|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
4-627 |
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: 945.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 4 QILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYD 82
Cdd:COG0021 2 PLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLwTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 83 LNLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEG 158
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGIANAVGMAIAERHlaARfNRPGHDIVDHYTYVIAGDGDLMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 159 ISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSI-NGHDYEEINKALEQAKKST-KPCLI 236
Cdd:COG0021 162 ISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVeDGHDLEAIDAAIEAAKAETdKPTLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 237 IAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK-- 314
Cdd:COG0021 242 ICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPE-PFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAAyp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 315 ---ELLERLLNP----DFNKiAYPDFK--GKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDFV----E 381
Cdd:COG0021 321 elaAELERRLAGelpeDWDA-ALPAFEadAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSpedpS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 382 GKNIHFGIREHAMAAINNAFARYGIFLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLST 461
Cdd:COG0021 400 GRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLAS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 462 FRAMPNFLTFRPADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL--NEPVFGDVKNGAYLLKESK-EAKFTLLASGSEV 537
Cdd:COG0021 480 LRAIPNLDVIRPADANETAAAWKLALeRKDGPTALILSRQNLPTLdrTAAAAEGVAKGAYVLADAEgTPDVILIATGSEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 538 WLCLESANELEKQGFACNVVSMPCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKD 611
Cdd:COG0021 560 SLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVrarVAVEAGVTDGWYKYvglDGAVIGIDTFGASAPA 639
|
650
....*....|....*.
gi 949779181 612 KDVFERFGFSVSKLVN 627
Cdd:COG0021 640 KVLFEEFGFTVENVVA 655
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-631 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 882.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 1 MNIQILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLS 79
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLwTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 80 GYDLNLEDLKNFRQLHSKTPGHPEI-STLGVEIATGPLGQGVANAVGFAMAAKKAQNLLGSD---LIDHKIYCLCGDGDL 155
Cdd:PRK05899 83 GYDLSIDDLKNFRQLGSKTPGHPEYgHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPgldIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 156 QEGISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSINGHDYEEINKALEQAKKSTKPCL 235
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKASTKPTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 236 IIAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPnisfhipqaskirfesavelgdleeakwkdkleksakke 315
Cdd:PRK05899 243 IIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY--------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 316 llerllnpdfnkiaypdfkgkdlatRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDFVE----GKNIHFGIRE 391
Cdd:PRK05899 284 -------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPedysGRYIHYGVRE 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 392 HAMAAINNAFARYGIFLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNFLTF 471
Cdd:PRK05899 339 FAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVI 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 472 RPADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL-NEPVFGDVKNGAYLLKEskEAKFTLLASGSEVWLCLESANELEK 549
Cdd:PRK05899 419 RPADANETAAAWKYALeRKDGPSALVLTRQNLPVLeRTAQEEGVAKGGYVLRD--DPDVILIATGSEVHLALEAADELEA 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 550 QGFACNVVSMPCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKDKDVFERFGFSVS 623
Cdd:PRK05899 497 EGIKVRVVSMPSTELFDEQDAAYKESVLPAAVtarVAVEAGVADGWYKYvglDGKVLGIDTFGASAPADELFKEFGFTVE 576
|
....*...
gi 949779181 624 KLVNFILS 631
Cdd:PRK05899 577 NIVAAAKE 584
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
10-627 |
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: 809.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 10 ANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDLNLEDL 88
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLwTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIEDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 89 KNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKKAQNL---LGSDLIDHKIYCLCGDGDLQEGISYEAC 164
Cdd:TIGR00232 84 KQFRQLHSKTPGHPEYGhTAGVEATTGPLGQGIANAVGMAIAEKTLAATfnkPGFEIVDHYTYVFVGDGCLQEGISYEVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 165 SLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVL-SINGHDYEEINKALEQAKKST-KPCLIIAKTTI 242
Cdd:TIGR00232 164 SLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTdKPTLIEVKTTI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 243 AKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRF-ESAVELGDLEEAKWKDKLEKSAKK-----EL 316
Cdd:TIGR00232 244 GFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYN-PFEIPQEVYDHFkKTVKERGAKAEQEWNELFAAYKKKypelaAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 317 LERLLNPDFNK---IAYPDF--KGKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDFVE---GKNIHFG 388
Cdd:TIGR00232 323 FTRRLSGELPAdwdKQLPEFkvKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHEnplGNYIHYG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 389 IREHAMAAINNAFARYGIFLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNF 468
Cdd:TIGR00232 403 VREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPNL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 469 LTFRPADGVENVKAWQIALNA-DIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKESKEAKFTLLASGSEVWLCLESANEL 547
Cdd:TIGR00232 483 SVWRPCDGNETAAAWKYALESqDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAVEAAKKL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 548 EKQGFACNVVSMPCFELFEKQDKAYQERLLKGEV--IGVEAAHSNELYKFCHK---VYGIESFGESGKDKDVFERFGFSV 622
Cdd:TIGR00232 563 AAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVtrLAIEAGAADEWYKYAGLvgaILGMDSFGESAPGDKLFEEFGFTV 642
|
....*
gi 949779181 623 SKLVN 627
Cdd:TIGR00232 643 ENVVA 647
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-322 |
2.08e-142 |
|
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: 417.17 E-value: 2.08e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 5 ILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDL 83
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLfKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 84 NLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEGI 159
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGhTAGVEVTTGPLGQGIANAVGMAIAERNlaATyNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 160 SYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSIN-GHDYEEINKALEQAKKST-KPCLII 237
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEdGHDVEAIAAAIEEAKAEKdKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 238 AKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK--- 314
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAype 320
|
330
....*....|
gi 949779181 315 --ELLERLLN 322
Cdd:pfam00456 321 laAEFARRLS 330
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-269 |
5.60e-136 |
|
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: 397.65 E-value: 5.60e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 11 NTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDLnLEDLK 89
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLyFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLP-EEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 90 NFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKKaqnllgsDLIDHKIYCLCGDGDLQEGISYEACSLAG 168
Cdd:cd02012 80 TFRQLGSRLPGHPEYGlTPGVEVTTGSLGQGLSVAVGMALAEKL-------LGFDYRVYVLLGDGELQEGSVWEAASFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 169 LHKLDNFILIYDSNNISIEGDV-GLAFNENVKMRFEAQGFEVLSINGHDYEEINKALEQAKKST-KPCLIIAKTTIAKGA 246
Cdd:cd02012 153 HYKLDNLIAIVDSNRIQIDGPTdDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKgKPTLIIAKTIKGKGV 232
|
250 260
....*....|....*....|...
gi 949779181 247 GELEGSHKSHGAPLGEEVIKKAK 269
Cdd:cd02012 233 PFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
385-502 |
2.74e-33 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 124.14 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 385 IHFGIREHAMAAINNAFARYGiFLPFSATFFIFSEYLKPAARIAALMKiKHFFIFTHDS-IGVGEDGPTHQPIEQLSTFR 463
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHG-LRPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 949779181 464 AMPNFLTFRPADGVENVKAWQIALNADIPSAFVLSRQKL 502
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSL 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
4-627 |
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: 945.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 4 QILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYD 82
Cdd:COG0021 2 PLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLwTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 83 LNLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEG 158
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGIANAVGMAIAERHlaARfNRPGHDIVDHYTYVIAGDGDLMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 159 ISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSI-NGHDYEEINKALEQAKKST-KPCLI 236
Cdd:COG0021 162 ISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVeDGHDLEAIDAAIEAAKAETdKPTLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 237 IAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK-- 314
Cdd:COG0021 242 ICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPE-PFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAAyp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 315 ---ELLERLLNP----DFNKiAYPDFK--GKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDFV----E 381
Cdd:COG0021 321 elaAELERRLAGelpeDWDA-ALPAFEadAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSpedpS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 382 GKNIHFGIREHAMAAINNAFARYGIFLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLST 461
Cdd:COG0021 400 GRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLAS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 462 FRAMPNFLTFRPADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL--NEPVFGDVKNGAYLLKESK-EAKFTLLASGSEV 537
Cdd:COG0021 480 LRAIPNLDVIRPADANETAAAWKLALeRKDGPTALILSRQNLPTLdrTAAAAEGVAKGAYVLADAEgTPDVILIATGSEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 538 WLCLESANELEKQGFACNVVSMPCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKD 611
Cdd:COG0021 560 SLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVrarVAVEAGVTDGWYKYvglDGAVIGIDTFGASAPA 639
|
650
....*....|....*.
gi 949779181 612 KDVFERFGFSVSKLVN 627
Cdd:COG0021 640 KVLFEEFGFTVENVVA 655
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-631 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 882.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 1 MNIQILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLS 79
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLwTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 80 GYDLNLEDLKNFRQLHSKTPGHPEI-STLGVEIATGPLGQGVANAVGFAMAAKKAQNLLGSD---LIDHKIYCLCGDGDL 155
Cdd:PRK05899 83 GYDLSIDDLKNFRQLGSKTPGHPEYgHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPgldIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 156 QEGISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSINGHDYEEINKALEQAKKSTKPCL 235
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKASTKPTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 236 IIAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPnisfhipqaskirfesavelgdleeakwkdkleksakke 315
Cdd:PRK05899 243 IIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY--------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 316 llerllnpdfnkiaypdfkgkdlatRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDFVE----GKNIHFGIRE 391
Cdd:PRK05899 284 -------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPedysGRYIHYGVRE 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 392 HAMAAINNAFARYGIFLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNFLTF 471
Cdd:PRK05899 339 FAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVI 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 472 RPADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL-NEPVFGDVKNGAYLLKEskEAKFTLLASGSEVWLCLESANELEK 549
Cdd:PRK05899 419 RPADANETAAAWKYALeRKDGPSALVLTRQNLPVLeRTAQEEGVAKGGYVLRD--DPDVILIATGSEVHLALEAADELEA 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 550 QGFACNVVSMPCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKDKDVFERFGFSVS 623
Cdd:PRK05899 497 EGIKVRVVSMPSTELFDEQDAAYKESVLPAAVtarVAVEAGVADGWYKYvglDGKVLGIDTFGASAPADELFKEFGFTVE 576
|
....*...
gi 949779181 624 KLVNFILS 631
Cdd:PRK05899 577 NIVAAAKE 584
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
10-627 |
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: 809.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 10 ANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDLNLEDL 88
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLwTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIEDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 89 KNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKKAQNL---LGSDLIDHKIYCLCGDGDLQEGISYEAC 164
Cdd:TIGR00232 84 KQFRQLHSKTPGHPEYGhTAGVEATTGPLGQGIANAVGMAIAEKTLAATfnkPGFEIVDHYTYVFVGDGCLQEGISYEVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 165 SLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVL-SINGHDYEEINKALEQAKKST-KPCLIIAKTTI 242
Cdd:TIGR00232 164 SLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTdKPTLIEVKTTI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 243 AKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRF-ESAVELGDLEEAKWKDKLEKSAKK-----EL 316
Cdd:TIGR00232 244 GFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYN-PFEIPQEVYDHFkKTVKERGAKAEQEWNELFAAYKKKypelaAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 317 LERLLNPDFNK---IAYPDF--KGKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDFVE---GKNIHFG 388
Cdd:TIGR00232 323 FTRRLSGELPAdwdKQLPEFkvKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHEnplGNYIHYG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 389 IREHAMAAINNAFARYGIFLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNF 468
Cdd:TIGR00232 403 VREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPNL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 469 LTFRPADGVENVKAWQIALNA-DIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKESKEAKFTLLASGSEVWLCLESANEL 547
Cdd:TIGR00232 483 SVWRPCDGNETAAAWKYALESqDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAVEAAKKL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 548 EKQGFACNVVSMPCFELFEKQDKAYQERLLKGEV--IGVEAAHSNELYKFCHK---VYGIESFGESGKDKDVFERFGFSV 622
Cdd:TIGR00232 563 AAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVtrLAIEAGAADEWYKYAGLvgaILGMDSFGESAPGDKLFEEFGFTV 642
|
....*
gi 949779181 623 SKLVN 627
Cdd:TIGR00232 643 ENVVA 647
|
|
| PLN02790 |
PLN02790 |
transketolase |
14-627 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 703.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 14 RFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYD-LNLEDLKNF 91
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLyDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 92 RQLHSKTPGHPE-ISTLGVEIATGPLGQGVANAVGFAMAAKKAQ---NLLGSDLIDHKIYCLCGDGDLQEGISYEACSLA 167
Cdd:PLN02790 82 RQWGSRTPGHPEnFETPGIEVTTGPLGQGIANAVGLALAEKHLAarfNKPDHKIVDHYTYCILGDGCQMEGISNEAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 168 GLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSING--HDYEEINKALEQAKKST-KPCLIIAKTTIAK 244
Cdd:PLN02790 162 GHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTdKPTLIKVTTTIGY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 245 GAGELEGSHKSHGAPLGEEVIKKAKEQAGFdPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK--EL---LER 319
Cdd:PLN02790 242 GSPNKANSYSVHGAALGEKEVDATRKNLGW-PYEPFHVPEDVKSHWSKHTKEGAALEAEWNAKFAEYKKKypEEaaeLKS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 320 LLN---PDFNKIAYPDFKGKD--LATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDF----VEGKNIHFGIR 390
Cdd:PLN02790 321 LISgelPSGWEKALPTFTPEDpaDATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFqkdtPEERNVRFGVR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 391 EHAMAAINNAFARYGI-FLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNFL 469
Cdd:PLN02790 401 EHGMGAICNGIALHSSgLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNIL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 470 TFRPADGVENVKAWQIA-LNADIPSAFVLSRQKLKALNEPVFGDVKNGAYLLK-ESKEAK--FTLLASGSEVWLCLESAN 545
Cdd:PLN02790 481 MLRPADGNETAGAYKVAvTNRKRPTVLALSRQKVPNLPGTSIEGVEKGGYVISdNSSGNKpdLILIGTGSELEIAAKAAK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 546 ELEKQGFACNVVSMPCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKDKDVFERFG 619
Cdd:PLN02790 561 ELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVtarVSVEAGSTFGWEKYvgsKGKVIGVDRFGASAPAGILYKEFG 640
|
....*...
gi 949779181 620 FSVSKLVN 627
Cdd:PLN02790 641 FTVENVVA 648
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
1-630 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 696.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 1 MNIQILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLS 79
Cdd:PTZ00089 1 MDGAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILwSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 80 GYDLNLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKKAQ---NLLGSDLIDHKIYCLCGDGDL 155
Cdd:PTZ00089 81 GYDLSMEDLKNFRQLGSRTPGHPERHiTPGVEVTTGPLGQGIANAVGLAIAEKHLAakfNRPGHPIFDNYVYVICGDGCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 156 QEGISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSI-NGH-DYEEINKALEQAKKST-K 232
Cdd:PTZ00089 161 QEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVdNGNtDFDGLRKAIEEAKKSKgK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 233 PCLIIAKTTIAKGAgELEGSHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSA 312
Cdd:PTZ00089 241 PKLIIVKTTIGYGS-SKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 313 KK-----ELLERL----LNPDFNKiAYPDFKGKD--LATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGDFV- 380
Cdd:PTZ00089 320 AAfpkeaQAIERRfkgeLPPGWEK-KLPKYTTNDkaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTk 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 381 ---EGKNIHFGIREHAMAAINNAFARYGIFLPFSATFFIFSEYLKPAARIAALMKIKHFFIFTHDSIGVGEDGPTHQPIE 457
Cdd:PTZ00089 399 aspEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 458 QLSTFRAMPNFLTFRPADGVENVKAWQIAL-NADIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKE-SKEAKFTLLASGS 535
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALaNAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDfTNSPQLILVASGS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 536 EVWLCLESANELEKQgFACNVVSMPCFELFEKQDKAYQERLLKGE---VIGVEAAHSNELYKFCHKVYGIESFGESGKDK 612
Cdd:PTZ00089 559 EVSLCVEAAKALSKE-LNVRVVSMPCWELFDQQSEEYQQSVLPSGgvpVLSVEAYVSFGWEKYSHVHVGISGFGASAPAN 637
|
650
....*....|....*...
gi 949779181 613 DVFERFGFSVSKLVNFIL 630
Cdd:PTZ00089 638 ALYKHFGFTVENVVEKAR 655
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-322 |
2.08e-142 |
|
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: 417.17 E-value: 2.08e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 5 ILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDL 83
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLfKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 84 NLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEGI 159
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGhTAGVEVTTGPLGQGIANAVGMAIAERNlaATyNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 160 SYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVKMRFEAQGFEVLSIN-GHDYEEINKALEQAKKST-KPCLII 237
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEdGHDVEAIAAAIEEAKAEKdKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 238 AKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK--- 314
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAype 320
|
330
....*....|
gi 949779181 315 --ELLERLLN 322
Cdd:pfam00456 321 laAEFARRLS 330
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-269 |
5.60e-136 |
|
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: 397.65 E-value: 5.60e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 11 NTLRFLSADMVQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDLnLEDLK 89
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLyFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLP-EEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 90 NFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKKaqnllgsDLIDHKIYCLCGDGDLQEGISYEACSLAG 168
Cdd:cd02012 80 TFRQLGSRLPGHPEYGlTPGVEVTTGSLGQGLSVAVGMALAEKL-------LGFDYRVYVLLGDGELQEGSVWEAASFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 169 LHKLDNFILIYDSNNISIEGDV-GLAFNENVKMRFEAQGFEVLSINGHDYEEINKALEQAKKST-KPCLIIAKTTIAKGA 246
Cdd:cd02012 153 HYKLDNLIAIVDSNRIQIDGPTdDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKgKPTLIIAKTIKGKGV 232
|
250 260
....*....|....*....|...
gi 949779181 247 GELEGSHKSHGAPLGEEVIKKAK 269
Cdd:cd02012 233 PFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
1-271 |
1.73e-86 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 271.18 E-value: 1.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 1 MNIQILQEQANTLRFLSADMVQKANSGHPGAPLGLADILSVLSYH-LKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLS 79
Cdd:COG3959 3 EDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKvMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 80 GYdLNLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFAMAAKkaqnLLGSDlidHKIYCLCGDGDLQEG 158
Cdd:COG3959 83 GY-FPKEELATFRKLGSRLQGHPDMKkTPGVEMSTGSLGQGLSVAVGMALAAK----LDGKD---YRVYVLLGDGELQEG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 159 ISYEACSLAGLHKLDNFILIYDSNNISIEGDV----GLafnENVKMRFEAQGFEVLSINGHDYEEINKALEQAKKST-KP 233
Cdd:COG3959 155 QVWEAAMAAAHYKLDNLIAIVDRNGLQIDGPTedvmSL---EPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKgKP 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 949779181 234 CLIIAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQ 271
Cdd:COG3959 232 TVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAE 269
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
342-499 |
3.60e-55 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 184.57 E-value: 3.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 342 DSNGEILNVLAKNLEGFLGGSADLGPSNKTELhsMGDFVEGKNIHFGIREHAMAAINNAFARYGiFLPFSATFFIFSEYL 421
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDK--FAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 949779181 422 KPAARI-AALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNFLTFRPADGVENVKAWQIALNADIPSAFVLSR 499
Cdd:cd07033 78 YDQIRHdVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
336-502 |
4.12e-49 |
|
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: 168.88 E-value: 4.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 336 KDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHSMGD-FVEGKNIHFGIREHAMAAINNAFARYGIFL-PFSAT 413
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHpQGAGRVIDTGIAEQAMVGFANGMALHGPLLpPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 414 FFIFSEYLKPAARI-AALMKIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNFLTFRPADGVENVKAW--QIALNAD 490
Cdd:pfam02779 81 FSDFLNRADDAIRHgAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAIRRDGR 160
|
170
....*....|..
gi 949779181 491 IPSAFVLSRQKL 502
Cdd:pfam02779 161 KPVVLRLPRQLL 172
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
385-502 |
2.74e-33 |
|
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
Pssm-ID: 214865 [Multi-domain] Cd Length: 136 Bit Score: 124.14 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 385 IHFGIREHAMAAINNAFARYGiFLPFSATFFIFSEYLKPAARIAALMKiKHFFIFTHDS-IGVGEDGPTHQPIEQLSTFR 463
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHG-LRPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 949779181 464 AMPNFLTFRPADGVENVKAWQIALNADIPSAFVLSRQKL 502
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSL 134
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
338-627 |
1.04e-21 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 95.92 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 338 LATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTElhsmgDFveGKN-----IHFGIREHAMAAINNAFARYGiFLPFSA 412
Cdd:COG3958 4 KAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLD-----KF--AKAfpdrfFNVGIAEQNMVGVAAGLALAG-KIPFVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 413 TFFIFSeylkpAARI-------AALMK--IKhfFIFTHDSIGVGEDGPTHQPIEQLSTFRAMPNFLTFRPADGVENVKAW 483
Cdd:COG3958 76 TFAPFL-----TGRAyeqirndIAYPNlnVK--IVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 484 QIALNADIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKESKEAkfTLLASGSEVWLCLESANELEKQGFACNVVSMPCF- 562
Cdd:COG3958 149 RAAAEHDGPVYLRLGRGAVPVVYDEDYEFEIGKARVLREGKDV--TIIATGIMVAEALEAAELLAKEGISARVINMHTIk 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949779181 563 ----ELFEKQDKAYQeRLLKGE---VIG-----VEAAHSNELYKFCHKVyGI-ESFGESGKDKDVFERFGFSVSKLVN 627
Cdd:COG3958 227 pldeEAILKAARKTG-AVVTAEehsIIGglgsaVAEVLAENYPVPLRRI-GVpDRFGESGSPEELLEKYGLDAEGIVA 302
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
13-190 |
4.22e-17 |
|
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: 83.51 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 13 LRFLSADMVQKANS------GHPGAPLGLADILSVLSYHLKHNPKNPtwLNRDrLVFSGGHASALLYSFLHLSGyDLNLE 86
Cdd:cd02017 11 IRWNAMAMVHRANKkdlgigGHIATFASAATLYEVGFNHFFRARGEG--GGGD-LVYFQGHASPGIYARAFLEG-RLTEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 87 DLKNFRQLHSKT-----PgHPEISTLGVEIATGPLGQGVANAVGFAMAAKKAQNLLGSDLIDHKIYCLCGDGDLQEGISY 161
Cdd:cd02017 87 QLDNFRQEVGGGglssyP-HPWLMPDFWEFPTVSMGLGPIQAIYQARFNRYLEDRGLKDTSDQKVWAFLGDGEMDEPESL 165
|
170 180
....*....|....*....|....*....
gi 949779181 162 EACSLAGLHKLDNFILIYDSNNISIEGDV 190
Cdd:cd02017 166 GAIGLAAREKLDNLIFVVNCNLQRLDGPV 194
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
111-247 |
1.00e-14 |
|
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: 72.96 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 111 IATGPLGQGVANAVGFAmaakKAQNLLGSDlidHKIYCLCGDGDLQEGISYEACSLAGlHKLDNFILIYDSNNISIEGDV 190
Cdd:cd02007 72 FGTGHSSTSISAALGMA----VARDLKGKK---RKVIAVIGDGALTGGMAFEALNNAG-YLKSNMIVILNDNEMSISPNV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 949779181 191 GLAFNenvkmRFEAQGFEVLS-INGHDYEEINKALEQAKKSTKPCLIIAKTTiaKGAG 247
Cdd:cd02007 144 GTPGN-----LFEELGFRYIGpVDGHNIEALIKVLKEVKDLKGPVLLHVVTK--KGKG 194
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
56-240 |
6.64e-11 |
|
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: 61.12 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 56 LNRDRLVFSG-GHASALLYSFLHLsgydlnledlknfrqlhsKTPGHPEISTlgveiATGPLGQGVANAVGFAMAAKkaq 134
Cdd:cd00568 10 LPEDAIVVNDaGNSAYWAYRYLPL------------------RRGRRFLTST-----GFGAMGYGLPAAIGAALAAP--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 135 nllgsdliDHKIYCLCGDGDLQEGISyeACSLAGLHKLdNFILIYDSNNISIEGDVGLA------------FNENVKMRF 202
Cdd:cd00568 64 --------DRPVVCIAGDGGFMMTGQ--ELATAVRYGL-PVIVVVFNNGGYGTIRMHQEafyggrvsgtdlSNPDFAALA 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 949779181 203 EAQGFEVLSINGHdyEEINKALEQAKKSTKPCLIIAKT 240
Cdd:cd00568 133 EAYGAKGVRVEDP--EDLEAALAEALAAGGPALIEVKT 168
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
123-247 |
9.67e-11 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 64.72 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 123 AVGFAMAAKkaqnLLGSDliDHKIYCLCGDGDLQEGISYEACSLAGlHKLDNFILIYDSNNISIEGDVGlAFNENV-KMR 201
Cdd:PRK05444 126 ALGMAKARD----LKGGE--DRKVVAVIGDGALTGGMAFEALNNAG-DLKSDLIVILNDNEMSISPNVG-ALSNYLaRLR 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 949779181 202 ----FEAQGFEVLS-INGHDYEEINKALEQAKKSTKPCLIIAKTTiaKGAG 247
Cdd:PRK05444 198 sstlFEELGFNYIGpIDGHDLDALIETLKNAKDLKGPVLLHVVTK--KGKG 246
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
112-318 |
2.46e-09 |
|
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: 58.66 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 112 ATGPLGQGVANAVGFAMAAKkaqnLLGSDLIdhkIYCLCGDGDLQEGISYEACSLAGLHKLdNFILIYDSNNISIEGDVG 191
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALK----YRGEDRV---AVCFFGDGATNEGDFHEALNFAALWKL-PVIFVCENNGYAISTPTS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 192 LAFNE-NVKMRFEAQGFEVLSINGHDYEEIN----KALEQAKKSTKPCLIIAKTTIAKGagelegsHKSHGAPLG----E 262
Cdd:cd02000 174 RQTAGtSIADRAAAYGIPGIRVDGNDVLAVYeaakEAVERARAGGGPTLIEAVTYRLGG-------HSTSDDPSRyrtkE 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949779181 263 EVikkaKEQAGFDPNisfhipqaskIRFESA-VELGDLEEAKWKdKLEKSAKKELLE 318
Cdd:cd02000 247 EV----EEWKKRDPI----------LRLRKYlIEAGILTEEELA-AIEAEVKAEVEE 288
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
517-625 |
5.55e-09 |
|
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: 54.52 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 517 AYLLKESKEAkfTLLASGSEVWLCLESANELEKQGFACNVVSMPCFELFekqDKAYQERLLK--GEVIGVE--------- 585
Cdd:pfam02780 3 AEILREGDDV--TIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPL---DKETILESVKktGRLVTVEeavprggfg 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 949779181 586 ---AAHSNELYKFCHKVY----GIESFGESGKDKDVFERFGFSVSKL 625
Cdd:pfam02780 78 sevAAALAEEAFDGLDAPvlrvGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
112-318 |
4.33e-08 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 55.53 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 112 ATGPLGQGVANAVGFAMAAKkaqnLLGSDLIdhkIYCLCGDGDLQEGISYEACSLAGLHKLDNFILIYDsNNISIEGDVG 191
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAK----LRGEDEV---AVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGYAISTPVE 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 192 LAFN-ENVKMRFEAQGFEVLSINGHD----YEEINKALEQAKKSTKPCLIIAKTTIAKGagelegsHKSHGAPLG----E 262
Cdd:COG1071 197 RQTAvETIADRAAGYGIPGVRVDGNDvlavYAAVKEAVERARAGEGPTLIEAKTYRLGG-------HSTSDDPTRyrtkE 269
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 949779181 263 EViKKAKEQagfDPNisfhipqaskIRFESA-VELGDLEEAKWkDKLEKSAKKELLE 318
Cdd:COG1071 270 EV-EEWRER---DPI----------ERLRAYlLEEGLLTEEEL-EAIEAEAKAEVEE 311
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
446-559 |
1.80e-07 |
|
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: 54.25 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 446 VGEDGPTHQPIEQLSTFRAMPNFLTFRPADGVENVKAWQIALNADIPSAF---------VLSRQKLKALnePVFgdvknG 516
Cdd:COG1154 422 VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIryprgngpgVELPAELEPL--PIG-----K 494
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 949779181 517 AYLLKESKEAkfTLLASGSEVWLCLESANELEKQGFACNVVSM 559
Cdd:COG1154 495 GEVLREGKDV--AILAFGTMVAEALEAAERLAAEGISATVVDA 535
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
27-556 |
2.17e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 47.40 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 27 GHPGAPLGLADiLSVLSYHLKHNPKnptwlnrDRLVFSGGHASallYSFLHLSGYDLNLEDLKNFRQLHSKTPG-HPEIS 105
Cdd:PLN02234 104 GHLGSNLGVVE-LTVALHYIFNTPH-------DKILWDVGHQS---YPHKILTGRRGKMKTIRQTNGLSGYTKRrESEHD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 106 TLGVEIATGPLGQGVANAVGfamaakkaQNLLGsdlIDHKIYCLCGDGDLQEGISYEACSLAGLHKLDNFILIYDSNNIS 185
Cdd:PLN02234 173 SFGTGHSSTTLSAGLGMAVG--------RDLKG---MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 186 IE-----------GDVGLAFN----------ENVKMRFEAQGFE-VLSINGHDYEEINKALEQAK--KSTKPCLIIAKTt 241
Cdd:PLN02234 242 LPtanldgptqpvGALSCALSrlqsncgmirETSSTLFEELGFHyVGPVDGHNIDDLVSILETLKstKTIGPVLIHVVT- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 242 iakgagelegsHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKleksakkellerll 321
Cdd:PLN02234 321 -----------EKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKTQSYTSCFVEALIAEAEADK-------------- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 322 npdfnkiaypdfkgkdlatrdsngeilNVLAknLEGFLGGSadlgpsnkTELHSMGDFVEGKNIHFGIREHAMAAINNAF 401
Cdd:PLN02234 376 ---------------------------DIVA--IHAAMGGG--------TMLNLFESRFPTRCFDVGIAEQHAVTFAAGL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 402 ARYGIfLPFSAtffIFSEYLKPAA-RIAALMKIKHFFI-FTHDSIGV-GEDGPTHQPIEQLSTFRAMPNFLTFRPADGVE 478
Cdd:PLN02234 419 ACEGL-KPFCT---IYSSFMQRAYdQVVHDVDLQKLPVrFAIDRAGLmGADGPTHCGAFDVTFMACLPNMIVMAPSDEAE 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 479 --NVKAWQIALNaDIPSAFVLSRQK-----LKALNEPVFGDVKNGAyLLKESKeaKFTLLASGSEVWLCLESANELEKQG 551
Cdd:PLN02234 495 lfNMVATAAAID-DRPSCFRYHRGNgigvsLPPGNKGVPLQIGRGR-ILRDGE--RVALLGYGSAVQRCLEAASMLSERG 570
|
....*
gi 949779181 552 FACNV 556
Cdd:PLN02234 571 LKITV 575
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
120-245 |
9.45e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 45.38 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 120 VANAVGFAmaakKAQNLLGSDlidHKIYCLCGDGDLQEGISYEACSLAGLHKlDNFILIYDSNNISIEGDVGLAFNENVK 199
Cdd:PRK12315 119 IALATGLA----KARDLKGEK---GNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAENHGGLYKNLKE 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 949779181 200 MR----------FEAQGFEVLSI-NGHDYEEINKALEQAKKSTKPCLIIAKTTIAKG 245
Cdd:PRK12315 191 LRdtngqsennlFKAMGLDYRYVeDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKG 247
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
439-556 |
1.25e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 45.28 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 439 FTHDSIG-VGEDGPTHQPIEQLSTFRAMPNFLTFRPADGVE--NVKAWQIALNaDIPSAFVLSRQ-----KLKALNEPVF 510
Cdd:PLN02582 453 FAMDRAGlVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAElfHMVATAAAID-DRPSCFRYPRGngigvQLPPNNKGIP 531
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 949779181 511 GDVKNGAYLLKESKEAkftLLASGSEVWLCLESANELEKQGFACNV 556
Cdd:PLN02582 532 IEVGKGRILLEGERVA---LLGYGTAVQSCLAAASLLERHGLSATV 574
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
90-240 |
2.13e-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: 42.58 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 90 NFRQLHSKTPGHPEISTLGveIATGPLGQGVANAVGFAMAAKkaqnllgsdliDHKIYCLCGDGDLQEGISyEACSLAGl 169
Cdd:cd02002 27 NGLPLRDQLPLTRPGSYFT--LRGGGLGWGLPAAVGAALANP-----------DRKVVAIIGDGSFMYTIQ-ALWTAAR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 170 HKLDNFILIYD-------SNNISIEGDVGLAFNENVKMRF-----------EAQGFEVLSIngHDYEEINKALEQAKKST 231
Cdd:cd02002 92 YGLPVTVVILNnrgygalRSFLKRVGPEGPGENAPDGLDLldpgidfaaiaKAFGVEAERV--ETPEELDEALREALAEG 169
|
....*....
gi 949779181 232 KPCLIIAKT 240
Cdd:cd02002 170 GPALIEVVV 178
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
61-182 |
3.90e-04 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 43.77 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 61 LVFSGGHASALLYSFLHLSGYdLNLEDLKNFRQLHSKtPG-----HPEISTLGVEIATGPLGQGVANAVGFAMAAKKAQN 135
Cdd:PRK13012 147 LVYFQPHSAPGIYARAFLEGR-LSEEQLDHFRQEIGG-PGlssypHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQH 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 949779181 136 LLGSDLIDHKIYCLCGDGDLQEGISYEACSLAGLHKLDNFILIYDSN 182
Cdd:PRK13012 225 RGLKDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLVFVINCN 271
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
112-240 |
3.31e-03 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 40.00 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 112 ATGPLGQGVANAVGFAMAAK-KAQNLLGSdlidhkiyCLCGDGDLQEGISYEACSLAGLHKLDnFILIYDSNNISIEGDV 190
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKyRGKKEVAI--------TLYGDGAANQGDFFEGLNFAALWKLP-VIFVCENNQYGISTPA 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 949779181 191 GLAFN-ENVKMRFEAQGFEVLSINGHD----YEEINKALEQAKKSTKPCLIIAKT 240
Cdd:pfam00676 170 ERASAsTTYADRARGYGIPGLHVDGMDplavYQASKFAAERARTGKGPFLIELVT 224
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
116-240 |
5.21e-03 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 39.46 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949779181 116 LGQGVANAVGFAMAAKKAQNLLGSDLIDHKIYCLCGDGDLQEGISYEACSLAGLHKLDnFILIYDSNNISIegdvGLAFN 195
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRQQVLKEVQPLRVTACFFGDGTTNNGQFFECLNMAVLWKLP-IIFVVENNQWAI----GMAHH 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 949779181 196 EN-----VKMRFEAQGFEVLSINGHD----YEEINKALEQAKKSTKPCLIIAKT 240
Cdd:CHL00149 205 RStsipeIHKKAEAFGLPGIEVDGMDvlavREVAKEAVERARQGDGPTLIEALT 258
|
|
| |
