|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
4-309 |
7.07e-175 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 486.13 E-value: 7.07e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 4 MIATRDAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFAV 83
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 84 GRAWEQVRQSLAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHRGPVYVRL 163
Cdd:COG3958 83 GRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 164 GRNKVPTVTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGA 243
Cdd:COG3958 163 GRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504364923 244 IVTAEEHSIVGGLGGAVAEFLAENSPVPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVL 309
Cdd:COG3958 243 VVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
9-165 |
1.51e-68 |
|
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: 210.38 E-value: 1.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 9 DAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFaVGRAWE 88
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFF-LQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504364923 89 QVRQSLAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHRGPVYVRLGR 165
Cdd:cd07033 80 QIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-309 |
5.64e-67 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 219.62 E-value: 5.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 8 RDAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKK------FPDRFFNMGIAEANMVGTAAGLAAA-GKIPFVSTFAI 80
Cdd:PRK05899 284 RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKdfapedYSGRYIHYGVREFAMAAIANGLALHgGFIPFGGTFLV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 81 FAvGRAWEQVRQSlAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKA-IRAAAAHRGPV 159
Cdd:PRK05899 364 FS-DYARNAIRLA-ALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAwKYALERKDGPS 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 160 YVRLGRNKVPTVTSTDTPFEIGKG-VQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLD-------- 230
Cdd:PRK05899 442 ALVLTRQNLPVLERTAQEEGVAKGgYVLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDeqdaayke 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 231 ----GEILRRAAQETGaiVTAEEHSIVGGLGgavaeflaenspvplKRVGInDRFGLSGKAEELLKYFGLMPADLAEAAR 306
Cdd:PRK05899 522 svlpAAVTARVAVEAG--VADGWYKYVGLDG---------------KVLGI-DTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 504364923 307 EVL 309
Cdd:PRK05899 584 ELL 586
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
4-170 |
1.32e-42 |
|
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: 144.62 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 4 MIATRDAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPD---RFFNMGIAEANMVGTAA--GLAAAGKIPFVSTF 78
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANgmALHGPLLPPVEATF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 79 AIFAvGRAWEQVRQSLAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAH--R 156
Cdd:pfam02779 82 SDFL-NRADDAIRHGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRdgR 160
|
170
....*....|....
gi 504364923 157 GPVYVRLGRNKVPT 170
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
4-165 |
7.56e-30 |
|
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: 110.27 E-value: 7.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 4 MIATRDAYGQTLAELGeengsvvvldadlsgstktsvfakkfpdrfFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFAV 83
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 84 gRAWEQVRQSLAYPKANVkVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHRGPVYVRL 163
Cdd:smart00861 52 -RAKDQIRSAGASGNVPV-VFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRL 129
|
..
gi 504364923 164 GR 165
Cdd:smart00861 130 ER 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
4-309 |
7.07e-175 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 486.13 E-value: 7.07e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 4 MIATRDAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFAV 83
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 84 GRAWEQVRQSLAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHRGPVYVRL 163
Cdd:COG3958 83 GRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 164 GRNKVPTVTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGA 243
Cdd:COG3958 163 GRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARKTGA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504364923 244 IVTAEEHSIVGGLGGAVAEFLAENSPVPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVL 309
Cdd:COG3958 243 VVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
9-165 |
1.51e-68 |
|
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: 210.38 E-value: 1.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 9 DAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFaVGRAWE 88
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFF-LQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504364923 89 QVRQSLAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHRGPVYVRLGR 165
Cdd:cd07033 80 QIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
8-309 |
5.64e-67 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 219.62 E-value: 5.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 8 RDAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKK------FPDRFFNMGIAEANMVGTAAGLAAA-GKIPFVSTFAI 80
Cdd:PRK05899 284 RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKdfapedYSGRYIHYGVREFAMAAIANGLALHgGFIPFGGTFLV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 81 FAvGRAWEQVRQSlAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKA-IRAAAAHRGPV 159
Cdd:PRK05899 364 FS-DYARNAIRLA-ALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAwKYALERKDGPS 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 160 YVRLGRNKVPTVTSTDTPFEIGKG-VQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLD-------- 230
Cdd:PRK05899 442 ALVLTRQNLPVLERTAQEEGVAKGgYVLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDeqdaayke 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 231 ----GEILRRAAQETGaiVTAEEHSIVGGLGgavaeflaenspvplKRVGInDRFGLSGKAEELLKYFGLMPADLAEAAR 306
Cdd:PRK05899 522 svlpAAVTARVAVEAG--VADGWYKYVGLDG---------------KVLGI-DTFGASAPADELFKEFGFTVENIVAAAK 583
|
...
gi 504364923 307 EVL 309
Cdd:PRK05899 584 ELL 586
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
9-309 |
1.68e-66 |
|
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: 219.11 E-value: 1.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 9 DAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFV---STFaifaVGR 85
Cdd:COG1154 321 DVFGDTLVELAEKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVaiySTF----LQR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 86 AWEQVRQSLAYPKANVKVVATHGGItVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHRGPVYVRLGR 165
Cdd:COG1154 397 AYDQVIHDVALQNLPVTFAIDRAGL-VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 166 NKVPTVT--STDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGA 243
Cdd:COG1154 476 GNGPGVElpAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDL 555
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504364923 244 IVTAEEHSIVGGLGGAVAEFLAENS-PVPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVL 309
Cdd:COG1154 556 VVTVEEGVLAGGFGSAVLEFLADAGlDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELL 622
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
9-309 |
9.97e-60 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 200.31 E-value: 9.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 9 DAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFV---STFaifaVGR 85
Cdd:PRK05444 283 KVFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVaiySTF----LQR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 86 AWEQVRQSLAYPKANVKVVATHGGItVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHR-GPVYVRLG 164
Cdd:PRK05444 359 AYDQVIHDVALQNLPVTFAIDRAGL-VGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDdGPIAIRYP 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 165 R-NKVPTVTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSqegiSARVIHMATIKPLDGEILRRAAQETGA 243
Cdd:PRK05444 438 RgNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDL 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504364923 244 IVTAEEHSIVGGLGGAVAEFLAENS-PVPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVL 309
Cdd:PRK05444 514 VVTVEEGAIMGGFGSAVLEFLADHGlDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
4-170 |
1.32e-42 |
|
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: 144.62 E-value: 1.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 4 MIATRDAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPD---RFFNMGIAEANMVGTAA--GLAAAGKIPFVSTF 78
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANgmALHGPLLPPVEATF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 79 AIFAvGRAWEQVRQSLAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAH--R 156
Cdd:pfam02779 82 SDFL-NRADDAIRHGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRdgR 160
|
170
....*....|....
gi 504364923 157 GPVYVRLGRNKVPT 170
Cdd:pfam02779 161 KPVVLRLPRQLLRP 174
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
9-314 |
1.72e-42 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 154.88 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 9 DAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFaVGRAWE 88
Cdd:PRK12571 323 SVFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTF-LQRGYD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 89 QVRQSLAYPKANVKVVATHGGITvGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAH-RGPVYVRLGRNK 167
Cdd:PRK12571 402 QLLHDVALQNLPVRFVLDRAGLV-GADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHdDGPIAVRFPRGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 168 VP--TVTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIV 245
Cdd:PRK12571 481 GVgvEIPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIVVI 560
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504364923 246 TaEEHSIVGGLGGAVAEFLAENSP----VPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVLTRKRP 314
Cdd:PRK12571 561 V-EEQGAMGGFGAHVLHHLADTGLldggLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARLSG 632
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
181-301 |
2.54e-35 |
|
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: 124.25 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 181 GKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIVTAEEHSIVGGLGGAV 260
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 504364923 261 AEFLAENS----PVPLKRVGINDrFGLSGKAEELLKYFGLMPADL 301
Cdd:pfam02780 81 AAALAEEAfdglDAPVLRVGGPD-FPEPGSADELEKLYGLTPEKI 124
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
11-313 |
3.82e-32 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 125.78 E-value: 3.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 11 YGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFaVGRAWEQV 90
Cdd:PLN02582 362 FAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSF-LQRGYDQV 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 91 RQSLAYPKANVKVVATHGGItVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPET-AKAIRAAAAHRGPVYVRLGRNKVP 169
Cdd:PLN02582 441 VHDVDLQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELfHMVATAAAIDDRPSCFRYPRGNGI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 170 TV----TSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIV 245
Cdd:PLN02582 520 GVqlppNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLI 599
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504364923 246 TAEEHSIvGGLGGAVAEFLAEN----SPVPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVLTRKR 313
Cdd:PLN02582 600 TVEEGSI-GGFGSHVAQFMALDglldGKLKWRPLVLPDRYIDHGAPADQLAEAGLTPSHIAATVLNVLGQTR 670
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
5-309 |
6.62e-32 |
|
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: 125.12 E-value: 6.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 5 IATRDAYGQTLAELGEENGSVVVLDADLSGSTKT------SVFAKKFPDRFFNMGIAEANM------------Vgtaagl 66
Cdd:COG0021 352 VATRKASGKVLNALAPVLPELIGGSADLAGSNKTtikgagSFSPEDPSGRNIHFGVREHAMgaimngialhggL------ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 67 aaagkIPFVSTFAIFAvgrawEQVRQSL---AYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGP 143
Cdd:COG0021 426 -----RPYGGTFLVFS-----DYMRPAIrlaALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASLRAIPNLDVIRPADAN 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 144 ETAKAIRAAAAHR-GPVYVRLGRNKVPTVTSTDTPFE-IGKG---VQLADGT-DLTFVTTGLMTAQALATAELLSQEGIS 217
Cdd:COG0021 496 ETAAAWKLALERKdGPTALILSRQNLPTLDRTAAAAEgVAKGayvLADAEGTpDVILIATGSEVSLAVEAAELLAAEGIK 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 218 ARVIHMatikP----------------LDGEILRRAAQETGaiVTAEEHSIVgGLGGAVaeflaenspvplkrVGInDRF 281
Cdd:COG0021 576 VRVVSM----PswelfeaqdaayresvLPPAVRARVAVEAG--VTDGWYKYV-GLDGAV--------------IGI-DTF 633
|
330 340
....*....|....*....|....*...
gi 504364923 282 GLSGKAEELLKYFGLMPADLAEAAREVL 309
Cdd:COG0021 634 GASAPAKVLFEEFGFTVENVVAAAKELL 661
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
9-313 |
6.39e-30 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 119.43 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 9 DAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFaVGRAWE 88
Cdd:PLN02225 385 DCFVEALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSAF-LQRAYD 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 89 QVRQSLAYPKANVKVVATHGGItVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPE-TAKAIRAAAAHRGPVYVRLGRNK 167
Cdd:PLN02225 464 QVVHDVDRQRKAVRFVITSAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDElVNMVATAAYVTDRPVCFRFPRGS 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 168 VPT---VTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAI 244
Cdd:PLN02225 543 IVNmnyLVPTGLPIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFL 622
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504364923 245 VTAEEhSIVGGLGGAVAEFLAENSP----VPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVLTRKR 313
Cdd:PLN02225 623 ITVEE-GCVGGFGSHVAQFIALDGQldgnIKWRPIVLPDGYIEEASPREQLALAGLTGHHIAATALSLLGRTR 694
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
4-165 |
7.56e-30 |
|
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: 110.27 E-value: 7.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 4 MIATRDAYGQTLAELGeengsvvvldadlsgstktsvfakkfpdrfFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFAV 83
Cdd:smart00861 2 KIATRKAFGEALAELA------------------------------IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFD 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 84 gRAWEQVRQSLAYPKANVkVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHRGPVYVRL 163
Cdd:smart00861 52 -RAKDQIRSAGASGNVPV-VFRHDGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRL 129
|
..
gi 504364923 164 GR 165
Cdd:smart00861 130 ER 131
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
5-312 |
1.35e-27 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 112.85 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 5 IATRDAYGQTLAELGEENGSVVVLDADLSGSTKTSV-----FAKKFPD-RFFNMGIAEANMVGTAAGLAAAGK-IPFVST 77
Cdd:PTZ00089 355 IATRKASENVLNPLFQILPELIGGSADLTPSNLTRPkeandFTKASPEgRYIRFGVREHAMCAIMNGIAAHGGfIPFGAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 78 FAIFaVGRAWEQVRQSlAYPKANVKVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAH-R 156
Cdd:PTZ00089 435 FLNF-YGYALGAVRLA-ALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYALALANaK 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 157 GPVYVRLGRNKVPTVTSTDTPFEIGKGVQLADGTD---LTFVTTGLMTAQALATAELLSQEgISARVIHMATIkpldgEI 233
Cdd:PTZ00089 513 TPTILCLSRQNTPPLPGSSIEGVLKGAYIVVDFTNspqLILVASGSEVSLCVEAAKALSKE-LNVRVVSMPCW-----EL 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504364923 234 LRRAAQETGAIVTAEEHSIVGGLGGAVAEFLAENSPVplkRVGINdRFGLSGKAEELLKYFGLMPADLAEAAREVLTRK 312
Cdd:PTZ00089 587 FDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHV---HVGIS-GFGASAPANALYKHFGFTVENVVEKARALAARF 661
|
|
| PLN02790 |
PLN02790 |
transketolase |
30-309 |
8.27e-27 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 110.50 E-value: 8.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 30 ADLSGSTKTSV-----FAKKFP-DRFFNMGIAEANM--VGTAAGLAAAGKIPFVSTFAIFaVGRAWEQVRQSlAYPKANV 101
Cdd:PLN02790 369 ADLASSNMTLLkdfgdFQKDTPeERNVRFGVREHGMgaICNGIALHSSGLIPYCATFFVF-TDYMRAAMRLS-ALSEAGV 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 102 KVVATHGGITVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIRAAAAHR-GPVYVRLGRNKVPTV--TSTDtpf 178
Cdd:PLN02790 447 IYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKVAVTNRkRPTVLALSRQKVPNLpgTSIE--- 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 179 EIGKGVQLADGT------DLTFVTTGLMTAQALATAELLSQEGISARVIHM----------ATIKP--LDGEILRRAAQE 240
Cdd:PLN02790 524 GVEKGGYVISDNssgnkpDLILIGTGSELEIAAKAAKELRKEGKKVRVVSMvcwelfeeqsDEYKEsvLPSSVTARVSVE 603
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504364923 241 TGaiVTAEEHSIVGGLGgavaeflaenspvplKRVGInDRFGLSGKAEELLKYFGLMPADLAEAAREVL 309
Cdd:PLN02790 604 AG--STFGWEKYVGSKG---------------KVIGV-DRFGASAPAGILYKEFGFTVENVVAAAKSLL 654
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
13-265 |
4.92e-24 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 102.10 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 13 QTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFaVGRAWEQVRQ 92
Cdd:PLN02234 365 EALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSF-MQRAYDQVVH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 93 SLAYPKANVKVVATHGGItVGEDGGSHQSVEDIAIMRAVPNMTVIVPADGPET-AKAIRAAAAHRGPVYVRLGRNKVPTV 171
Cdd:PLN02234 444 DVDLQKLPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELfNMVATAAAIDDRPSCFRYHRGNGIGV 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 172 T----STDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIVTA 247
Cdd:PLN02234 523 SlppgNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITV 602
|
250
....*....|....*...
gi 504364923 248 EEHSIvGGLGGAVAEFLA 265
Cdd:PLN02234 603 EEGSI-GGFGSHVVQFLA 619
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
9-309 |
1.62e-22 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 97.77 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 9 DAYGQTLAELGEENGSVVVLDADLSGSTKTSVFAKKFPDRFFNMGIAEANMVGTAAGLAAAGKIPFVSTFAIFaVGRAWE 88
Cdd:PRK12315 282 SVTLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTF-LQRAYD 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 89 QVRQSLAYPKANVKVVATHGGITVGEDggSHQSVEDIAIMRAVPNMTVIVPADGPETAKAIR-AAAAHRGPVYVRLGRNK 167
Cdd:PRK12315 361 QLSHDLAINNNPAVMIVFGGSISGNDV--THLGIFDIPMISNIPNLVYLAPTTKEELIAMLEwALTQHEHPVAIRVPEHG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 168 VPTVTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQE-GISARVIHMATIKPLDGEILRRAAQETGAIVT 246
Cdd:PRK12315 439 VESGPTVDTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELLEKLKEDHELVVT 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504364923 247 AEEHSIVGGLGGAVAEFLAeNSPVPLKRVGINDRFGLSGKAEELLKYFGLMPADLAEAAREVL 309
Cdd:PRK12315 519 LEDGILDGGFGEKIARYYG-NSDMKVLNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDILSVL 580
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
171-309 |
2.56e-17 |
|
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 439793 [Multi-domain] Cd Length: 325 Bit Score: 80.83 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 171 VTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIVTAEEH 250
Cdd:COG0022 183 VPEEDYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKTGRLVVVDEA 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504364923 251 SIVGGLGGAVAEFLAEN------SPVplKRVGIND-RFGLSGKAEELlkyfgLMP--ADLAEAAREVL 309
Cdd:COG0022 263 PRTGGFGAEIAARIAEEafdyldAPV--KRVTGPDtPIPYAPALEKA-----YLPsaDRIVAAVRELL 323
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
8-309 |
3.05e-17 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 81.18 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 8 RDAYGQTLAELGEENGSVVVLDADLS---GSTKTSV-FAKKF-PDRFFNMGIAEANMVGTAAGLAAAGKIPFVS-TFAIF 81
Cdd:PTZ00182 38 REAINSALDEELARDPKVFVLGEDVAqygGVYKCTKgLLDKYgPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEfMFADF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 82 AVgRAWEQVRQSLA---YPKA---NVKVV--ATHGGitVGEDGGSH-QSVEdiAIMRAVPNMTVIVPADGPETAKAIRAA 152
Cdd:PTZ00182 118 IF-PAFDQIVNEAAkyrYMSGgqfDCPIVirGPNGA--VGHGGAYHsQSFE--AYFAHVPGLKVVAPSDPEDAKGLLKAA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 153 AAHRGPV----YVRLGRNKVPTVTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKP 228
Cdd:PTZ00182 193 IRDPNPVvffePKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 229 LDGEILRRAAQETGAIVTAEEHSIVGGLGGAVAEFLAENS----PVPLKRV-GINDRFGLSGKAEELlkyfgLMP--ADL 301
Cdd:PTZ00182 273 WDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMEDCflylEAPIKRVcGADTPFPYAKNLEPA-----YLPdkEKV 347
|
....*...
gi 504364923 302 AEAAREVL 309
Cdd:PTZ00182 348 VEAAKRVL 355
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
170-312 |
1.82e-16 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 78.61 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 170 TVTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIVTAEE 249
Cdd:PRK09212 182 EVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKTNRLVVVEE 261
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504364923 250 HSIVGGLGGAVAEFLAENS----PVPLKRVgindrfglSGK------AEELLKYFGLMPADLAEAAREVLTRK 312
Cdd:PRK09212 262 GWPFAGVGAEIAALIMKEAfdylDAPVERV--------TGKdvplpyAANLEKLALPSEEDIIEAVKKVCYRS 326
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
171-275 |
2.36e-11 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 63.69 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 171 VTSTDTPFEIGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIVTAEEH 250
Cdd:PLN02683 210 VLDSSFVLPIGKAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEG 289
|
90 100
....*....|....*....|....*....
gi 504364923 251 SIVGGLGGAVAEFLAENS----PVPLKRV 275
Cdd:PLN02683 290 WPQHGVGAEICASVVEESfdylDAPVERI 318
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
180-261 |
7.02e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 59.55 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 180 IGKGVQLADGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIVTAEEHSIVGGLGGA 259
Cdd:PRK11892 331 IGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAE 410
|
..
gi 504364923 260 VA 261
Cdd:PRK11892 411 IA 412
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
188-267 |
3.96e-04 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 41.65 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504364923 188 DGTDLTFVTTGLMTAQALATAELLSQEGISARVIHMATIKPLDGEILRRAAQETGAIVTAEEHSIVGGLGGAVAEFLAEN 267
Cdd:CHL00144 200 PGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEH 279
|
|
| |
