|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
1-310 |
3.83e-146 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 413.33 E-value: 3.83e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 1 MNKIANRQVMCEVLMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPAC 80
Cdd:COG3958 1 MEKKAMRDAFGEALVELA-EEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 81 FLSMRSIEQVKVDVAYSDTNVKLIGISGGVSYGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPAY 160
Cdd:COG3958 80 FLTGRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 161 VRLGRNAVEDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAE 240
Cdd:COG3958 160 LRLGRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821746 241 TKLLISIEEHSIYGGLGAAVSEVVSSS-PTSIRHliLGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNL 310
Cdd:COG3958 240 TGAVVTAEEHSIIGGLGSAVAEVLAENyPVPLRR--IGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
8-165 |
1.56e-60 |
|
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: 189.96 E-value: 1.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 8 QVMCEVLMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPAcFLSMRSI 87
Cdd:cd07033 1 KAFGEALLELA-KKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFS-FFLQRAY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489821746 88 EQVKVDVAYSDTNVKLIGISGGVSYGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPAYVRLGR 165
Cdd:cd07033 79 DQIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
14-310 |
1.51e-50 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 176.04 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 14 LMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSIEQVKVD 93
Cdd:PRK05444 289 LCELA-EKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQ-RAYDQVIHD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 94 VAYSDTNVKLI----GISggvsyGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDY-LLQSNRPAYVRLGR-NA 167
Cdd:PRK05444 367 VALQNLPVTFAidraGLV-----GADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTaLAYDDGPIAIRYPRgNG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 168 VEDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKlkgiSARVLNFSTIKPFDQGAVEAALAETKLLISI 247
Cdd:PRK05444 442 VGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTV 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821746 248 EEHSIYGGLGAAVSEVVSSSPTSIRHLILGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNL 310
Cdd:PRK05444 518 EEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
40-165 |
4.85e-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: 110.65 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 40 AFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLsMRSIEQVKVDVAYSDTNVkLIGISGGVSYGALGMSH 119
Cdd:smart00861 8 AFGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFF-DRAKDQIRSAGASGNVPV-VFRHDGGGGVGEDGPTH 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489821746 120 HSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPAYVRLGR 165
Cdd:smart00861 86 HSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
181-302 |
2.61e-25 |
|
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: 98.05 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 181 GKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAETKLLISIEEHSIYGGLGAAV 260
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489821746 261 SEVVSSspTSIRHL-----ILGIPDEPAiAGTSQEIFDYYGLSATGI 302
Cdd:pfam02780 81 AAALAE--EAFDGLdapvlRVGGPDFPE-PGSADELEKLYGLTPEKI 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
1-310 |
3.83e-146 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 413.33 E-value: 3.83e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 1 MNKIANRQVMCEVLMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPAC 80
Cdd:COG3958 1 MEKKAMRDAFGEALVELA-EEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 81 FLSMRSIEQVKVDVAYSDTNVKLIGISGGVSYGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPAY 160
Cdd:COG3958 80 FLTGRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 161 VRLGRNAVEDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAE 240
Cdd:COG3958 160 LRLGRGAVPVVYDEDYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAARK 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489821746 241 TKLLISIEEHSIYGGLGAAVSEVVSSS-PTSIRHliLGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNL 310
Cdd:COG3958 240 TGAVVTAEEHSIIGGLGSAVAEVLAENyPVPLRR--IGVPDRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
8-165 |
1.56e-60 |
|
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: 189.96 E-value: 1.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 8 QVMCEVLMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPAcFLSMRSI 87
Cdd:cd07033 1 KAFGEALLELA-KKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTFS-FFLQRAY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489821746 88 EQVKVDVAYSDTNVKLIGISGGVSYGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPAYVRLGR 165
Cdd:cd07033 79 DQIRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
8-311 |
1.01e-57 |
|
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: 196.00 E-value: 1.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 8 QVMCEVLMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSI 87
Cdd:COG1154 321 DVFGDTLVELA-EKDPRIVAITAAMPEGTGLDKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQ-RAY 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 88 EQVKVDVAYSDTNVkLIGI-SGGVSyGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPAYVRLGRN 166
Cdd:COG1154 399 DQVIHDVALQNLPV-TFAIdRAGLV-GADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 167 AVEDCYAEKPV--FQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAETKLL 244
Cdd:COG1154 477 NGPGVELPAELepLPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLV 556
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489821746 245 ISIEEHSIYGGLGAAVSEVVSSSPTSIRHLILGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNLG 311
Cdd:COG1154 557 VTVEEGVLAGGFGSAVLEFLADAGLDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIARAILELLG 623
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
14-310 |
1.51e-50 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 176.04 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 14 LMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSIEQVKVD 93
Cdd:PRK05444 289 LCELA-EKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVAIYSTFLQ-RAYDQVIHD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 94 VAYSDTNVKLI----GISggvsyGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDY-LLQSNRPAYVRLGR-NA 167
Cdd:PRK05444 367 VALQNLPVTFAidraGLV-----GADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTaLAYDDGPIAIRYPRgNG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 168 VEDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKlkgiSARVLNFSTIKPFDQGAVEAALAETKLLISI 247
Cdd:PRK05444 442 VGVELPELEPLPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTV 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489821746 248 EEHSIYGGLGAAVSEVVSSSPTSIRHLILGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNL 310
Cdd:PRK05444 518 EEGAIMGGFGSAVLEFLADHGLDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
42-306 |
1.20e-38 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 143.74 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 42 AEKFPERLVETGIAEQNIVGIAAGLA-HSGKRAFVASPACFLS-MRSieQVKVDvAYSDTNVKLIGISGGVSYGALGMSH 119
Cdd:PRK05899 324 PEDYSGRYIHYGVREFAMAAIANGLAlHGGFIPFGGTFLVFSDyARN--AIRLA-ALMKLPVIYVFTHDSIGVGEDGPTH 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 120 HSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQS-NRPAYVRLGRNAVEDCYAEKPVFQIGKAG-TLRKGNDVSILAT 197
Cdd:PRK05899 401 QPVEQLASLRAIPNLTVIRPADANETAAAWKYALERkDGPSALVLTRQNLPVLERTAQEEGVAKGGyVLRDDPDVILIAT 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 198 GEMVRVALDAREELKLKGISARVLNFSTIKPFDqgAVEAALAETKL------LISIEEHSIYGGLGAAVSEvvsssptsi 271
Cdd:PRK05899 481 GSEVHLALEAADELEAEGIKVRVVSMPSTELFD--EQDAAYKESVLpaavtaRVAVEAGVADGWYKYVGLD--------- 549
|
250 260 270
....*....|....*....|....*....|....*
gi 489821746 272 rHLILGIPDEPAiAGTSQEIFDYYGLSATGIVATV 306
Cdd:PRK05899 550 -GKVLGIDTFGA-SAPADELFKEFGFTVENIVAAA 582
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
9-314 |
3.20e-38 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 142.94 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 9 VMCEVLMKEATRnDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSIE 88
Cdd:PRK12571 324 VFGEELTKEAAE-DSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFLQ-RGYD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 89 QVKVDVAYSDTNVKLIGISGGVSyGALGMSHHSLQDIAVTRAIPNLEVILPAD------RLETEAVFDyllqsNRPAYVR 162
Cdd:PRK12571 402 QLLHDVALQNLPVRFVLDRAGLV-GADGATHAGAFDLAFLTNLPNMTVMAPRDeaelrhMLRTAAAHD-----DGPIAVR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 163 LGR-NAV-EDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAE 240
Cdd:PRK12571 476 FPRgEGVgVEIPAEGTILGIGKGRVPREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRH 555
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489821746 241 TKLLISIEEHSIyGGLGAAVSEVVSSS---PTSIRHLILGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNLGDER 314
Cdd:PRK12571 556 HIVVIVEEQGAM-GGFGAHVLHHLADTgllDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTGALARLS 631
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
40-165 |
4.85e-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: 110.65 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 40 AFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLsMRSIEQVKVDVAYSDTNVkLIGISGGVSYGALGMSH 119
Cdd:smart00861 8 AFGEALAELAIDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFF-DRAKDQIRSAGASGNVPV-VFRHDGGGGVGEDGPTH 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489821746 120 HSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPAYVRLGR 165
Cdd:smart00861 86 HSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLER 131
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
9-311 |
2.68e-29 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 117.41 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 9 VMCEVLMKEaTRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSIE 88
Cdd:PRK12315 283 VTLDYLLKK-IKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFLQ-RAYD 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 89 QVKVDVAYSDTNVKLIgISGGVSYGAlGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLL-QSNRPAYVRLGRNA 167
Cdd:PRK12315 361 QLSHDLAINNNPAVMI-VFGGSISGN-DVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALtQHEHPVAIRVPEHG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 168 VEDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLK-GISARVLNFSTIKPFDQGAVEAALAETKLLIS 246
Cdd:PRK12315 439 VESGPTVDTDYSTLKYEVTKAGEKVAILALGDFYELGEKVAKKLKEElGIDATLINPKFITGLDEELLEKLKEDHELVVT 518
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489821746 247 IEEHSIYGGLGAAVSEVVssSPTSIRHLILGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNLG 311
Cdd:PRK12315 519 LEDGILDGGFGEKIARYY--GNSDMKVLNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDILSVLK 581
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
12-314 |
2.23e-28 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 115.00 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 12 EVLMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSIEQVK 91
Cdd:PLN02582 364 EALIAEA-EVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFLQ-RGYDQVV 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 92 VDVAYSDTNVKLIGISGGVsYGALGMSHHSLQDIAVTRAIPNLEVILPADRLE------TEAVFDyllqsNRPAYVRLGR 165
Cdd:PLN02582 442 HDVDLQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAElfhmvaTAAAID-----DRPSCFRYPR 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 166 N-----AVEDCYAEKPVfQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAE 240
Cdd:PLN02582 516 GngigvQLPPNNKGIPI-EVGKGRILLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKS 594
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489821746 241 TKLLISIEEHSIyGGLGAAVSEVVS-----SSPTSIRHLILgiPDEPAIAGTSQEIFDYYGLSATGIVATVMKNLGDER 314
Cdd:PLN02582 595 HEVLITVEEGSI-GGFGSHVAQFMAldgllDGKLKWRPLVL--PDRYIDHGAPADQLAEAGLTPSHIAATVLNVLGQTR 670
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
12-314 |
3.94e-27 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 111.35 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 12 EVLMKEATRnDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSIEQVK 91
Cdd:PLN02225 389 EALVMEAEK-DRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSAFLQ-RAYDQVV 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 92 VDVAYSDTNVKLIGISGGVsYGALGMSHHSLQDIAVTRAIPNLEVILPADRLE-TEAVFDYLLQSNRPAYVRLGRNAVED 170
Cdd:PLN02225 467 HDVDRQRKAVRFVITSAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDElVNMVATAAYVTDRPVCFRFPRGSIVN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 171 CYAEKPV---FQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAETKLLISI 247
Cdd:PLN02225 546 MNYLVPTglpIEIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITV 625
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 248 EEHSIyGGLGAAVSEVVSSSPT---SIRHLILGIPDEPAIAGTSQEIFDYYGLSATGIVATVMKNLGDER 314
Cdd:PLN02225 626 EEGCV-GGFGSHVAQFIALDGQldgNIKWRPIVLPDGYIEEASPREQLALAGLTGHHIAATALSLLGRTR 694
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
181-302 |
2.61e-25 |
|
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: 98.05 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 181 GKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAETKLLISIEEHSIYGGLGAAV 260
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489821746 261 SEVVSSspTSIRHL-----ILGIPDEPAiAGTSQEIFDYYGLSATGI 302
Cdd:pfam02780 81 AAALAE--EAFDGLdapvlRVGGPDFPE-PGSADELEKLYGLTPEKI 124
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
3-168 |
6.65e-25 |
|
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: 98.39 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 3 KIANRQVMCEVLMKEATRnDSNLVVLTSDSRGSASLGAFAEKFPE---RLVETGIAEQNIVGIAAGLAHSG--KRAFVAS 77
Cdd:pfam02779 2 KIATRKASGEALAELAKR-DPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHGplLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 78 PACFlSMRSIEQVKVDVAYSDTNVKLIGISGGVSYGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFD--YLLQS 155
Cdd:pfam02779 81 FSDF-LNRADDAIRHGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRaaIRRDG 159
|
170
....*....|...
gi 489821746 156 NRPAYVRLGRNAV 168
Cdd:pfam02779 160 RKPVVLRLPRQLL 172
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
15-264 |
6.60e-24 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 100.06 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 15 MKEATRNDSNLVVLTSD--SRGSA---SLGaFAEKF-PERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSMRSIE 88
Cdd:PTZ00182 45 LDEELARDPKVFVLGEDvaQYGGVykcTKG-LLDKYgPDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 89 QVKVDVA---Y---SDTNVKLI--GISGGVSYGALgmsHHSlQDIAVTRA-IPNLEVILPADRLETEAVFDYLLQSNRPA 159
Cdd:PTZ00182 124 QIVNEAAkyrYmsgGQFDCPIVirGPNGAVGHGGA---YHS-QSFEAYFAhVPGLKVVAPSDPEDAKGLLKAAIRDPNPV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 160 ----YVRLGRNAVEDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVE 235
Cdd:PTZ00182 200 vffePKLLYRESVEVVPEADYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIV 279
|
250 260
....*....|....*....|....*....
gi 489821746 236 AALAETKLLISIEEHSIYGGLGAAVSEVV 264
Cdd:PTZ00182 280 KSVKKTGRCVIVHEAPPTCGIGAEIAAQI 308
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
12-265 |
6.73e-22 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 95.94 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 12 EVLMKEAtRNDSNLVVLTSDSRGSASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSmRSIEQVK 91
Cdd:PLN02234 365 EALIAEA-EADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFMQ-RAYDQVV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 92 VDVAYSDTNVKLIGISGGVsYGALGMSHHSLQDIAVTRAIPNLEVILPADRLE------TEAVFDyllqsNRPAYVRLGR 165
Cdd:PLN02234 443 HDVDLQKLPVRFAIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAElfnmvaTAAAID-----DRPSCFRYHR 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 166 N---AVEDCYAEKPV-FQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAET 241
Cdd:PLN02234 517 GngiGVSLPPGNKGVpLQIGRGRILRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSH 596
|
250 260
....*....|....*....|....
gi 489821746 242 KLLISIEEHSIyGGLGAAVSEVVS 265
Cdd:PLN02234 597 EVLITVEEGSI-GGFGSHVVQFLA 619
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
1-264 |
2.29e-20 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 89.78 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 1 MNKIANRQVMCEVlMKEATRNDSNlVVLTSDSRGSASlGAFA------EKF-PERLVETGIAEQNIVGIAAGLAHSGKRA 73
Cdd:PRK09212 1 MAQLTVREALRDA-MQEEMERDPK-VFLMGEEVGEYQ-GAYKvtqgllEQFgPKRVIDTPITEHGFAGLAVGAAFAGLRP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 74 FVASPACFLSMRSIEQVKVDVAysdtnvKLIGISGG------VSYGALGM-----SHHSlQDIAVTRA-IPNLEVILPAD 141
Cdd:PRK09212 78 IVEFMTFNFSMQAIDQIVNSAA------KTNYMSGGqlkcpiVFRGPNGAaarvaAQHS-QCYAAWYShIPGLKVVAPYF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 142 RLETEAVFDYLLQSNRPayVRLGRNAV-----EDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGI 216
Cdd:PRK09212 151 AADCKGLLKTAIRDPNP--VIFLENEIlyghsHEVPEEEESIPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489821746 217 SARVLNFSTIKPFDQGAVEAALAETKLLISIEEHSIYGGLGAAVSEVV 264
Cdd:PRK09212 229 SVEVIDLRTLRPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALI 276
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
43-264 |
5.40e-18 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 83.33 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 43 EKF-PERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSMRSIEQVKVDVAYS------DTNVKLI-----GISGGV 110
Cdd:PLN02683 69 QKYgPDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTnymsagQISVPIVfrgpnGAAAGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 111 SygalgmSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLLQSNRPayVRLGRNAV---------EDCYAEKPVFQIG 181
Cdd:PLN02683 149 G------AQHSQCFAAWYSSVPGLKVLAPYSSEDARGLLKAAIRDPDP--VVFLENELlygesfpvsAEVLDSSFVLPIG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 182 KAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAETKLLISIEEHSIYGGLGAAVS 261
Cdd:PLN02683 221 KAKIEREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEIC 300
|
...
gi 489821746 262 EVV 264
Cdd:PLN02683 301 ASV 303
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
46-264 |
6.47e-12 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 65.71 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 46 PERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSMRSIEQVKVDVAysdtnvKLIGISGG------VSYGALGMS- 118
Cdd:PRK11892 188 ARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFMTFNFAMQAIDQIINSAA------KTLYMSGGqmgcpiVFRGPNGAAa 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 119 ----HHSlQDIAVTRA-IPNLEVILP---AD---------RLETEAVFdylLQsNRPAYVRLGRNAVEDCYaekpVFQIG 181
Cdd:PRK11892 262 rvaaQHS-QDYAAWYShIPGLKVVAPysaADakgllkaaiRDPNPVIF---LE-NEILYGQSFDVPKLDDF----VLPIG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 182 KAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAETKLLISIEEHSIYGGLGAAVS 261
Cdd:PRK11892 333 KARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIA 412
|
...
gi 489821746 262 EVV 264
Cdd:PRK11892 413 ARV 415
|
|
| PLN02790 |
PLN02790 |
transketolase |
17-308 |
2.85e-11 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 64.27 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 17 EATRNDSNLV------VLTSDSRGSASL-----------GAFAEKFP-ERLVETGIAEQNIVGIAAGLA-HSGkrAFVAS 77
Cdd:PLN02790 344 DATRNLSQKClnalakVLPGLIGGSADLassnmtllkdfGDFQKDTPeERNVRFGVREHGMGAICNGIAlHSS--GLIPY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 78 PACFLsmrsieqvkVDVAYSDTNVKLIGISG-GVSY---------GALGMSHHSLQDIAVTRAIPNLEVILPADRLETEA 147
Cdd:PLN02790 422 CATFF---------VFTDYMRAAMRLSALSEaGVIYvmthdsiglGEDGPTHQPIEHLASLRAMPNILMLRPADGNETAG 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 148 VFDY-LLQSNRPAYVRLGRNAV---EDCYAEKpvfqIGKAGTLRKGN------DVSILATGEMVRVALDAREELKLKGIS 217
Cdd:PLN02790 493 AYKVaVTNRKRPTVLALSRQKVpnlPGTSIEG----VEKGGYVISDNssgnkpDLILIGTGSELEIAAKAAKELRKEGKK 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 218 ARVLNFSTIKPFDQGAV---EAAL-AETKLLISIEEHSIYGGlgaavSEVVSSsptsiRHLILGIpDEPAIAGTSQEIFD 293
Cdd:PLN02790 569 VRVVSMVCWELFEEQSDeykESVLpSSVTARVSVEAGSTFGW-----EKYVGS-----KGKVIGV-DRFGASAPAGILYK 637
|
330
....*....|....*
gi 489821746 294 YYGLSATGIVATVMK 308
Cdd:PLN02790 638 EFGFTVENVVAAAKS 652
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
40-308 |
8.51e-11 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 62.77 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 40 AFAEKFPE-RLVETGIAEQNIVGIAAGLAHSGkrAFVASPACFLSMRSIEQVKVDV-AYSDTNVKLIGISGGVSYGALGM 117
Cdd:PTZ00089 395 DFTKASPEgRYIRFGVREHAMCAIMNGIAAHG--GFIPFGATFLNFYGYALGAVRLaALSHHPVIYVATHDSIGLGEDGP 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 118 SHHSLQDIAVTRAIPNLEVILPADRLETEAVFD-YLLQSNRPAYVRLGRNAVedcyaekpVFQIGKA--GTLRKGNDVS- 193
Cdd:PTZ00089 473 THQPVETLALLRATPNLLVIRPADGTETSGAYAlALANAKTPTILCLSRQNT--------PPLPGSSieGVLKGAYIVVd 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 194 --------ILATGEMVRVALDAREELKlKGISARVLNFSTIKPFDQGAVE---AALAETKLL-ISIEEHSIYGglgaavS 261
Cdd:PTZ00089 545 ftnspqliLVASGSEVSLCVEAAKALS-KELNVRVVSMPCWELFDQQSEEyqqSVLPSGGVPvLSVEAYVSFG------W 617
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489821746 262 EVVSssptsirHLILGIPDEPAiAGTSQEIFDYYGLSATGIVATVMK 308
Cdd:PTZ00089 618 EKYS-------HVHVGISGFGA-SAPANALYKHFGFTVENVVEKARA 656
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
10-260 |
3.56e-10 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 60.14 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 10 MCEVLMKEATR--------NDSNLVVLTSD---SRGSASLG-AFAEKFPE-RLVETGIAEQNIVGIAAGLAHSGKRAFVA 76
Cdd:CHL00144 1 MSEVFLFEALReaideemaRDPRVFVIGEDvghYGGSYKVTkGLHEKYGDlRVLDTPIAENSFTGMAIGAAMTGLRPIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 77 SPACFLSMRSIEQVKVDV----AYSDTNVKL-IGISGGVSYGALGMSHHSLQDIAVTRAIPNLEVILPADRLETEAVFDY 151
Cdd:CHL00144 81 GMNMGFLLLAFNQISNNAgmlhYTSGGNFTIpIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVACSTPYNAKGLLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 152 LLQSNRPA----YVRLgRNAVEDCYAEKPVFQIGKAGTLRKGNDVSILATGEMVRVALDAREELKLKGISARVLNFSTIK 227
Cdd:CHL00144 161 AIRSNNPViffeHVLL-YNLKEEIPDNEYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLK 239
|
250 260 270
....*....|....*....|....*....|...
gi 489821746 228 PFDQGAVEAALAETKLLISIEEHSIYGGLGAAV 260
Cdd:CHL00144 240 PLDLGTISKSVKKTHKVLIVEECMKTGGIGAEL 272
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
35-163 |
4.62e-06 |
|
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: 45.80 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 35 SASLGAFAEKFPERLVETGIAEQNIVGIAAGLAHSGKRAFVASPACFLSMRSIEQVkVDVAysDTNVKLIGISGGVSYGA 114
Cdd:cd06586 23 ISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLLNAINGL-ADAA--AEHLPVVFLIGARGISA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489821746 115 LGMS-HHSLQDIAVTRAIPNLEVILPADRLETEAVFDYLL---QSNRPAYVRL 163
Cdd:cd06586 100 QAKQtFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRtayASQGPVVVRL 152
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
15-141 |
2.36e-05 |
|
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919 [Multi-domain] Cd Length: 167 Bit Score: 44.01 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489821746 15 MKEATRNDSNLVVLTSD--SRGsaslGAF------AEKF-PERLVETGIAEQNIVGIAAGLAHSGKR----------AFV 75
Cdd:cd07036 7 LDEEMERDPRVVVLGEDvgDYG----GVFkvtkglLDKFgPDRVIDTPIAEAGIVGLAVGAAMNGLRpiveimfadfALP 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489821746 76 A-----SPACFLSMRSIEQVKVDVaysdtnVKLIGISGGVSYGAlgmsHHSlQDI-AVTRAIPNLEVILPAD 141
Cdd:cd07036 83 AfdqivNEAAKLRYMSGGQFKVPI------VIRGPNGGGIGGGA----QHS-QSLeAWFAHIPGLKVVAPST 143
|
|
| porA |
PRK09622 |
2-oxoacid:ferredoxin oxidoreductase subunit alpha; |
191-266 |
2.21e-04 |
|
2-oxoacid:ferredoxin oxidoreductase subunit alpha;
Pssm-ID: 181999 [Multi-domain] Cd Length: 407 Bit Score: 42.45 E-value: 2.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489821746 191 DVSILATGEMVRVALDAREELKLKGISARVLNFSTIKPFDQGAVEAALAETKLLISIEEHSIYGGLGAAVSEVVSS 266
Cdd:PRK09622 269 EVAIVALGTTYESAIVAAKEMRKEGIKAGVATIRVLRPFPYERLGQALKNLKALAILDRSSPAGAMGALFNEVTSA 344
|
|
| |
