|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
5-306 |
1.50e-122 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 353.24 E-value: 1.50e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 5 TKEMRLVYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFAS 84
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 85 RRVFDQVFLSLGYSQLSATIIGSDAGVSAEMNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLKYIRT 164
Cdd:COG3958 83 GRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 165 IRKAATAVYEGCEDFSKG-FIQLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEElkpLLID---- 239
Cdd:COG3958 163 GRGAVPVVYDEDYEFEIGkARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEE---AILKaark 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491104595 240 -QSIVTIENHNRIGGIGSALCEWLSMEKDTTVSRMGIDERFGQVGQMKYLLEEYGLAVKDIVEHCKSI 306
Cdd:COG3958 240 tGAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKEL 307
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
11-166 |
1.09e-47 |
|
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: 157.22 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 11 VYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFgPFASRRVFDQ 90
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTF-SFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491104595 91 VFLSLGYSQLSATIIGSDAGVSAEMNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLKYIRTIR 166
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
11-301 |
1.20e-29 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 118.26 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 11 VYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYL---HTFgpfaSRRV 87
Cdd:PRK05444 284 VFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVaiySTF----LQRA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 88 FDQVFLSLGYSQLSATIIGSDAGVSAEmNGGTHMPFEELGLLRLIPKATIFEVSDdiqfEAVLKQTLSIdGLKY------ 161
Cdd:PRK05444 360 YDQVIHDVALQNLPVTFAIDRAGLVGA-DGPTHQGAFDLSYLRCIPNMVIMAPSD----ENELRQMLYT-ALAYddgpia 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 162 IRTIRKAATAV-YEGCE--DFSKGFIqLRQGKDIALVASGIMVSRAIEAADYLKelgiEASVIDLFKIKPPPEELKPLLI 238
Cdd:PRK05444 434 IRYPRGNGVGVeLPELEplPIGKGEV-LREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELA 508
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491104595 239 DQS--IVTIENHNRIGGIGSALCEWLSMEK-DTTVSRMGIDERFGQVGQMKYLLEEYGLAVKDIVE 301
Cdd:PRK05444 509 AKHdlVVTVEEGAIMGGFGSAVLEFLADHGlDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIAR 574
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
186-299 |
1.85e-21 |
|
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: 87.65 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 186 LRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEElkplLIDQS------IVTIENHNRIGGIGSALC 259
Cdd:pfam02780 6 LREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKE----TILESvkktgrLVTVEEAVPRGGFGSEVA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 491104595 260 ----EWLSMEKDTTVSRMGIdERFGQVGQMKYLLEEYGLAVKDI 299
Cdd:pfam02780 82 aalaEEAFDGLDAPVLRVGG-PDFPEPGSADELEKLYGLTPEKI 124
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
38-168 |
1.35e-20 |
|
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: 85.62 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 38 STNALASEFgkryINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFASRRvFDQVFLSLGYSQLSAtIIGSDAGVSAEMNG 117
Cdd:smart00861 9 FGEALAELA----IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRA-KDQIRSAGASGNVPV-VFRHDGGGGVGEDG 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491104595 118 GTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLKYIRTIRKA 168
Cdd:smart00861 83 PTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKS 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
5-306 |
1.50e-122 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 353.24 E-value: 1.50e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 5 TKEMRLVYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFAS 84
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGLALAGKIPFVSTFAPFLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 85 RRVFDQVFLSLGYSQLSATIIGSDAGVSAEMNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLKYIRT 164
Cdd:COG3958 83 GRAYEQIRNDIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVYLRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 165 IRKAATAVYEGCEDFSKG-FIQLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEElkpLLID---- 239
Cdd:COG3958 163 GRGAVPVVYDEDYEFEIGkARVLREGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEE---AILKaark 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491104595 240 -QSIVTIENHNRIGGIGSALCEWLSMEKDTTVSRMGIDERFGQVGQMKYLLEEYGLAVKDIVEHCKSI 306
Cdd:COG3958 240 tGAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPDRFGESGSPEELLEKYGLDAEGIVAAAKEL 307
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
11-166 |
1.09e-47 |
|
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: 157.22 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 11 VYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFgPFASRRVFDQ 90
Cdd:cd07033 2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHGLKPFVSTF-SFFLQRAYDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491104595 91 VFLSLGYSQLSATIIGSDAGVSAEMNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLKYIRTIR 166
Cdd:cd07033 81 IRHDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
11-301 |
1.20e-29 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 118.26 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 11 VYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYL---HTFgpfaSRRV 87
Cdd:PRK05444 284 VFGETLCELAEKDPKIVAITAAMPEGTGLVKFSKRFPDRYFDVGIAEQHAVTFAAGLATEGLKPVVaiySTF----LQRA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 88 FDQVFLSLGYSQLSATIIGSDAGVSAEmNGGTHMPFEELGLLRLIPKATIFEVSDdiqfEAVLKQTLSIdGLKY------ 161
Cdd:PRK05444 360 YDQVIHDVALQNLPVTFAIDRAGLVGA-DGPTHQGAFDLSYLRCIPNMVIMAPSD----ENELRQMLYT-ALAYddgpia 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 162 IRTIRKAATAV-YEGCE--DFSKGFIqLRQGKDIALVASGIMVSRAIEAADYLKelgiEASVIDLFKIKPPPEELKPLLI 238
Cdd:PRK05444 434 IRYPRGNGVGVeLPELEplPIGKGEV-LREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELA 508
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491104595 239 DQS--IVTIENHNRIGGIGSALCEWLSMEK-DTTVSRMGIDERFGQVGQMKYLLEEYGLAVKDIVE 301
Cdd:PRK05444 509 AKHdlVVTVEEGAIMGGFGSAVLEFLADHGlDVPVLNLGLPDEFIDHGSREELLAELGLDAEGIAR 574
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
40-301 |
1.90e-29 |
|
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: 117.81 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 40 NALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYL---HTFgpfaSRRVFDQVFLSLGYSQLSAT-------IIGSDa 109
Cdd:COG1154 351 DKFAERFPDRFFDVGIAEQHAVTFAAGLATEGLKPVVaiySTF----LQRAYDQVIHDVALQNLPVTfaidragLVGAD- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 110 gvsaemnGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDG---LKYIR------TIRKAATAVYEGcedfs 180
Cdd:COG1154 426 -------GPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGptaIRYPRgngpgvELPAELEPLPIG----- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 181 KGFIqLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEElkpLLIDQS-----IVTIENHNRIGGIG 255
Cdd:COG1154 494 KGEV-LREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEE---LILELArehdlVVTVEEGVLAGGFG 569
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 491104595 256 SALCEWLSMEK-DTTVSRMGIDERFGQVGQMKYLLEEYGLAVKDIVE 301
Cdd:COG1154 570 SAVLEFLADAGlDVPVLRLGLPDRFIEHGSRAELLAELGLDAEGIAR 616
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
6-301 |
9.63e-27 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 109.84 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 6 KEMRLVYR----DFLLQANQENKQITVLEADLSSSMSTNALAS------EFGKRYINLGIMEAEMVGLAAGFAIKG-YKP 74
Cdd:PRK05899 277 KELGWDYRkasgKALNALAKALPELVGGSADLAGSNNTKIKGSkdfapeDYSGRYIHYGVREFAMAAIANGLALHGgFIP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 75 YLHTFGPFASRrVFDQVFLSlGYSQLSATIIGSDAGVSAEMNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTL 154
Cdd:PRK05899 357 FGGTFLVFSDY-ARNAIRLA-ALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYAL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 155 -SIDGLKYIRTIRKAATAVYEGC--EDFSKGFIQLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKP--- 228
Cdd:PRK05899 435 eRKDGPSALVLTRQNLPVLERTAqeEGVAKGGYVLRDDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELfde 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491104595 229 PPEELKpllidQSIVTIENHNRIGGIGSALCEWLSMEKDTTVsRMGIDeRFGQVGQMKYLLEEYGLAVKDIVE 301
Cdd:PRK05899 515 QDAAYK-----ESVLPAAVTARVAVEAGVADGWYKYVGLDGK-VLGID-TFGASAPADELFKEFGFTVENIVA 580
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
11-305 |
1.70e-26 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 109.43 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 11 VYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFAsRRVFDQ 90
Cdd:PRK12571 324 VFGEELTKEAAEDSDIVAITAAMPLGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYSTFL-QRGYDQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 91 VFLSLGYSQLSATIIGSDAGVSAEmNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSID----GLKYIR--T 164
Cdd:PRK12571 403 LLHDVALQNLPVRFVLDRAGLVGA-DGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDdgpiAVRFPRgeG 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 165 IRKAATAVYEGCEdFSKGFIqLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEELKPLLIDQSI-V 243
Cdd:PRK12571 482 VGVEIPAEGTILG-IGKGRV-PREGPDVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIvV 559
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491104595 244 TIENHNRIGGIGSALCEWLS----MEKDTTVSRMGIDERFGQVGQMKYLLEEYGLAVKDIVEHCKS 305
Cdd:PRK12571 560 IVEEQGAMGGFGAHVLHHLAdtglLDGGLKLRTLGLPDRFIDHASREEMYAEAGLTAPDIAAAVTG 625
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
186-299 |
1.85e-21 |
|
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: 87.65 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 186 LRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEElkplLIDQS------IVTIENHNRIGGIGSALC 259
Cdd:pfam02780 6 LREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKE----TILESvkktgrLVTVEEAVPRGGFGSEVA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 491104595 260 ----EWLSMEKDTTVSRMGIdERFGQVGQMKYLLEEYGLAVKDI 299
Cdd:pfam02780 82 aalaEEAFDGLDAPVLRVGG-PDFPEPGSADELEKLYGLTPEKI 124
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
11-308 |
8.36e-21 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 92.38 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 11 VYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFAsRRVFDQ 90
Cdd:PRK12315 283 VTLDYLLKKIKEGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGIAANGARPVIFVNSTFL-QRAYDQ 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 91 VFLSLGYSQLSATIIGSDAGVSAemNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKqtLSIDGLKYIRTIRKAAT 170
Cdd:PRK12315 362 LSHDLAINNNPAVMIVFGGSISG--NDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLE--WALTQHEHPVAIRVPEH 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 171 AVYEGCE---DFSKGFIQ-LRQGKDIALVASGIMVSRAIEAADYLKE-LGIEASVIDLFKIKPPPEE-LKPLLIDQSIV- 243
Cdd:PRK12315 438 GVESGPTvdtDYSTLKYEvTKAGEKVAILALGDFYELGEKVAKKLKEeLGIDATLINPKFITGLDEElLEKLKEDHELVv 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491104595 244 TIENHNRIGGIGSALCEWLSmEKDTTVSRMGIDERFGQVGQMKYLLEEYGLAVKDIVEHCKSIYK 308
Cdd:PRK12315 518 TLEDGILDGGFGEKIARYYG-NSDMKVLNYGAKKEFNDRVPVEELYKRNHLTPEQIVEDILSVLK 581
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
38-168 |
1.35e-20 |
|
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: 85.62 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 38 STNALASEFgkryINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFASRRvFDQVFLSLGYSQLSAtIIGSDAGVSAEMNG 117
Cdd:smart00861 9 FGEALAELA----IDTGIAEQAMVGFAAGLALHGLRPVVEIFFTFFDRA-KDQIRSAGASGNVPV-VFRHDGGGGVGEDG 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491104595 118 GTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLKYIRTIRKA 168
Cdd:smart00861 83 PTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKS 133
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
8-166 |
4.84e-19 |
|
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: 82.60 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 8 MRLVYRDFLLQANQENKQITVLEADLSSSMSTNALASEF---GKRYINLGIMEAEMVGLAAGFAIKG--YKPYLHTFGPF 82
Cdd:pfam02779 5 TRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHpqgAGRVIDTGIAEQAMVGFANGMALHGplLPPVEATFSDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 83 ASRrVFDQVFLSLGYSQLSATIIGSDAGVSAEMNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLK-- 160
Cdd:pfam02779 85 LNR-ADDAIRHGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGRKpv 163
|
....*.
gi 491104595 161 YIRTIR 166
Cdd:pfam02779 164 VLRLPR 169
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
16-265 |
6.48e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 75.13 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 16 LLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFAsRRVFDQVFLSL 95
Cdd:PLN02234 367 LIAEAEADKDIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCTIYSSFM-QRAYDQVVHDV 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 96 GYSQLSATIIGSDAGVSAEmNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDG----LKYIR--TIRKAA 169
Cdd:PLN02234 446 DLQKLPVRFAIDRAGLMGA-DGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAAIDDrpscFRYHRgnGIGVSL 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 170 TAVYEGCE-DFSKGFIqLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEEL-KPLLIDQSIVTIEN 247
Cdd:PLN02234 525 PPGNKGVPlQIGRGRI-LRDGERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALiRSLAKSHEVLITVE 603
|
250
....*....|....*...
gi 491104595 248 HNRIGGIGSALCEWLSME 265
Cdd:PLN02234 604 EGSIGGFGSHVVQFLALD 621
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
4-265 |
1.36e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 71.08 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 4 STKEMRLVYRDFLLQANQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFA 83
Cdd:PLN02582 354 KTQSYTTYFAEALIAEAEVDKDVVAIHAAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 84 SrRVFDQVFLSLGYSQLSATIIGSDAGVSAEmNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDG----L 159
Cdd:PLN02582 434 Q-RGYDQVVHDVDLQKLPVRFAMDRAGLVGA-DGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDrpscF 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 160 KYIR--TIRKAATAVYEGCE-DFSKGFIqLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEELKPL 236
Cdd:PLN02582 512 RYPRgnGIGVQLPPNNKGIPiEVGKGRI-LLEGERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRS 590
|
250 260 270
....*....|....*....|....*....|.
gi 491104595 237 LID--QSIVTIEnHNRIGGIGSALCEWLSME 265
Cdd:PLN02582 591 LAKshEVLITVE-EGSIGGFGSHVAQFMALD 620
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
186-259 |
3.84e-10 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 60.00 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 186 LRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEElkplLIDQSI------VTIENHNRIGGIGSALC 259
Cdd:PTZ00182 230 VREGKDVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRE----TIVKSVkktgrcVIVHEAPPTCGIGAEIA 305
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
187-228 |
8.77e-10 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 59.16 E-value: 8.77e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 491104595 187 RQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKP 228
Cdd:PRK11892 338 REGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRP 379
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
9-265 |
1.85e-09 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 58.57 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 9 RLVYRDFLLQA----NQENKQITVLEADLSSSMSTNALASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFAs 84
Cdd:PLN02225 380 RRTYSDCFVEAlvmeAEKDRDIVVVHAGMEMDASLITFQERFPDRFFNVGMAEQHAVTFSAGLSSGGLKPFCIIPSAFL- 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 85 RRVFDQVFLSLGYSQLSATIIGSDAGVSaemngGTHMPFEELGLlrlipkatifevsdDIQFEAVLKQTLSIDGLKYIRT 164
Cdd:PLN02225 459 QRAYDQVVHDVDRQRKAVRFVITSAGLV-----GSDGPVQCGAF--------------DIAFMSSLPNMIAMAPADEDEL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 165 IRKAATAVYEG----CEDFSKGFIQLR-------------------QGKDIALVASGIMVSRAIEAADYLKELGIEASVI 221
Cdd:PLN02225 520 VNMVATAAYVTdrpvCFRFPRGSIVNMnylvptglpieigrgrvlvEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVA 599
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 491104595 222 DLFKIKPPPEEL-KPLLIDQSIVTIENHNRIGGIGSALCEWLSME 265
Cdd:PLN02225 600 DARFCKPLDIKLvRDLCQNHKFLITVEEGCVGGFGSHVAQFIALD 644
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
39-258 |
1.12e-08 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 55.50 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 39 TNALASEFG-KRYINLGIMEAEMVGLAAGFAIKGYKPYLH--TFGpFAsRRVFDQV--------FLSLGysQLSATII-- 105
Cdd:PRK09212 41 TQGLLEQFGpKRVIDTPITEHGFAGLAVGAAFAGLRPIVEfmTFN-FS-MQAIDQIvnsaaktnYMSGG--QLKCPIVfr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 106 ---GSDAGVSAEMNGG-----THMP--------FEE--LGLLRLI---PKATIF---EVSDDIQFEaVLKQTLSIDglky 161
Cdd:PRK09212 117 gpnGAAARVAAQHSQCyaawySHIPglkvvapyFAAdcKGLLKTAirdPNPVIFlenEILYGHSHE-VPEEEESIP---- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 162 irtIRKAATavyegcedfskgfiqLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPPPEE--LKPLLID 239
Cdd:PRK09212 192 ---IGKAAI---------------LREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTEtiIESVKKT 253
|
250
....*....|....*....
gi 491104595 240 QSIVTIENHNRIGGIGSAL 258
Cdd:PRK09212 254 NRLVVVEEGWPFAGVGAEI 272
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
39-259 |
4.34e-07 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 50.59 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 39 TNALASEFG-KRYINLGIMEAEMVGLAAGFAIKGYKPYLHTFGPFASRRVFDQV--------FLSLGysQLSATII---- 105
Cdd:PLN02683 64 TKGLLQKYGpDRVLDTPITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIinsaaktnYMSAG--QISVPIVfrgp 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 106 -GSDAGVSAEMNGG-----THMPfeelGLLRLIP----------KATIFEVSDDIQFE---------AVLKQTLSIDglk 160
Cdd:PLN02683 142 nGAAAGVGAQHSQCfaawySSVP----GLKVLAPyssedargllKAAIRDPDPVVFLEnellygesfPVSAEVLDSS--- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 161 YIRTIRKAATavyegcedfskgfiqLRQGKDIALVASGIMVSRAIEAADYLKELGIEASVIDLFKIKPppeeLKPLLIDQ 240
Cdd:PLN02683 215 FVLPIGKAKI---------------EREGKDVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRP----LDRDTINA 275
|
250 260
....*....|....*....|....*
gi 491104595 241 S------IVTIENHNRIGGIGSALC 259
Cdd:PLN02683 276 SvrktnrLVTVEEGWPQHGVGAEIC 300
|
|
| PLN02790 |
PLN02790 |
transketolase |
31-306 |
7.38e-07 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 50.40 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 31 ADLSSS------MSTNALASEFGKRYINLGIMEAEMVGLAAGFAI--KGYKPYLHTFGPFAsrrvfDQVFLSLGYSQLSa 102
Cdd:PLN02790 369 ADLASSnmtllkDFGDFQKDTPEERNVRFGVREHGMGAICNGIALhsSGLIPYCATFFVFT-----DYMRAAMRLSALS- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 103 tiigsDAGVSAEM---------NGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLK----------------QTLSID 157
Cdd:PLN02790 443 -----EAGVIYVMthdsiglgeDGPTHQPIEHLASLRAMPNILMLRPADGNETAGAYKvavtnrkrptvlalsrQKVPNL 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 158 GLKYIRTIRKAATAVYEGCEDfskgfiqlrQGKDIALVASGIMVSRAIEAADYLKELGIEASVI-----DLFKIKppPEE 232
Cdd:PLN02790 518 PGTSIEGVEKGGYVISDNSSG---------NKPDLILIGTGSELEIAAKAAKELRKEGKKVRVVsmvcwELFEEQ--SDE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 233 LKPLLIDQSI---VTIEN------HNRIGGIGSAlcewlsmekdttvsrMGIDeRFGQVGQMKYLLEEYGLAVKDIVEHC 303
Cdd:PLN02790 587 YKESVLPSSVtarVSVEAgstfgwEKYVGSKGKV---------------IGVD-RFGASAPAGILYKEFGFTVENVVAAA 650
|
...
gi 491104595 304 KSI 306
Cdd:PLN02790 651 KSL 653
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
31-301 |
1.02e-06 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 50.06 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 31 ADLSSSMSTnALASE-------FGKRYINLGIMEAEMVGLAAG-FAIKGYKPYLHTFGPFASRrVFDQVFLSlGYSQLSA 102
Cdd:PTZ00089 380 ADLTPSNLT-RPKEAndftkasPEGRYIRFGVREHAMCAIMNGiAAHGGFIPFGATFLNFYGY-ALGAVRLA-ALSHHPV 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 103 TIIGSDAGVSAEMNGGTHMPFEELGLLRLIPKATIFEVSDDIQFEAVLKQTLSIDGLKYIRTIRKAATAVYEGC--EDFS 180
Cdd:PTZ00089 457 IYVATHDSIGLGEDGPTHQPVETLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSsiEGVL 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 181 KGFIQLRQ---GKDIALVASGIMVSRAIEAADYLKElgiEASV-------IDLFKIKppPEELKpllidQSIVTIENHNR 250
Cdd:PTZ00089 537 KGAYIVVDftnSPQLILVASGSEVSLCVEAAKALSK---ELNVrvvsmpcWELFDQQ--SEEYQ-----QSVLPSGGVPV 606
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 251 IggigsalcewlSMEKDTTvsrMGID---------ERFGQVGQMKYLLEEYGLAVKDIVE 301
Cdd:PTZ00089 607 L-----------SVEAYVS---FGWEkyshvhvgiSGFGASAPANALYKHFGFTVENVVE 652
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
42-143 |
3.72e-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: 40.41 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491104595 42 LASEFGKRYINLGIMEAEMVGLAAGFAIKGYKPY-LHTFGPFASrRVFDQVfLSLGYSQLSATIIGSDAGVSAeMNGGTH 120
Cdd:cd06586 29 ALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVvIVTSGTGLL-NAINGL-ADAAAEHLPVVFLIGARGISA-QAKQTF 105
|
90 100
....*....|....*....|...
gi 491104595 121 MPFEELGLLRLIPKATIFEVSDD 143
Cdd:cd06586 106 QSMFDLGMYRSIPEANISSPSPA 128
|
|
| |
