|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
8-311 |
4.62e-170 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 473.80 E-value: 4.62e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 8 YKGMRKGYGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFAS 87
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 88 GRAWEIIRNLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRM 167
Cdd:COG3958 83 GRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 168 PRRDTEIIYenEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIKKA---N 244
Cdd:COG3958 163 GRGAVPVVY--DEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAarkT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506213855 245 DFVVTVEDHSIIGGLGGAVAEVIASNgLNKKLLRIGINDVFGRSGKADELLKHYGLDGESIAKRIME 311
Cdd:COG3958 241 GAVVTAEEHSIIGGLGSAVAEVLAEN-YPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKE 306
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
13-169 |
7.45e-82 |
|
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: 244.66 E-value: 7.45e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 13 KGYGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFaSGRAWE 92
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFF-LQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506213855 93 IIRNLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRMPR 169
Cdd:cd07033 80 QIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
15-311 |
2.13e-73 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 236.52 E-value: 2.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 15 YGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTG-KIVFA--SSFAMfasgRAW 91
Cdd:PRK05444 285 FGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGlKPVVAiySTFLQ----RAY 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 92 -EIIRNlVAYPKLNVKVVATHAGItVGEDGASHQMCEDIAIMRAIPNMVVIAPTDyyhtKNVIR-----VIAEYKGPVYV 165
Cdd:PRK05444 361 dQVIHD-VALQNLPVTFAIDRAGL-VGADGPTHQGAFDLSYLRCIPNMVIMAPSD----ENELRqmlytALAYDDGPIAI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 166 RMPrRDTEIIYENEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKengiSAEIVEISTIKPIDEKIIK---K 242
Cdd:PRK05444 435 RYP-RGNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLelaA 509
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506213855 243 ANDFVVTVEDHSIIGGLGGAVAEVIASNGLNKKLLRIGINDVFGRSGKADELLKHYGLDGESIAKRIME 311
Cdd:PRK05444 510 KHDLVVTVEEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILE 578
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
11-170 |
9.35e-55 |
|
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: 176.20 E-value: 9.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 11 MRKGYGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPD---RFFNAGVAEQNMIGMAAGLATTG--KIVFASSFAMF 85
Cdd:pfam02779 5 TRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATFSDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 86 ASgRAWEIIRNLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIR--VIAEYKGPV 163
Cdd:pfam02779 85 LN-RADDAIRHGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRaaIRRDGRKPV 163
|
....*..
gi 506213855 164 YVRMPRR 170
Cdd:pfam02779 164 VLRLPRQ 170
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
39-169 |
5.61e-39 |
|
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: 134.15 E-value: 5.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 39 STQTAmFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFASgRAWEIIRNLVAYPKLNVkVVATHAGITVGE 118
Cdd:smart00861 4 ATRKA-FGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFD-RAKDQIRSAGASGNVPV-VFRHDGGGGVGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 506213855 119 DGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRMPR 169
Cdd:smart00861 81 DGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
8-311 |
4.62e-170 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 473.80 E-value: 4.62e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 8 YKGMRKGYGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFAS 87
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 88 GRAWEIIRNLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRM 167
Cdd:COG3958 83 GRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 168 PRRDTEIIYenEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIKKA---N 244
Cdd:COG3958 163 GRGAVPVVY--DEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAarkT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506213855 245 DFVVTVEDHSIIGGLGGAVAEVIASNgLNKKLLRIGINDVFGRSGKADELLKHYGLDGESIAKRIME 311
Cdd:COG3958 241 GAVVTAEEHSIIGGLGSAVAEVLAEN-YPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKE 306
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
13-169 |
7.45e-82 |
|
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: 244.66 E-value: 7.45e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 13 KGYGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFaSGRAWE 92
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSFF-LQRAYD 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506213855 93 IIRNLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRMPR 169
Cdd:cd07033 80 QIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
16-311 |
7.37e-78 |
|
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: 249.16 E-value: 7.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 16 GETLVELGKKYENLVVLDAdlsgstqtAM--------FAKEFPDRFFNAGVAEQNMIGMAAGLATTGKI-VFA--SSFAM 84
Cdd:COG1154 324 GDTLVELAEKDPRIVAITA--------AMpegtgldkFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKpVVAiySTFLQ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 85 fasgRAW-EIIRNlVAYPKLNVKVVATHAGItVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPV 163
Cdd:COG1154 396 ----RAYdQVIHD-VALQNLPVTFAIDRAGL-VGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPT 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 164 YVRMPRRDTEIIYENEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIKKA 243
Cdd:COG1154 470 AIRYPRGNGPGVELPAELEPLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILEL 549
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506213855 244 ---NDFVVTVEDHSIIGGLGGAVAEVIASNGLNKKLLRIGINDVFGRSGKADELLKHYGLDGESIAKRIME 311
Cdd:COG1154 550 areHDLVVTVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILE 620
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
15-311 |
2.13e-73 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 236.52 E-value: 2.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 15 YGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTG-KIVFA--SSFAMfasgRAW 91
Cdd:PRK05444 285 FGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGlKPVVAiySTFLQ----RAY 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 92 -EIIRNlVAYPKLNVKVVATHAGItVGEDGASHQMCEDIAIMRAIPNMVVIAPTDyyhtKNVIR-----VIAEYKGPVYV 165
Cdd:PRK05444 361 dQVIHD-VALQNLPVTFAIDRAGL-VGADGPTHQGAFDLSYLRCIPNMVIMAPSD----ENELRqmlytALAYDDGPIAI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 166 RMPrRDTEIIYENEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKengiSAEIVEISTIKPIDEKIIK---K 242
Cdd:PRK05444 435 RYP-RGNGVGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLelaA 509
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506213855 243 ANDFVVTVEDHSIIGGLGGAVAEVIASNGLNKKLLRIGINDVFGRSGKADELLKHYGLDGESIAKRIME 311
Cdd:PRK05444 510 KHDLVVTVEEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILE 578
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
12-309 |
1.80e-72 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 234.26 E-value: 1.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 12 RKGYGETLVELGKKYENLVVLDADLSGSTQTAMFA------KEFPDRFFNAGVAEQNMIGMAAGLATTG-KIVFASSFAM 84
Cdd:PRK05899 284 RKASGKALNALAKALPELVGGSADLAGSNNTKIKGskdfapEDYSGRYIHYGVREFAMAAIANGLALHGgFIPFGGTFLV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 85 FASgRAWEIIRnLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYK-GPV 163
Cdd:PRK05899 364 FSD-YARNAIR-LAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALERKdGPS 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 164 YVRMPRRDTEIIYENEEEATFEIGkGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKiikka 243
Cdd:PRK05899 442 ALVLTRQNLPVLERTAQEEGVAKG-GYVLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ----- 515
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506213855 244 ndfvvtvEDHSIIGGLGGAVAEVIA-----SNGLNK----KLLRIGINDvFGRSGKADELLKHYGLDGESIAKRI 309
Cdd:PRK05899 516 -------DAAYKESVLPAAVTARVAveagvADGWYKyvglDGKVLGIDT-FGASAPADELFKEFGFTVENIVAAA 582
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
11-170 |
9.35e-55 |
|
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: 176.20 E-value: 9.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 11 MRKGYGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPD---RFFNAGVAEQNMIGMAAGLATTG--KIVFASSFAMF 85
Cdd:pfam02779 5 TRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEATFSDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 86 ASgRAWEIIRNLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIR--VIAEYKGPV 163
Cdd:pfam02779 85 LN-RADDAIRHGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRaaIRRDGRKPV 163
|
....*..
gi 506213855 164 YVRMPRR 170
Cdd:pfam02779 164 VLRLPRQ 170
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
15-309 |
2.95e-50 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 176.07 E-value: 2.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 15 YGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTG-KIVFA--SSFAMfasgRAW 91
Cdd:PRK12571 325 FGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGlKPFCAvySTFLQ----RGY 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 92 EIIRNLVAYPKLNVKVVATHAGITvGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEY-KGPVYVRMPRR 170
Cdd:PRK12571 401 DQLLHDVALQNLPVRFVLDRAGLV-GADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHdDGPIAVRFPRG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 171 DTEIIYENEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIKKA--NDFVV 248
Cdd:PRK12571 480 EGVGVEIPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLvrHHIVV 559
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506213855 249 TVEDHSIIGGLGGAVAEVIASNGLNKKLLRI---GINDVFGRSGKADELLKHYGLDGESIAKRI 309
Cdd:PRK12571 560 IVEEQGAMGGFGAHVLHHLADTGLLDGGLKLrtlGLPDRFIDHASREEMYAEAGLTAPDIAAAV 623
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
39-169 |
5.61e-39 |
|
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: 134.15 E-value: 5.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 39 STQTAmFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFASgRAWEIIRNLVAYPKLNVkVVATHAGITVGE 118
Cdd:smart00861 4 ATRKA-FGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFD-RAKDQIRSAGASGNVPV-VFRHDGGGGVGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 506213855 119 DGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRMPR 169
Cdd:smart00861 81 DGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
15-272 |
2.81e-37 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 140.81 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 15 YGETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFASgRAWEII 94
Cdd:PLN02582 362 FAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFLQ-RGYDQV 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 95 RNLVAYPKLNVKVVATHAGItVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKG-PVYVRMPRRD-- 171
Cdd:PLN02582 441 VHDVDLQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDrPSCFRYPRGNgi 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 172 TEIIYENEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIK---KANDFVV 248
Cdd:PLN02582 520 GVQLPPNNKGIPIEVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRslaKSHEVLI 599
|
250 260
....*....|....*....|....
gi 506213855 249 TVEDHSiIGGLGGAVAEVIASNGL 272
Cdd:PLN02582 600 TVEEGS-IGGFGSHVAQFMALDGL 622
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
187-305 |
3.58e-36 |
|
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: 126.56 E-value: 3.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 187 GKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIKKA---NDFVVTVEDHSIIGGLGGAV 263
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESvkkTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 506213855 264 AEVIASN---GLNKKLLRIGINDvFGRSGKADELLKHYGLDGESI 305
Cdd:pfam02780 81 AAALAEEafdGLDAPVLRVGGPD-FPEPGSADELEKLYGLTPEKI 124
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
17-306 |
1.15e-33 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 130.61 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 17 ETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFASgRAWEIIRN 96
Cdd:PLN02225 389 EALVMEAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSAFLQ-RAYDQVVH 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 97 LVAYPKLNVKVVATHAGItVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKG-PVYVRMPRrdTEII 175
Cdd:PLN02225 468 DVDRQRKAVRFVITSAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAYVTDrPVCFRFPR--GSIV 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 176 YENEEEAT---FEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIK---KANDFVVT 249
Cdd:PLN02225 545 NMNYLVPTglpIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRdlcQNHKFLIT 624
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 250 VEDhSIIGGLGGAVAEVIASNGL---NKKLLRIGINDVFGRSGKADELLKHYGLDGESIA 306
Cdd:PLN02225 625 VEE-GCVGGFGSHVAQFIALDGQldgNIKWRPIVLPDGYIEEASPREQLALAGLTGHHIA 683
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
17-272 |
8.40e-31 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 122.13 E-value: 8.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 17 ETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFASgRAWEIIRN 96
Cdd:PLN02234 365 EALIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQ-RAYDQVVH 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 97 LVAYPKLNVKVVATHAGItVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKG-PVYVRMPRRDTEII 175
Cdd:PLN02234 444 DVDLQKLPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDrPSCFRYHRGNGIGV 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 176 Y--ENEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKIIK---KANDFVVTV 250
Cdd:PLN02234 523 SlpPGNKGVPLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRslaKSHEVLITV 602
|
250 260
....*....|....*....|..
gi 506213855 251 EDHSiIGGLGGAVAEVIASNGL 272
Cdd:PLN02234 603 EEGS-IGGFGSHVVQFLALDGL 623
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
12-316 |
8.19e-29 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 116.31 E-value: 8.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 12 RKGYGETLVELGKKYENLVVLDADLSGSTQTA-----MFAKEFPD-RFFNAGVAEQNMIGMAAGLATTGKIV-FASSFAM 84
Cdd:PTZ00089 358 RKASENVLNPLFQILPELIGGSADLTPSNLTRpkeanDFTKASPEgRYIRFGVREHAMCAIMNGIAAHGGFIpFGATFLN 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 85 FaSGRAWEIIRnLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRV-IAEYKGPV 163
Cdd:PTZ00089 438 F-YGYALGAVR-LAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYALaLANAKTPT 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 164 YVRMPRRDTEIIYENEEEATFeigKGKILVEGED----LTIIATGEEVPEALKAGEILKENgISAEIVEIstikPIDEKI 239
Cdd:PTZ00089 516 ILCLSRQNTPPLPGSSIEGVL---KGAYIVVDFTnspqLILVASGSEVSLCVEAAKALSKE-LNVRVVSM----PCWELF 587
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506213855 240 IKKANDFVVTVEDHsiiGGLGGAVAEVIASNGLNKKL-LRIGINDvFGRSGKADELLKHYGLDGESIAKRIMEETSKF 316
Cdd:PTZ00089 588 DQQSEEYQQSVLPS---GGVPVLSVEAYVSFGWEKYShVHVGISG-FGASAPANALYKHFGFTVENVVEKARALAARF 661
|
|
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
12-311 |
2.40e-28 |
|
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: 114.72 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 12 RKGYGETLVELGKKYENLVVLDADLSGSTQTAM-----FAKEFPD-RFFNAGVAEQnmiGMAA---GLATTGK-IVFASS 81
Cdd:COG0021 355 RKASGKVLNALAPVLPELIGGSADLAGSNKTTIkgagsFSPEDPSgRNIHFGVREH---AMGAimnGIALHGGlRPYGGT 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 82 FAMFAsgrawEIIRN---LVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIAE 158
Cdd:COG0021 432 FLVFS-----DYMRPairLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLALE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 159 YK-GPVYVRMPRRDTEIIYENEEEATfEIGKGK-ILVEGE---DLTIIATGEEVPEALKAGEILKENGISAEIV-----E 228
Cdd:COG0021 507 RKdGPTALILSRQNLPTLDRTAAAAE-GVAKGAyVLADAEgtpDVILIATGSEVSLAVEAAELLAAEGIKVRVVsmpswE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 229 ISTIKPID--EKIIKKANDFVVTVEDHSIIG-----GLGGAVaeviasnglnkkllrIGINDvFGRSGKADELLKHYGLD 301
Cdd:COG0021 586 LFEAQDAAyrESVLPPAVRARVAVEAGVTDGwykyvGLDGAV---------------IGIDT-FGASAPAKVLFEEFGFT 649
|
330
....*....|
gi 506213855 302 GESIAKRIME 311
Cdd:COG0021 650 VENVVAAAKE 659
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
16-311 |
1.88e-26 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 109.32 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 16 GETLVELGKKYENLVVLDADLSGSTQTAMFAKEFPDRFFNAGVAEQNMIGMAAGLATTG--KIVFA-SSFAMfasgRAWE 92
Cdd:PRK12315 285 LDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGarPVIFVnSTFLQ----RAYD 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 93 IIRNLVAYPKLNVKVVAthAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIR-VIAEYKGPVYVRMPrrD 171
Cdd:PRK12315 361 QLSHDLAINNNPAVMIV--FGGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEwALTQHEHPVAIRVP--E 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 172 TEIIYENEEEATFEIGKGKILVEGEDLTIIATGEEVPEALKAGEILKEN-GISAEIVEISTIKPIDEKI---IKKANDFV 247
Cdd:PRK12315 437 HGVESGPTVDTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELlekLKEDHELV 516
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506213855 248 VTVEDHSIIGGLGGAVAEVIASNGLnkKLLRIGINDVFGRSGKADELLKHYGLDGESIAKRIME 311
Cdd:PRK12315 517 VTLEDGILDGGFGEKIARYYGNSDM--KVLNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDILS 578
|
|
| PLN02790 |
PLN02790 |
transketolase |
13-311 |
6.42e-23 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 98.94 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 13 KGYGET-LVELGKKYENLVVLDADLSGSTQTAM-----FAKEFPD----RFfnaGVAEQNMIGMAAGLA--TTGKIVFAS 80
Cdd:PLN02790 347 RNLSQKcLNALAKVLPGLIGGSADLASSNMTLLkdfgdFQKDTPEernvRF---GVREHGMGAICNGIAlhSSGLIPYCA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 81 SFAMFaSGRAWEIIRnLVAYPKLNVKVVATHAGITVGEDGASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRV-IAEY 159
Cdd:PLN02790 424 TFFVF-TDYMRAAMR-LSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKVaVTNR 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 160 KGPVYVRMPRRDTEIIyenEEEATFEIGKGKILVEGE------DLTIIATGEEVPEALKAGEILKENGISAEIV-----E 228
Cdd:PLN02790 502 KRPTVLALSRQKVPNL---PGTSIEGVEKGGYVISDNssgnkpDLILIGTGSELEIAAKAAKELRKEGKKVRVVsmvcwE 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 229 ISTIKPID--EKIIKKANDFVVTVEDHSIIG-----GLGGAVaeviasnglnkkllrIGINDvFGRSGKADELLKHYGLD 301
Cdd:PLN02790 579 LFEEQSDEykESVLPSSVTARVSVEAGSTFGwekyvGSKGKV---------------IGVDR-FGASAPAGILYKEFGFT 642
|
330
....*....|
gi 506213855 302 GESIAKRIME 311
Cdd:PLN02790 643 VENVVAAAKS 652
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
50-269 |
1.50e-21 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 93.51 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 50 PDRFFNAGVAEQNMIGMAAGLATTG-----KIVFASsFAMfasgRAWEIIRNLVA---Y---PKLNVKVVATHAGITVGE 118
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNGlrpiaEFMFAD-FIF----PAFDQIVNEAAkyrYmsgGQFDCPIVIRGPNGAVGH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 119 DGASHQMCEDiAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRMPrrdtEIIYENEEEA------TFEIGKGKIL 192
Cdd:PTZ00182 156 GGAYHSQSFE-AYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEP----KLLYRESVEVvpeadyTLPLGKAKVV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 193 VEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPID----EKIIKKANDfVVTVEDHSIIGGLGgavAEVIA 268
Cdd:PTZ00182 231 REGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDretiVKSVKKTGR-CVIVHEAPPTCGIG---AEIAA 306
|
.
gi 506213855 269 S 269
Cdd:PTZ00182 307 Q 307
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
50-284 |
5.24e-17 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 80.15 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 50 PDRFFNAGVAEQNMIGMAAGLATTG--KIV-FAS-SFAMFASGrawEIIR-----NLVAYPKLNVKVVATHAGITVGEDG 120
Cdd:PRK09212 50 PKRVIDTPITEHGFAGLAVGAAFAGlrPIVeFMTfNFSMQAID---QIVNsaaktNYMSGGQLKCPIVFRGPNGAAARVA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 121 ASHQMCEDiAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRmprrDTEIIYEN-----EEEATFEIGKGKILVEG 195
Cdd:PRK09212 127 AQHSQCYA-AWYSHIPGLKVVAPYFAADCKGLLKTAIRDPNPVIFL----ENEILYGHshevpEEEESIPIGKAAILREG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 196 EDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKII----KKANDfVVTVEDHSIIGGLGGAVAEVIASNG 271
Cdd:PRK09212 202 SDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIiesvKKTNR-LVVVEEGWPFAGVGAEIAALIMKEA 280
|
250
....*....|....*.
gi 506213855 272 ---LNKKLLRIGINDV 284
Cdd:PRK09212 281 fdyLDAPVERVTGKDV 296
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
120-284 |
4.03e-13 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 69.08 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 120 GASHQMCEdIAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPVYVRmprrDTEIIYENE----EEA-----TFEIGKGK 190
Cdd:PLN02683 149 GAQHSQCF-AAWYSSVPGLKVLAPYSSEDARGLLKAAIRDPDPVVFL----ENELLYGESfpvsAEVldssfVLPIGKAK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 191 ILVEGEDLTIIATGEEVPEALKAGEILKENGISAEIVEISTIKPIDEKII----KKANDfVVTVEDHSIIGGLGGAVAEV 266
Cdd:PLN02683 224 IEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTInasvRKTNR-LVTVEEGWPQHGVGAEICAS 302
|
170 180
....*....|....*....|.
gi 506213855 267 I---ASNGLNKKLLRIGINDV 284
Cdd:PLN02683 303 VveeSFDYLDAPVERIAGADV 323
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
135-284 |
2.33e-11 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 64.17 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 135 IPNMVVIAPTDyyhtknvirvIAEYKG--PVYVRMPrrDTEIIYENE------------EEATFEIGKGKILVEGEDLTI 200
Cdd:PRK11892 278 IPGLKVVAPYS----------AADAKGllKAAIRDP--NPVIFLENEilygqsfdvpklDDFVLPIGKARIHREGKDVTI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 201 IATGEEVPEALKAGEILKENGISAEIVEISTIKPID-EKII---KKANDfVVTVEDHSIIGGLGGAVAEVIASNG---LN 273
Cdd:PRK11892 346 VSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDtETIVesvKKTNR-LVTVEEGWPQSGVGAEIAARVMEQAfdyLD 424
|
170
....*....|.
gi 506213855 274 KKLLRIGINDV 284
Cdd:PRK11892 425 APVLRVTGKDV 435
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
52-270 |
5.28e-06 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 47.43 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 52 RFFNAGVAEQNMIGMAAGLATTGKIVFASSFAMFASGRAWEIIRN---LVAYPK---LNVKVVATHAGITVGEDGASH-Q 124
Cdd:CHL00144 52 RVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFNQISNnagMLHYTSggnFTIPIVIRGPGGVGRQLGAEHsQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 125 MCEdiAIMRAIPNMVVIAPTDYYHTKNVIRVIAEYKGPV----YVRMPRRDTEIIyenEEEATFEIGKGKILVEGEDLTI 200
Cdd:CHL00144 132 RLE--SYFQSVPGLQIVACSTPYNAKGLLKSAIRSNNPViffeHVLLYNLKEEIP---DNEYLLPLEKAEVVRPGNDITI 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506213855 201 IATGEEVPEALKAGEILKENGISAEIVEISTIKPID----EKIIKKANDfVVTVEDHSIIGGLGGAVAEVIASN 270
Cdd:CHL00144 207 LTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDlgtiSKSVKKTHK-VLIVEECMKTGGIGAELIAQINEH 279
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
45-169 |
1.02e-04 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; 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 group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 41.95 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213855 45 FAKEFPDRFFNAGVAEQNMIGMAAGLATTGK----IVFASSFAMFAsgraweiIRNLVAYPKLNVKVVA-THAGITVGED 119
Cdd:cd06586 29 ALREGDKRIIDTVIHELGAAGAAAGYARAGGppvvIVTSGTGLLNA-------INGLADAAAEHLPVVFlIGARGISAQA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 506213855 120 GASHQMCEDIAIMRAIPNMVVIAPTDYYHTKNVIRVIA---EYKGPVYVRMPR 169
Cdd:cd06586 102 KQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRtayASQGPVVVRLPR 154
|
|
| |
