENYGldpekrfnvseevyEIFQNTMLKRANEDESqwnsllekyaetypelaeefklaisgklpknykdelp 345
Cdd:PRK12315 269 GQSKVPASGESYS--------------SVTLDYLLKKIKEGKP------------------------------------- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 346 rfelghngasradsgtvIQAISKTVPSFFGGS--ADLAGSNKSNVNDATDYSsetpegknvwfgvreFAMGAavnGMAAH 423
Cdd:PRK12315 298 -----------------VVAINAAIPGVFGLKefRKKYPDQYVDVGIAEQES---------------VAFAS---GIAAN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 424 GGLhpygATFFVFSDYLKPAL-RLSSIMGLN---ATFIFTHDSIavGEDGPTHEPIEQLAGLRAIPNMNVIRPADGNETR 499
Cdd:PRK12315 343 GAR----PVIFVNSTFLQRAYdQLSHDLAINnnpAVMIVFGGSI--SGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELI 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446403588 500 VAWEVALESESTPtslVLTRQnlPVLDVPED-VVEEGVRKGAYTVYGSEEtpEFLLLASGSEVSLAVEAAKDLEKQ 574
Cdd:PRK12315 417 AMLEWALTQHEHP---VAIRV--PEHGVESGpTVDTDYSTLKYEVTKAGE--KVAILALGDFYELGEKVAKKLKEE 485
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
11-252 |
1.38e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 45.09 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 11 DTLRALSIDTIEKAnSGHPGLPMGAAPMAYTLwtrHLNFN-PQskdyfnrDRFVLSAGHGSALLYSLLHVSGsleleELK 89
Cdd:PLN02234 89 DELRSDVIFNVSKT-GGHLGSNLGVVELTVAL---HYIFNtPH-------DKILWDVGHQSYPHKILTGRRG-----KMK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 90 QFRQWGSKTpGHPEYRHTDGVEVTTGPLGQGFAMSVGLALAEDhLAGKFNKegynvvdhyTYVLASDGDLMEGISHEAAS 169
Cdd:PLN02234 153 TIRQTNGLS-GYTKRRESEHDSFGTGHSSTTLSAGLGMAVGRD-LKGMNNS---------VVSVIGDGAMTAGQAYEAMN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446403588 170 FAGHNKLSKLVVLYDSNDISLD-----------GELNKAFS----------ENTKARFEAYGWNYLLVKDGNDLEEIDKA 228
Cdd:PLN02234 222 NAGYLHSNMIVILNDNKQVSLPtanldgptqpvGALSCALSrlqsncgmirETSSTLFEELGFHYVGPVDGHNIDDLVSI 301
|
250 260
....*....|....*....|....*.
gi 446403588 229 ITTAKSQE--GPTIIEVKTTIGFGSP 252
Cdd:PLN02234 302 LETLKSTKtiGPVLIHVVTEKGRGYP 327
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
515-587 |
1.77e-04 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 44.92 E-value: 1.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446403588 515 LVLTRQNLPVLDVPEDVvEEGVRKGAYTVYGSEETPEFLLLASGSEVSLAVEAAKDLEKQ-GKSVRVVSMPNWN 587
Cdd:PRK13012 699 LTVMNENYAQPALPEGA-EEGILKGMYRLAAAAEAPRVQLLGSGAILREVLAAARLLADDwGVDADVWSVTSFT 771
|
|
| aceE |
PRK09405 |
pyruvate dehydrogenase subunit E1; Reviewed |
528-587 |
7.63e-03 |
|
pyruvate dehydrogenase subunit E1; Reviewed
Pssm-ID: 236500 [Multi-domain] Cd Length: 891 Bit Score: 39.36 E-value: 7.63e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446403588 528 PEDVvEEGVRKGAY---TVYGSEETPEFLLLASGSEVSLAVEAAKDLEKQ-GKSVRVVSMPNWN 587
Cdd:PRK09405 704 PEGA-EEGILKGMYkleTAEGKKGKPKVQLLGSGTILREVLEAAEILAEDyGVAADVWSVTSFN 766
|
|
| |
