|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
7-630 |
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: 895.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 7 QILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYD 85
Cdd:COG0021 2 PLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLwTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 86 LSLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEG 161
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGIANAVGMAIAERHlaARfNRPGHDIVDHYTYVIAGDGDLMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 162 ISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSI-NGHDYEEINKALEQAKKST-KPCLI 239
Cdd:COG0021 162 ISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVeDGHDLEAIDAAIEAAKAETdKPTLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 240 IAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK-- 317
Cdd:COG0021 242 ICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPE-PFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAAyp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 318 ---ELLERLLNP----DFNKiAYPDFK--GKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDFV----E 384
Cdd:COG0021 321 elaAELERRLAGelpeDWDA-ALPAFEadAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSpedpS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 385 GKNIHFGIREHa*aainnafarYGIFLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLST 464
Cdd:COG0021 400 GRNIHFGVREHamgaimngialHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLAS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 465 FRA*PNFLTFRPADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL--NEPVFGDVKNGAYLLKESK-EAKFTLLASGSEV 540
Cdd:COG0021 480 LRAIPNLDVIRPADANETAAAWKLALeRKDGPTALILSRQNLPTLdrTAAAAEGVAKGAYVLADAEgTPDVILIATGSEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 541 WLCLESANELEKQGFACNVVS*PCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKD 614
Cdd:COG0021 560 SLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVrarVAVEAGVTDGWYKYvglDGAVIGIDTFGASAPA 639
|
650
....*....|....*.
3M34_A 615 KDVFERFGFSVSKLVN 630
Cdd:COG0021 640 KVLFEEFGFTVENVVA 655
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
5-634 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 834.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 5 NIQILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSG 83
Cdd:PRK05899 4 DMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLwTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 84 YDLSLEDLKNFRQLHSKTPGHPEI-STLGVEIATGPLGQGVANAVGFA*AAKKAQNLLGSD---LIDHKIYCLCGDGDLQ 159
Cdd:PRK05899 84 YDLSIDDLKNFRQLGSKTPGHPEYgHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPgldIVDHYTYVLCGDGDLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 160 EGISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSINGHDYEEINKALEQAKKSTKPCLI 239
Cdd:PRK05899 164 EGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKASTKPTLI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 240 IAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPnisfhipqaskirfesavelgdleeakwkdkleksakkel 319
Cdd:PRK05899 244 IAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY---------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 320 lerllnpdfnkiaypdfkgkdlatRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDFVE----GKNIHFGIREH 395
Cdd:PRK05899 284 ------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPedysGRYIHYGVREF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 396 A*AAINNAFARYGIFLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNFLTFR 475
Cdd:PRK05899 340 AMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 476 PADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL-NEPVFGDVKNGAYLLKEskEAKFTLLASGSEVWLCLESANELEKQ 553
Cdd:PRK05899 420 PADANETAAAWKYALeRKDGPSALVLTRQNLPVLeRTAQEEGVAKGGYVLRD--DPDVILIATGSEVHLALEAADELEAE 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 554 GFACNVVS*PCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKDKDVFERFGFSVSK 627
Cdd:PRK05899 498 GIKVRVVSMPSTELFDEQDAAYKESVLPAAVtarVAVEAGVADGWYKYvglDGKVLGIDTFGASAPADELFKEFGFTVEN 577
|
....*..
3M34_A 628 LVNFILS 634
Cdd:PRK05899 578 IVAAAKE 584
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
13-630 |
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: 777.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 13 ANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDLSLEDL 91
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLwTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIEDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 92 KNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKKAQNL---LGSDLIDHKIYCLCGDGDLQEGISYEAC 167
Cdd:TIGR00232 84 KQFRQLHSKTPGHPEYGhTAGVEATTGPLGQGIANAVGMAIAEKTLAATfnkPGFEIVDHYTYVFVGDGCLQEGISYEVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 168 SLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVL-SINGHDYEEINKALEQAKKST-KPCLIIAKTTI 245
Cdd:TIGR00232 164 SLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTdKPTLIEVKTTI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 246 AKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRF-ESAVELGDLEEAKWKDKLEKSAKK-----EL 319
Cdd:TIGR00232 244 GFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYN-PFEIPQEVYDHFkKTVKERGAKAEQEWNELFAAYKKKypelaAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 320 LERLLNPDFNK---IAYPDF--KGKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDFVE---GKNIHFG 391
Cdd:TIGR00232 323 FTRRLSGELPAdwdKQLPEFkvKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHEnplGNYIHYG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 392 IREHA*AAINNAFARYGIFLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNF 471
Cdd:TIGR00232 403 VREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPNL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 472 LTFRPADGVENVKAWQIALNA-DIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKESKEAKFTLLASGSEVWLCLESANEL 550
Cdd:TIGR00232 483 SVWRPCDGNETAAAWKYALESqDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAVEAAKKL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 551 EKQGFACNVVS*PCFELFEKQDKAYQERLLKGEV--IGVEAAHSNELYKFCHK---VYGIESFGESGKDKDVFERFGFSV 625
Cdd:TIGR00232 563 AAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVtrLAIEAGAADEWYKYAGLvgaILGMDSFGESAPGDKLFEEFGFTV 642
|
....*
3M34_A 626 SKLVN 630
Cdd:TIGR00232 643 ENVVA 647
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
8-325 |
4.78e-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: 416.40 E-value: 4.78e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 8 ILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDL 86
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLfKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 87 SLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEGI 162
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGhTAGVEVTTGPLGQGIANAVGMAIAERNlaATyNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 163 SYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSIN-GHDYEEINKALEQAKKST-KPCLII 240
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEdGHDVEAIAAAIEEAKAEKdKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 241 AKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK--- 317
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAype 320
|
330
....*....|
3M34_A 318 --ELLERLLN 325
Cdd:pfam00456 321 laAEFARRLS 330
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
14-272 |
5.13e-134 |
|
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: 5.13e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 14 NTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYdLSLEDLK 92
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLyFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 93 NFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKKaqnllgsDLIDHKIYCLCGDGDLQEGISYEACSLAG 171
Cdd:cd02012 80 TFRQLGSRLPGHPEYGlTPGVEVTTGSLGQGLSVAVGMALAEKL-------LGFDYRVYVLLGDGELQEGSVWEAASFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 172 LHKLDNFILIYDSNNISIEGDV-GLAFNENVK*RFEAQGFEVLSINGHDYEEINKALEQAKKST-KPCLIIAKTTIAKGA 249
Cdd:cd02012 153 HYKLDNLIAIVDSNRIQIDGPTdDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKgKPTLIIAKTIKGKGV 232
|
250 260
....*....|....*....|...
3M34_A 250 GELEGSHKSHGAPLGEEVIKKAK 272
Cdd:cd02012 233 PFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
388-505 |
1.13e-23 |
|
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: 96.79 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 388 IHFGIREHA*AAINnafarYGI----FLPFSATFFIFSEYLKPAARIAAL*KiKHFFIFTHDS-IGVGEDGPTHQPIEQL 462
Cdd:smart00861 18 IDTGIAEQAMVGFA-----AGLalhgLRPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
3M34_A 463 STFRA*PNFLTFRPADGVENVKAWQIALNADIPSAFVLSRQKL 505
Cdd:smart00861 92 ALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSL 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
7-630 |
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: 895.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 7 QILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYD 85
Cdd:COG0021 2 PLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLwTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 86 LSLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEG 161
Cdd:COG0021 82 LSLDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGIANAVGMAIAERHlaARfNRPGHDIVDHYTYVIAGDGDLMEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 162 ISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSI-NGHDYEEINKALEQAKKST-KPCLI 239
Cdd:COG0021 162 ISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVeDGHDLEAIDAAIEAAKAETdKPTLI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 240 IAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK-- 317
Cdd:COG0021 242 ICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPE-PFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAAyp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 318 ---ELLERLLNP----DFNKiAYPDFK--GKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDFV----E 384
Cdd:COG0021 321 elaAELERRLAGelpeDWDA-ALPAFEadAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSpedpS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 385 GKNIHFGIREHa*aainnafarYGIFLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLST 464
Cdd:COG0021 400 GRNIHFGVREHamgaimngialHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLAS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 465 FRA*PNFLTFRPADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL--NEPVFGDVKNGAYLLKESK-EAKFTLLASGSEV 540
Cdd:COG0021 480 LRAIPNLDVIRPADANETAAAWKLALeRKDGPTALILSRQNLPTLdrTAAAAEGVAKGAYVLADAEgTPDVILIATGSEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 541 WLCLESANELEKQGFACNVVS*PCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKD 614
Cdd:COG0021 560 SLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVrarVAVEAGVTDGWYKYvglDGAVIGIDTFGASAPA 639
|
650
....*....|....*.
3M34_A 615 KDVFERFGFSVSKLVN 630
Cdd:COG0021 640 KVLFEEFGFTVENVVA 655
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
5-634 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 834.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 5 NIQILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSG 83
Cdd:PRK05899 4 DMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLwTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 84 YDLSLEDLKNFRQLHSKTPGHPEI-STLGVEIATGPLGQGVANAVGFA*AAKKAQNLLGSD---LIDHKIYCLCGDGDLQ 159
Cdd:PRK05899 84 YDLSIDDLKNFRQLGSKTPGHPEYgHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPgldIVDHYTYVLCGDGDLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 160 EGISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSINGHDYEEINKALEQAKKSTKPCLI 239
Cdd:PRK05899 164 EGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKASTKPTLI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 240 IAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPnisfhipqaskirfesavelgdleeakwkdkleksakkel 319
Cdd:PRK05899 244 IAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY---------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 320 lerllnpdfnkiaypdfkgkdlatRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDFVE----GKNIHFGIREH 395
Cdd:PRK05899 284 ------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPedysGRYIHYGVREF 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 396 A*AAINNAFARYGIFLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNFLTFR 475
Cdd:PRK05899 340 AMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 476 PADGVENVKAWQIAL-NADIPSAFVLSRQKLKAL-NEPVFGDVKNGAYLLKEskEAKFTLLASGSEVWLCLESANELEKQ 553
Cdd:PRK05899 420 PADANETAAAWKYALeRKDGPSALVLTRQNLPVLeRTAQEEGVAKGGYVLRD--DPDVILIATGSEVHLALEAADELEAE 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 554 GFACNVVS*PCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKDKDVFERFGFSVSK 627
Cdd:PRK05899 498 GIKVRVVSMPSTELFDEQDAAYKESVLPAAVtarVAVEAGVADGWYKYvglDGKVLGIDTFGASAPADELFKEFGFTVEN 577
|
....*..
3M34_A 628 LVNFILS 634
Cdd:PRK05899 578 IVAAAKE 584
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
13-630 |
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: 777.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 13 ANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDLSLEDL 91
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLwTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIEDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 92 KNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKKAQNL---LGSDLIDHKIYCLCGDGDLQEGISYEAC 167
Cdd:TIGR00232 84 KQFRQLHSKTPGHPEYGhTAGVEATTGPLGQGIANAVGMAIAEKTLAATfnkPGFEIVDHYTYVFVGDGCLQEGISYEVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 168 SLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVL-SINGHDYEEINKALEQAKKST-KPCLIIAKTTI 245
Cdd:TIGR00232 164 SLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTdKPTLIEVKTTI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 246 AKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNiSFHIPQASKIRF-ESAVELGDLEEAKWKDKLEKSAKK-----EL 319
Cdd:TIGR00232 244 GFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYN-PFEIPQEVYDHFkKTVKERGAKAEQEWNELFAAYKKKypelaAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 320 LERLLNPDFNK---IAYPDF--KGKDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDFVE---GKNIHFG 391
Cdd:TIGR00232 323 FTRRLSGELPAdwdKQLPEFkvKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHEnplGNYIHYG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 392 IREHA*AAINNAFARYGIFLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNF 471
Cdd:TIGR00232 403 VREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPNL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 472 LTFRPADGVENVKAWQIALNA-DIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKESKEAKFTLLASGSEVWLCLESANEL 550
Cdd:TIGR00232 483 SVWRPCDGNETAAAWKYALESqDGPTALILSRQNLPQLEESSLEKVLKGGYVLKDSKGPDLILIATGSEVQLAVEAAKKL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 551 EKQGFACNVVS*PCFELFEKQDKAYQERLLKGEV--IGVEAAHSNELYKFCHK---VYGIESFGESGKDKDVFERFGFSV 625
Cdd:TIGR00232 563 AAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVtrLAIEAGAADEWYKYAGLvgaILGMDSFGESAPGDKLFEEFGFTV 642
|
....*
3M34_A 626 SKLVN 630
Cdd:TIGR00232 643 ENVVA 647
|
|
| PLN02790 |
PLN02790 |
transketolase |
17-630 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 673.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 17 RFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYD-LSLEDLKNF 94
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLyDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 95 RQLHSKTPGHPE-ISTLGVEIATGPLGQGVANAVGFA*AAKKAQ---NLLGSDLIDHKIYCLCGDGDLQEGISYEACSLA 170
Cdd:PLN02790 82 RQWGSRTPGHPEnFETPGIEVTTGPLGQGIANAVGLALAEKHLAarfNKPDHKIVDHYTYCILGDGCQMEGISNEAASLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 171 GLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSING--HDYEEINKALEQAKKST-KPCLIIAKTTIAK 247
Cdd:PLN02790 162 GHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTdKPTLIKVTTTIGY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 248 GAGELEGSHKSHGAPLGEEVIKKAKEQAGFdPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK--EL---LER 322
Cdd:PLN02790 242 GSPNKANSYSVHGAALGEKEVDATRKNLGW-PYEPFHVPEDVKSHWSKHTKEGAALEAEWNAKFAEYKKKypEEaaeLKS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 323 LLN---PDFNKIAYPDFKGKD--LATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDF----VEGKNIHFGIR 393
Cdd:PLN02790 321 LISgelPSGWEKALPTFTPEDpaDATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFqkdtPEERNVRFGVR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 394 EHA*AAINNAFARYGI-FLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNFL 472
Cdd:PLN02790 401 EHGMGAICNGIALHSSgLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNIL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 473 TFRPADGVENVKAWQIA-LNADIPSAFVLSRQKLKALNEPVFGDVKNGAYLLK-ESKEAK--FTLLASGSEVWLCLESAN 548
Cdd:PLN02790 481 MLRPADGNETAGAYKVAvTNRKRPTVLALSRQKVPNLPGTSIEGVEKGGYVISdNSSGNKpdLILIGTGSELEIAAKAAK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 549 ELEKQGFACNVVS*PCFELFEKQDKAYQERLLKGEV---IGVEAAHSNELYKF---CHKVYGIESFGESGKDKDVFERFG 622
Cdd:PLN02790 561 ELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVtarVSVEAGSTFGWEKYvgsKGKVIGVDRFGASAPAGILYKEFG 640
|
....*...
3M34_A 623 FSVSKLVN 630
Cdd:PLN02790 641 FTVENVVA 648
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
5-633 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 668.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 5 NIQILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSG 83
Cdd:PTZ00089 2 DGAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILwSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 84 YDLSLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKKAQ---NLLGSDLIDHKIYCLCGDGDLQ 159
Cdd:PTZ00089 82 YDLSMEDLKNFRQLGSRTPGHPERHiTPGVEVTTGPLGQGIANAVGLAIAEKHLAakfNRPGHPIFDNYVYVICGDGCLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 160 EGISYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSI-NGH-DYEEINKALEQAKKST-KP 236
Cdd:PTZ00089 162 EGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVdNGNtDFDGLRKAIEEAKKSKgKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 237 CLIIAKTTIAKGAgELEGSHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAK 316
Cdd:PTZ00089 242 KLIIVKTTIGYGS-SKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYTA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 317 K-----ELLERL----LNPDFNKiAYPDFKGKD--LATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GDFV-- 383
Cdd:PTZ00089 321 AfpkeaQAIERRfkgeLPPGWEK-KLPKYTTNDkaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTka 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 384 --EGKNIHFGIREHA*AAINNAFARYGIFLPFSATFFIFSEYLKPAARIAAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQ 461
Cdd:PTZ00089 400 spEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVET 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 462 LSTFRA*PNFLTFRPADGVENVKAWQIAL-NADIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKE-SKEAKFTLLASGSE 539
Cdd:PTZ00089 480 LALLRATPNLLVIRPADGTETSGAYALALaNAKTPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDfTNSPQLILVASGSE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 540 VWLCLESANELEKQgFACNVVS*PCFELFEKQDKAYQERLLKGE---VIGVEAAHSNELYKFCHKVYGIESFGESGKDKD 616
Cdd:PTZ00089 560 VSLCVEAAKALSKE-LNVRVVSMPCWELFDQQSEEYQQSVLPSGgvpVLSVEAYVSFGWEKYSHVHVGISGFGASAPANA 638
|
650
....*....|....*..
3M34_A 617 VFERFGFSVSKLVNFIL 633
Cdd:PTZ00089 639 LYKHFGFTVENVVEKAR 655
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
8-325 |
4.78e-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: 416.40 E-value: 4.78e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 8 ILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYDL 86
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLfKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 87 SLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKK--AQ-NLLGSDLIDHKIYCLCGDGDLQEGI 162
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGhTAGVEVTTGPLGQGIANAVGMAIAERNlaATyNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 163 SYEACSLAGLHKLDNFILIYDSNNISIEGDVGLAFNENVK*RFEAQGFEVLSIN-GHDYEEINKALEQAKKST-KPCLII 240
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEdGHDVEAIAAAIEEAKAEKdKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 241 AKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKLEKSAKK--- 317
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAype 320
|
330
....*....|
3M34_A 318 --ELLERLLN 325
Cdd:pfam00456 321 laAEFARRLS 330
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
14-272 |
5.13e-134 |
|
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: 5.13e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 14 NTLRFLSAD*VQKANSGHPGAPLGLADILSVL-SYHLKHNPKNPTWLNRDRLVFSGGHASALLYSFLHLSGYdLSLEDLK 92
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLyFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 93 NFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKKaqnllgsDLIDHKIYCLCGDGDLQEGISYEACSLAG 171
Cdd:cd02012 80 TFRQLGSRLPGHPEYGlTPGVEVTTGSLGQGLSVAVGMALAEKL-------LGFDYRVYVLLGDGELQEGSVWEAASFAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 172 LHKLDNFILIYDSNNISIEGDV-GLAFNENVK*RFEAQGFEVLSINGHDYEEINKALEQAKKST-KPCLIIAKTTIAKGA 249
Cdd:cd02012 153 HYKLDNLIAIVDSNRIQIDGPTdDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKgKPTLIIAKTIKGKGV 232
|
250 260
....*....|....*....|...
3M34_A 250 GELEGSHKSHGAPLGEEVIKKAK 272
Cdd:cd02012 233 PFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
2-274 |
6.37e-85 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 267.33 E-value: 6.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 2 NA*NIQILQEQANTLRFLSAD*VQKANSGHPGAPLGLADILSVLSYH-LKHNPKNPTWLNRDRLVFSGGHASALLYSFLH 80
Cdd:COG3959 1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKvMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 81 LSGYdLSLEDLKNFRQLHSKTPGHPEIS-TLGVEIATGPLGQGVANAVGFA*AAKkaqnLLGSDlidHKIYCLCGDGDLQ 159
Cdd:COG3959 81 EKGY-FPKEELATFRKLGSRLQGHPDMKkTPGVEMSTGSLGQGLSVAVGMALAAK----LDGKD---YRVYVLLGDGELQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 160 EGISYEACSLAGLHKLDNFILIYDSNNISIEGDV----GLafnENVK*RFEAQGFEVLSINGHDYEEINKALEQAKKST- 234
Cdd:COG3959 153 EGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDGPTedvmSL---EPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKg 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
3M34_A 235 KPCLIIAKTTIAKGAGELEGSHKSHGAPLGEEVIKKAKEQ 274
Cdd:COG3959 230 KPTVIIAHTVKGKGVSFMENRPKWHGKAPNDEELEQALAE 269
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
345-502 |
3.66e-43 |
|
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: 152.21 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 345 DSNGEILNVLAKNLEGFLGGSADLGPSNKTELhs*GDFVEGKNIHFGIREHA*AAINNAFARYGiFLPFSATFFIFSEYL 424
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDK--FAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3M34_A 425 KPAARI-AAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNFLTFRPADGVENVKAWQIALNADIPSAFVLSR 502
Cdd:cd07033 78 YDQIRHdVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
339-505 |
1.26e-39 |
|
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: 143.07 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 339 KDLATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTELHS*GD-FVEGKNIHFGIREHA*AAINnafarYGI------FL 411
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHpQGAGRVIDTGIAEQAMVGFA-----NGMalhgplLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 412 PFSATFFIFSEYLKPAARI-AAL*KIKHFFIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNFLTFRPADGVENVKAW--QI 488
Cdd:pfam02779 76 PVEATFSDFLNRADDAIRHgAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLraAI 155
|
170
....*....|....*..
3M34_A 489 ALNADIPSAFVLSRQKL 505
Cdd:pfam02779 156 RRDGRKPVVLRLPRQLL 172
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
388-505 |
1.13e-23 |
|
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: 96.79 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 388 IHFGIREHA*AAINnafarYGI----FLPFSATFFIFSEYLKPAARIAAL*KiKHFFIFTHDS-IGVGEDGPTHQPIEQL 462
Cdd:smart00861 18 IDTGIAEQAMVGFA-----AGLalhgLRPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|...
3M34_A 463 STFRA*PNFLTFRPADGVENVKAWQIALNADIPSAFVLSRQKL 505
Cdd:smart00861 92 ALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKSL 134
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
16-213 |
2.14e-16 |
|
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: 81.58 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 16 LRFLSAD*VQKANS------GHPGAPLGLADILSVLSYHLKHNPKNPtwLNRDrLVFSGGHASALLYSFLHLSGyDLSLE 89
Cdd:cd02017 11 IRWNAMAMVHRANKkdlgigGHIATFASAATLYEVGFNHFFRARGEG--GGGD-LVYFQGHASPGIYARAFLEG-RLTEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 90 DLKNFRQLHSKT-----PgHPEISTLGVEIATGPLGQGVANAVGFA*AAKKAQNLLGSDLIDHKIYCLCGDGDLQEGISY 164
Cdd:cd02017 87 QLDNFRQEVGGGglssyP-HPWLMPDFWEFPTVSMGLGPIQAIYQARFNRYLEDRGLKDTSDQKVWAFLGDGEMDEPESL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
3M34_A 165 EACSLAGLHKLDNFILIYDSNNISIEGDV---GLAFNEnVK*RFEAQGFEVL 213
Cdd:cd02017 166 GAIGLAAREKLDNLIFVVNCNLQRLDGPVrgnGKIIQE-LEGIFRGAGWNVI 216
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
341-630 |
2.18e-15 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 77.43 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 341 LATRDSNGEILNVLAKNLEGFLGGSADLGPSNKTElhs*gDFveGKN-----IHFGIREHA*aainnafarYGI------ 409
Cdd:COG3958 4 KAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLD-----KF--AKAfpdrfFNVGIAEQNM---------VGVaaglal 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 410 --FLPFSATFFIFSeylkpAARiaAL*KIKHF---------FIFTHDSIGVGEDGPTHQPIEQLSTFRA*PNFLTFRPAD 478
Cdd:COG3958 68 agKIPFVSTFAPFL-----TGR--AYEQIRNDiaypnlnvkIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPAD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 479 GVENVKAWQIALNADIPSAFVLSRQKLKALNEPVFGDVKNGAYLLKESKEAkfTLLASGSEVWLCLESANELEKQGFACN 558
Cdd:COG3958 141 AVETEAAVRAAAEHDGPVYLRLGRGAVPVVYDEDYEFEIGKARVLREGKDV--TIIATGIMVAEALEAAELLAKEGISAR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 559 VVS*PCF-----ELFEKQDKAYQeRLLKGE---VIG-----VEAAHSNELYKFCHKVyGI-ESFGESGKDKDVFERFGFS 624
Cdd:COG3958 219 VINMHTIkpldeEAILKAARKTG-AVVTAEehsIIGglgsaVAEVLAENYPVPLRRI-GVpDRFGESGSPEELLEKYGLD 296
|
....*.
3M34_A 625 VSKLVN 630
Cdd:COG3958 297 AEGIVA 302
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
114-250 |
1.09e-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: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 114 IATGPLGQGVANAVGFA*aakKAQNLLGSDlidHKIYCLCGDGDLQEGISYEACSLAGlHKLDNFILIYDSNNISIEGDV 193
Cdd:cd02007 72 FGTGHSSTSISAALGMA----VARDLKGKK---RKVIAVIGDGALTGGMAFEALNNAG-YLKSNMIVILNDNEMSISPNV 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
3M34_A 194 GLAFNenvk*RFEAQGFEVLS-INGHDYEEINKALEQAKKSTKPCLIIAKTTiaKGAG 250
Cdd:cd02007 144 GTPGN-----LFEELGFRYIGpVDGHNIEALIKVLKEVKDLKGPVLLHVVTK--KGKG 194
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
126-250 |
7.74e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 61.64 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 126 AVGFA*aakKAQNLLGSDliDHKIYCLCGDGDLQEGISYEACSLAGlHKLDNFILIYDSNNISIEGDVGlAFNENV-K*R 204
Cdd:PRK05444 126 ALGMA----KARDLKGGE--DRKVVAVIGDGALTGGMAFEALNNAG-DLKSDLIVILNDNEMSISPNVG-ALSNYLaRLR 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
3M34_A 205 ----FEAQGFEVLS-INGHDYEEINKALEQAKKSTKPCLIIAKTTiaKGAG 250
Cdd:PRK05444 198 sstlFEELGFNYIGpIDGHDLDALIETLKNAKDLKGPVLLHVVTK--KGKG 246
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
59-243 |
9.37e-10 |
|
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: 58.04 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 59 LNRDRLVFSG-GHASALLYSFLHLsgydlsledlknfrqlhsKTPGHPEISTlgveiATGPLGQGVANAVGFA*AAKkaq 137
Cdd:cd00568 10 LPEDAIVVNDaGNSAYWAYRYLPL------------------RRGRRFLTST-----GFGAMGYGLPAAIGAALAAP--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 138 nllgsdliDHKIYCLCGDGDLQEGISyeACSLAGLHKLdNFILIYDSNNISIEGDVGLA------------FNENVK*RF 205
Cdd:cd00568 64 --------DRPVVCIAGDGGFMMTGQ--ELATAVRYGL-PVIVVVFNNGGYGTIRMHQEafyggrvsgtdlSNPDFAALA 132
|
170 180 190
....*....|....*....|....*....|....*...
3M34_A 206 EAQGFEVLSINGHdyEEINKALEQAKKSTKPCLIIAKT 243
Cdd:cd00568 133 EAYGAKGVRVEDP--EDLEAALAEALAAGGPALIEVKT 168
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
115-321 |
5.04e-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: 57.89 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 115 ATGPLGQGVANAVGFA*AAKkaqnLLGSDLIdhkIYCLCGDGDLQEGISYEACSLAGLHKLdNFILIYDSNNISIEGDVG 194
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALK----YRGEDRV---AVCFFGDGATNEGDFHEALNFAALWKL-PVIFVCENNGYAISTPTS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 195 LAFNE-NVK*RFEAQGFEVLSINGHDYEEIN----KALEQAKKSTKPCLIIAKTTIAKGagelegsHKSHGAPLG----E 265
Cdd:cd02000 174 RQTAGtSIADRAAAYGIPGIRVDGNDVLAVYeaakEAVERARAGGGPTLIEAVTYRLGG-------HSTSDDPSRyrtkE 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
3M34_A 266 EVikkaKEQAGFDPNisfhipqaskIRFESA-VELGDLEEAKWKdKLEKSAKKELLE 321
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 ... |
520-628 |
7.92e-08 |
|
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: 51.06 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 520 AYLLKESKEAkfTLLASGSEVWLCLESANELEKQGFACNVVS*PCFELFekqDKAYQERLLK--GEVIGVE--------- 588
Cdd:pfam02780 3 AEILREGDDV--TIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPL---DKETILESVKktGRLVTVEeavprggfg 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
3M34_A 589 ---AAHSNELYKFCHKVY----GIESFGESGKDKDVFERFGFSVSKL 628
Cdd:pfam02780 78 sevAAALAEEAFDGLDAPvlrvGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
449-560 |
3.28e-06 |
|
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: 50.01 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 449 VGEDGPTHQPIEQLSTFRA*PNFLTFRPADGVENVKAWQIALNADIPSAF---------VLSRQKLKALnePVFgdvknG 519
Cdd:COG1154 422 VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIryprgngpgVELPAELEPL--PIG-----K 494
|
90 100 110 120
....*....|....*....|....*....|....*....|.
3M34_A 520 AYLLKESKEAkfTLLASGSEVWLCLESANELEKQGFACNVV 560
Cdd:COG1154 495 GEVLREGKDV--AILAFGTMVAEALEAAERLAAEGISATVV 533
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
64-185 |
1.91e-04 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 44.54 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 64 LVFSGGHASALLYSFLHLSGYdLSLEDLKNFRQLHSKtPG-----HPEISTLGVEIATGPLGQGVANAVGFA*AAKKAQN 138
Cdd:PRK13012 147 LVYFQPHSAPGIYARAFLEGR-LSEEQLDHFRQEIGG-PGlssypHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQH 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
3M34_A 139 LLGSDLIDHKIYCLCGDGDLQEGISYEACSLAGLHKLDNFILIYDSN 185
Cdd:PRK13012 225 RGLKDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLVFVINCN 271
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
123-248 |
2.01e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 44.23 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 123 VANAVGFA*aakKAQNLLGSDlidHKIYCLCGDGDLQEGISYEACSLAGLHKlDNFILIYDSNNISIEGDVGLAFNENVK 202
Cdd:PRK12315 119 IALATGLA----KARDLKGEK---GNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAENHGGLYKNLKE 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
3M34_A 203 *R----------FEAQGFEVLSI-NGHDYEEINKALEQAKKSTKPCLIIAKTTIAKG 248
Cdd:PRK12315 191 LRdtngqsennlFKAMGLDYRYVeDGNDIESLIEAFKEVKDIDHPIVLHIHTLKGKG 247
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
442-559 |
3.13e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 43.74 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 442 FTHDSIG-VGEDGPTHQPIEQLSTFRA*PNFLTFRPADGVE--NVKAWQIALNaDIPSAFVLSRQ-----KLKALNEPVF 513
Cdd:PLN02582 453 FAMDRAGlVGADGPTHCGAFDVTYMACLPNMVVMAPSDEAElfHMVATAAAID-DRPSCFRYPRGngigvQLPPNNKGIP 531
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
3M34_A 514 GDVKNGAYLLKESKEAkftLLASGSEVWLCLESANELEKQGFACNV 559
Cdd:PLN02582 532 IEVGKGRILLEGERVA---LLGYGTAVQSCLAAASLLERHGLSATV 574
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
30-559 |
1.06e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 42.01 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 30 GHPGAPLGLADiLSVLSYHLKHNPKnptwlnrDRLVFSGGHASallYSFLHLSGYDLSLEDLKNFRQLHSKTPG-HPEIS 108
Cdd:PLN02234 104 GHLGSNLGVVE-LTVALHYIFNTPH-------DKILWDVGHQS---YPHKILTGRRGKMKTIRQTNGLSGYTKRrESEHD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 109 TLGVEIATGPLGQGVANAVGfa*aakkaQNLLGsdlIDHKIYCLCGDGDLQEGISYEACSLAGLHKLDNFILIYDSNNIS 188
Cdd:PLN02234 173 SFGTGHSSTTLSAGLGMAVG--------RDLKG---MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 189 IE-----------GDVGLAFN----------ENVK*RFEAQGFE-VLSINGHDYEEINKALEQAK--KSTKPCLIIAKTt 244
Cdd:PLN02234 242 LPtanldgptqpvGALSCALSrlqsncgmirETSSTLFEELGFHyVGPVDGHNIDDLVSILETLKstKTIGPVLIHVVT- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 245 iakgagelegsHKSHGAPLGEEVIKKAKEQAGFDPNISFHIPQASKIRFESAVELGDLEEAKWKDKleksakkellerll 324
Cdd:PLN02234 321 -----------EKGRGYPYAERADDKYHGVLKFDPETGKQFKNISKTQSYTSCFVEALIAEAEADK-------------- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 325 npdfNKIAYPDFKGkdlatrdsNGEILNVLAKNlegFLGGSADLGPSNKTEL-HS*GDFVEGknihfgireha*aainna 403
Cdd:PLN02234 376 ----DIVAIHAAMG--------GGTMLNLFESR---FPTRCFDVGIAEQHAVtFAAGLACEG------------------ 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 404 farygiFLPFSAtffIFSEYLKPAA-RIAAL*KIKHFFI-FTHDSIGV-GEDGPTHQPIEQLSTFRA*PNFLTFRPADGV 480
Cdd:PLN02234 423 ------LKPFCT---IYSSFMQRAYdQVVHDVDLQKLPVrFAIDRAGLmGADGPTHCGAFDVTFMACLPNMIVMAPSDEA 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 481 E--NVKAWQIALNaDIPSAFVLSRQK-----LKALNEPVFGDVKNGAyLLKESKeaKFTLLASGSEVWLCLESANELEKQ 553
Cdd:PLN02234 494 ElfNMVATAAAID-DRPSCFRYHRGNgigvsLPPGNKGVPLQIGRGR-ILRDGE--RVALLGYGSAVQRCLEAASMLSER 569
|
....*.
3M34_A 554 GFACNV 559
Cdd:PLN02234 570 GLKITV 575
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
70-243 |
4.50e-03 |
|
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: 38.73 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 70 HASALLYSFLHLSGYDLSL--EDLKNFRQLHSKTPGHPEISTLGveIATGPLGQGVANAVGFA*AAKkaqnllgsdliDH 147
Cdd:cd02002 2 TPEYLAAALAAALPEDAIIvdEAVTNGLPLRDQLPLTRPGSYFT--LRGGGLGWGLPAAVGAALANP-----------DR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 148 KIYCLCGDGDLQEGISyEACSLAGlHKLDNFILIYDSNNISI-EGDVGLAFNENVK*RF-----------------EAQG 209
Cdd:cd02002 69 KVVAIIGDGSFMYTIQ-ALWTAAR-YGLPVTVVILNNRGYGAlRSFLKRVGPEGPGENApdgldlldpgidfaaiaKAFG 146
|
170 180 190
....*....|....*....|....*....|....
3M34_A 210 FEVLSIngHDYEEINKALEQAKKSTKPCLIIAKT 243
Cdd:cd02002 147 VEAERV--ETPEELDEALREALAEGGPALIEVVV 178
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
119-243 |
5.06e-03 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 39.46 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 119 LGQGVANAVGFA*AAKKAQNLLGSDLIDHKIYCLCGDGDLQEGISYEACSLAGLHKLDnFILIYDSNNISIegdvGLAFN 198
Cdd:CHL00149 130 IGEGIPIALGAAFQSIYRQQVLKEVQPLRVTACFFGDGTTNNGQFFECLNMAVLWKLP-IIFVVENNQWAI----GMAHH 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
3M34_A 199 EN-----VK*RFEAQGFEVLSINGHD----YEEINKALEQAKKSTKPCLIIAKT 243
Cdd:CHL00149 205 RStsipeIHKKAEAFGLPGIEVDGMDvlavREVAKEAVERARQGDGPTLIEALT 258
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
115-243 |
8.64e-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: 38.46 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3M34_A 115 ATGPLGQGVANAVGFA*AAK-KAQNLLGSdlidhkiyCLCGDGDLQEGISYEACSLAGLHKLDnFILIYDSNNISIEGDV 193
Cdd:pfam00676 99 GNGILGAQVPLGAGIALAAKyRGKKEVAI--------TLYGDGAANQGDFFEGLNFAALWKLP-VIFVCENNQYGISTPA 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
3M34_A 194 GLAFN-ENVK*RFEAQGFEVLSINGHD----YEEINKALEQAKKSTKPCLIIAKT 243
Cdd:pfam00676 170 ERASAsTTYADRARGYGIPGLHVDGMDplavYQASKFAAERARTGKGPFLIELVT 224
|
|
| |
