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Conserved domains on  [gi|695765934|ref|WP_032688965|]
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MULTISPECIES: transketolase [Raoultella]

Protein Classification

transketolase( domain architecture ID 10008162)

transketolase with the TPP di-phosphate residue-binding domain but lacking the TPP pyrimidine-binding domain and the C-terminal domain; transketolase catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
7-276 4.01e-147

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


:

Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 412.93  E-value: 4.01e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   7 DVQALERQARAVRRHIIRL--NANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLA 84
Cdd:COG3959    4 DIKELEEKARQIRRDILRMiyAAGS---GHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  85 EAGFFPVDWLSTYQHANSHLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAA 164
Cdd:COG3959   81 EKGYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKLDGKDYRVYVLLGDGELQEGQVWEAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 165 LAAAHYGLDNLIIINDKNNLQLAGPTREIMNTDPLAEKWKAFGMTVTECQGNNMASVVATLEGLK-QEGKPNVIIANTTK 243
Cdd:COG3959  161 MAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKaVKGKPTVIIAHTVK 240

                        250       260       270
                 ....*....|....*....|....*....|...
gi 695765934 244 GAGISFIQGRPEWHHRVPKGEEIALALEELKDE 276
Cdd:COG3959  241 GKGVSFMENRPKWHGKAPNDEELEQALAELEAE 273
 
Name Accession Description Interval E-value
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
7-276 4.01e-147

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 412.93  E-value: 4.01e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   7 DVQALERQARAVRRHIIRL--NANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLA 84
Cdd:COG3959    4 DIKELEEKARQIRRDILRMiyAAGS---GHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  85 EAGFFPVDWLSTYQHANSHLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAA 164
Cdd:COG3959   81 EKGYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKLDGKDYRVYVLLGDGELQEGQVWEAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 165 LAAAHYGLDNLIIINDKNNLQLAGPTREIMNTDPLAEKWKAFGMTVTECQGNNMASVVATLEGLK-QEGKPNVIIANTTK 243
Cdd:COG3959  161 MAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKaVKGKPTVIIAHTVK 240

                        250       260       270
                 ....*....|....*....|....*....|...
gi 695765934 244 GAGISFIQGRPEWHHRVPKGEEIALALEELKDE 276
Cdd:COG3959  241 GKGVSFMENRPKWHGKAPNDEELEQALAELEAE 273
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 16-270 3.48e-114

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 328.69  E-value: 3.48e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  16 RAVRRHIIRL--NANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLAEAGFFPVDW 93
Cdd:cd02012    1 NRIRRLSIDMvqKAGS---GHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  94 LSTYQHANSHLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAALAAAHYGLD 173
Cdd:cd02012   78 LKTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 174 NLIIINDKNNLQLAGPTREIMNTDPLAEKWKAFGMTVTECQGNNMASVVATLEGLKQ-EGKPNVIIANTTKGAGISFIQG 252
Cdd:cd02012  158 NLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKsKGKPTLIIAKTIKGKGVPFMEN 237

                        250
                 ....*....|....*...
gi 695765934 253 RPEWHHRVPKGEEIALAL 270
Cdd:cd02012  238 TAKWHGKPLGEEEVELAK 255
PRK05899 PRK05899
transketolase; Reviewed
 7-273 1.87e-68

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 221.93  E-value: 1.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   7 DVQALERQARAVRRHIIR--LNANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLA 84
Cdd:PRK05899   4 DMELLQLLANAIRVLSIDavQKANS---GHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  85 EAGF-FPVDWLSTYQHANSHLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKK-------------NHsarRVFLIT 150
Cdd:PRK05899  81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYlaalfnrpgldivDH---YTYVLC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 151 GDGELAEGSNWEAALAAAHYGLDNLIIINDKNNLQLAGPTREIMNTDpLAEKWKAFGMTVTECQGNNMASVVATLEGLKQ 230
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 695765934 231 EGKPNVIIANTTKGAGISFIQGRPEWHHRVPKGEEIALALEEL 273
Cdd:PRK05899 237 STKPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL 279
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
 32-273 2.20e-36

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 132.13  E-value: 2.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   32 GGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLAEAGF-FPVDWLSTYQHANSHLPGHPVR 110
Cdd:pfam00456  22 SGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSMEDLKSFRQLGSKTPGHPEF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  111 QKTPGIELNTGALGHGLPVAVGLALaAKKNHSAR-----------RVFLITGDGELAEGSNWEAALAAAHYGLDNLIIIN 179
Cdd:pfam00456 102 GHTAGVEVTTGPLGQGIANAVGMAI-AERNLAATynrpgfdivdhYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFY 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  180 DKNNLQLAGPTrEIMNTDPLAEKWKAFGMTVTE-CQGNNMASVVATLEGLKQE-GKPNVIIANTTKGAGISFIQGRPEWH 257
Cdd:pfam00456 181 DDNQISIDGET-KISFTEDTAARFEAYGWHVIEvEDGHDVEAIAAAIEEAKAEkDKPTLIKCRTVIGYGSPNKQGTHDVH 259

                         250
                  ....*....|....*.
gi 695765934  258 HRVPKGEEIALALEEL 273
Cdd:pfam00456 260 GAPLGADEVAALKQKL 275
 
Name Accession Description Interval E-value
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
7-276 4.01e-147

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 412.93  E-value: 4.01e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   7 DVQALERQARAVRRHIIRL--NANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLA 84
Cdd:COG3959    4 DIKELEEKARQIRRDILRMiyAAGS---GHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  85 EAGFFPVDWLSTYQHANSHLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAA 164
Cdd:COG3959   81 EKGYFPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKLDGKDYRVYVLLGDGELQEGQVWEAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 165 LAAAHYGLDNLIIINDKNNLQLAGPTREIMNTDPLAEKWKAFGMTVTECQGNNMASVVATLEGLK-QEGKPNVIIANTTK 243
Cdd:COG3959  161 MAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKaVKGKPTVIIAHTVK 240

                        250       260       270
                 ....*....|....*....|....*....|...
gi 695765934 244 GAGISFIQGRPEWHHRVPKGEEIALALEELKDE 276
Cdd:COG3959  241 GKGVSFMENRPKWHGKAPNDEELEQALAELEAE 273
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
 16-270 3.48e-114

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 328.69  E-value: 3.48e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  16 RAVRRHIIRL--NANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLAEAGFFPVDW 93
Cdd:cd02012    1 NRIRRLSIDMvqKAGS---GHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEED 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  94 LSTYQHANSHLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAALAAAHYGLD 173
Cdd:cd02012   78 LKTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 174 NLIIINDKNNLQLAGPTREIMNTDPLAEKWKAFGMTVTECQGNNMASVVATLEGLKQ-EGKPNVIIANTTKGAGISFIQG 252
Cdd:cd02012  158 NLIAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKsKGKPTLIIAKTIKGKGVPFMEN 237

                        250
                 ....*....|....*...
gi 695765934 253 RPEWHHRVPKGEEIALAL 270
Cdd:cd02012  238 TAKWHGKPLGEEEVELAK 255
PRK05899 PRK05899
transketolase; Reviewed
 7-273 1.87e-68

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 221.93  E-value: 1.87e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   7 DVQALERQARAVRRHIIR--LNANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLA 84
Cdd:PRK05899   4 DMELLQLLANAIRVLSIDavQKANS---GHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  85 EAGF-FPVDWLSTYQHANSHLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKK-------------NHsarRVFLIT 150
Cdd:PRK05899  81 LAGYdLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYlaalfnrpgldivDH---YTYVLC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 151 GDGELAEGSNWEAALAAAHYGLDNLIIINDKNNLQLAGPTREIMNTDpLAEKWKAFGMTVTECQGNNMASVVATLEGLKQ 230
Cdd:PRK05899 158 GDGDLMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTED-VKKRFEAYGWHVIEVDGHDVEAIDAAIEEAKA 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 695765934 231 EGKPNVIIANTTKGAGISFIQGRPEWHHRVPKGEEIALALEEL 273
Cdd:PRK05899 237 STKPTLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL 279
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
 32-273 2.20e-36

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 132.13  E-value: 2.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   32 GGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLAEAGF-FPVDWLSTYQHANSHLPGHPVR 110
Cdd:pfam00456  22 SGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSMEDLKSFRQLGSKTPGHPEF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  111 QKTPGIELNTGALGHGLPVAVGLALaAKKNHSAR-----------RVFLITGDGELAEGSNWEAALAAAHYGLDNLIIIN 179
Cdd:pfam00456 102 GHTAGVEVTTGPLGQGIANAVGMAI-AERNLAATynrpgfdivdhYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFY 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  180 DKNNLQLAGPTrEIMNTDPLAEKWKAFGMTVTE-CQGNNMASVVATLEGLKQE-GKPNVIIANTTKGAGISFIQGRPEWH 257
Cdd:pfam00456 181 DDNQISIDGET-KISFTEDTAARFEAYGWHVIEvEDGHDVEAIAAAIEEAKAEkDKPTLIKCRTVIGYGSPNKQGTHDVH 259

                         250
                  ....*....|....*.
gi 695765934  258 HRVPKGEEIALALEEL 273
Cdd:pfam00456 260 GAPLGADEVAALKQKL 275
PTZ00089 PTZ00089
transketolase; Provisional
 27-265 1.47e-34

transketolase; Provisional


Pssm-ID: 173383 [Multi-domain]  Cd Length: 661  Bit Score: 131.34  E-value: 1.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  27 ANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLAEAGF-FPVDWLSTYQHANSHLP 105
Cdd:PTZ00089  24 ANS---GHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDLKNFRQLGSRTP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 106 GHPVRQKTPGIELNTGALGHGLPVAVGLALAAkKNHSAR-----------RVFLITGDGELAEGSNWEAALAAAHYGLDN 174
Cdd:PTZ00089 101 GHPERHITPGVEVTTGPLGQGIANAVGLAIAE-KHLAAKfnrpghpifdnYVYVICGDGCLQEGVSQEALSLAGHLGLEK 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 175 LIIINDKNNLQLAGPTrEIMNTDPLAEKWKAFGMTVTE-CQGN-NMASVVATLEGLKQ-EGKPNVIIANTTKGAGiSFIQ 251
Cdd:PTZ00089 180 LIVLYDDNKITIDGNT-DLSFTEDVEKKYEAYGWHVIEvDNGNtDFDGLRKAIEEAKKsKGKPKLIIVKTTIGYG-SSKA 257

                        250
                 ....*....|....
gi 695765934 252 GrPEWHHRVPKGEE 265
Cdd:PTZ00089 258 G-TEKVHGAPLGDE 270
PLN02790 PLN02790
transketolase
 26-274 4.61e-28

transketolase


Pssm-ID: 215424 [Multi-domain]  Cd Length: 654  Bit Score: 112.81  E-value: 4.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  26 NANSpagGHTGADLSQVELLTALYFRILNVAPDRIADEGRDIYIQSKGHAVGCYYCVLAEAGF--FPVDWLSTYQHANSH 103
Cdd:PLN02790  11 KANS---GHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQFRQWGSR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 104 LPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKknHSARR------------VFLITGDGELAEGSNWEAALAAAHYG 171
Cdd:PLN02790  88 TPGHPENFETPGIEVTTGPLGQGIANAVGLALAEK--HLAARfnkpdhkivdhyTYCILGDGCQMEGISNEAASLAGHWG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 172 LDNLIIINDKNNLQLAGPTrEIMNTDPLAEKWKAFGMTVTECQGNN--MASVVATLEGLKQE-GKPNVIIANTTKGAGiS 248
Cdd:PLN02790 166 LGKLIVLYDDNHISIDGDT-EIAFTEDVDKRYEALGWHTIWVKNGNtdYDEIRAAIKEAKAVtDKPTLIKVTTTIGYG-S 243

                        250       260
                 ....*....|....*....|....*..
gi 695765934 249 FIQGRPEWHHRVPKGE-EIALALEELK 274
Cdd:PLN02790 244 PNKANSYSVHGAALGEkEVDATRKNLG 270
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
 27-273 2.21e-25

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: 105.09  E-value: 2.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  27 ANSpagGHTGADLSQVELLTALYFRILNVAPdriAD---EGRDIYIQSKGHAVGCYYCVLAEAGF-FPVDWLSTYQHANS 102
Cdd:COG0021   22 ANS---GHPGLPMGMAPIAYVLWTKFLKHNP---ANpkwPNRDRFVLSAGHGSMLLYSLLHLTGYdLSLDDLKNFRQLGS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 103 HLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKK-------------NHsarRVFLITGDGELAEGSNWEAALAAAH 169
Cdd:COG0021   96 KTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHlaarfnrpghdivDH---YTYVIAGDGDLMEGISHEAASLAGH 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 170 YGLDNLIIINDKNNLQLAGPTREIMNTDpLAEKWKAFGMTVTECQ-GNNMASVVATLEGLKQE-GKPNVIIANTTKGAGI 247
Cdd:COG0021  173 LKLGKLIVLYDDNGISIDGDTDLAFSED-VAKRFEAYGWHVIRVEdGHDLEAIDAAIEAAKAEtDKPTLIICKTIIGYGS 251

                        250       260       270
                 ....*....|....*....|....*....|.
gi 695765934 248 SFIQGRPEWHhrvpkG-----EEIALALEEL 273
Cdd:COG0021  252 PNKQGTAKAH-----GaplgaEEIAATKEAL 277
TPP_E1_EcPDC_like cd02017
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ...
 9-192 1.23e-11

Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.


Pssm-ID: 238975 [Multi-domain]  Cd Length: 386  Bit Score: 64.25  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   9 QALERQARAVRR---HIIRLNANSPA---GGHTGADLSQVELLTALYFRILNVapdRIADEGRD-IYIQskGHAVGCYYC 81
Cdd:cd02017    1 LEIERRIRSLIRwnaMAMVHRANKKDlgiGGHIATFASAATLYEVGFNHFFRA---RGEGGGGDlVYFQ--GHASPGIYA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  82 VLAEAGFFPVDWLSTYQH--ANSHLPGHPVRQKTPGI-ELNTGALGHGLPVAVGLALAAK-------KNHSARRVFLITG 151
Cdd:cd02017   76 RAFLEGRLTEEQLDNFRQevGGGGLSSYPHPWLMPDFwEFPTVSMGLGPIQAIYQARFNRyledrglKDTSDQKVWAFLG 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 695765934 152 DGELAEGSNWEAALAAAHYGLDNLIIINDKNNLQLAGPTRE 192
Cdd:cd02017  156 DGEMDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPVRG 196
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 107-241 5.02e-11

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 59.96  E-value: 5.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 107 HPVRQKTPGIELNTGALGHGLPVAVGLALAAKKnhsaRRVFLITGDGELAEgsNWEAALAAAHYGLD-NLIIIND----- 180
Cdd:cd00568   32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAPD----RPVVCIAGDGGFMM--TGQELATAVRYGLPvIVVVFNNggygt 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765934 181 -----KNNLQLAGPTREIMNTDpLAEKWKAFGMTVTECQGNnmASVVATLEGLKQEGKPNVIIANT 241
Cdd:cd00568  106 irmhqEAFYGGRVSGTDLSNPD-FAALAEAYGAKGVRVEDP--EDLEAALAEALAAGGPALIEVKT 168
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
 32-246 8.31e-10

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 57.17  E-value: 8.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  32 GGHTGADLSQVELLTALYfRILNVAPDRIA-DEGRdiyiQSKGHAVgcyycVLAEAGFFPVdwLSTYqhanSHLPGHPVR 110
Cdd:cd02007    1 GGHLGSNLGVVELTLALH-YVFDSPKDKIIwDVGH----QAYPHKI-----LTGRRDQFHT--LRQY----GGLSGFTKR 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 111 QKTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAALAAAHYGLDNLIIINDKNnlqlagpt 190
Cdd:cd02007   65 SESEYDAFGTGHSSTSISAALGMAVARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLKSNMIVILNDNE-------- 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765934 191 reiMNTDPLAEK----WKAFGMT-VTECQGNNMASVVATLEGLKQEGKPNVIIANTTKGAG 246
Cdd:cd02007  137 ---MSISPNVGTpgnlFEELGFRyIGPVDGHNIEALIKVLKEVKDLKGPVLLHVVTKKGKG 194
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
 112-224 2.63e-09

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 56.74  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 112 KTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAALAAAHYGLDNLIIINDkNNLQLAGPTR 191
Cdd:cd02000   95 KEKNFFGGNGIVGGQVPLAAGAALALKYRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPTS 173

                         90       100       110
                 ....*....|....*....|....*....|...
gi 695765934 192 EIMNTDPLAEKWKAFGMTVTECQGNNMASVVAT 224
Cdd:cd02000  174 RQTAGTSIADRAAAYGIPGIRVDGNDVLAVYEA 206
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 7-262 5.87e-09

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 56.27  E-value: 5.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   7 DVQA-----LERQARAVRRHIIrlNANSPAGGHTGADLSQVELLTALYfrilnvapdRIADEGRDIYIQSKGHAvgCY-Y 80
Cdd:PRK12571  17 DLRAlsdaeLEQLADELRAEVI--SAVSETGGHLGSSLGVVELTVALH---------AVFNTPKDKLVWDVGHQ--CYpH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  81 CVLAEAGffpvDWLSTYQHANShLPGHPVRQKTPGIELNTGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSN 160
Cdd:PRK12571  84 KILTGRR----DRFRTLRQKGG-LSGFTKRSESEYDPFGAAHSSTSISAALGFAKARALGQPDGDVVAVIGDGSLTAGMA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 161 WEAALAAAHYGLDNLIIINDkNNLQLAGPT-------REIMNTDPLAE-----------------------KWKAFGMT- 209
Cdd:PRK12571 159 YEALNNAGAADRRLIVILND-NEMSIAPPVgalaaylSTLRSSDPFARlraiakgveerlpgplrdgarraRELVTGMIg 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765934 210 ------------VTECQGNNMASVVATLEGLKQE-GKPNVIIANTTKGAGISFIQGRPEWHHRVPK 262
Cdd:PRK12571 238 ggtlfeelgftyVGPIDGHDMEALLSVLRAARARaDGPVLVHVVTEKGRGYAPAEADEDKYHAVGK 303
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
 1-262 8.09e-08

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 53.18  E-value: 8.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   1 MNPYNYDVQALERQARAVRRHIIrLNAnSPAGGHTGADLSQVELLTALYFrILNVAPDRIAdegRDIYIQSKGHAVgcyy 80
Cdd:PLN02234  74 MHMKNLSIKELKVLSDELRSDVI-FNV-SKTGGHLGSNLGVVELTVALHY-IFNTPHDKIL---WDVGHQSYPHKI---- 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  81 cVLAEAGffpvdWLSTYQHANShLPGHPVRQKTPGIELNTG----ALGHGLPVAVGLALAAKKNhsarRVFLITGDGELA 156
Cdd:PLN02234 144 -LTGRRG-----KMKTIRQTNG-LSGYTKRRESEHDSFGTGhsstTLSAGLGMAVGRDLKGMNN----SVVSVIGDGAMT 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 157 EGSNWEAALAAAHYGLDNLIIINDKNNLQLA-----GPTREIMNTD-PLAEKWKAFGMT---------------VTECQG 215
Cdd:PLN02234 213 AGQAYEAMNNAGYLHSNMIVILNDNKQVSLPtanldGPTQPVGALScALSRLQSNCGMIretsstlfeelgfhyVGPVDG 292

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 695765934 216 NNMASVVATLEGLKQEGK--PNVIIANTTKGAGISFIQGRPEWHHRVPK 262
Cdd:PLN02234 293 HNIDDLVSILETLKSTKTigPVLIHVVTEKGRGYPYAERADDKYHGVLK 341
AcoA COG1071
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ...
 120-224 8.89e-08

TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440689 [Multi-domain]  Cd Length: 348  Bit Score: 52.45  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 120 TGALGHGLPVAVGLALAAKKNHSARRVFLITGDGELAEGSNWEAALAAAHYGLDNLIIINdkNNlQLA--GPTREIMNTD 197
Cdd:COG1071  126 SGIVGGQLPHAVGAALAAKLRGEDEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCE--NN-GYAisTPVERQTAVE 202

                         90       100
                 ....*....|....*....|....*..
gi 695765934 198 PLAEKWKAFGMTVTECQGNNMASVVAT 224
Cdd:COG1071  203 TIADRAAGYGIPGVRVDGNDVLAVYAA 229
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 5-261 7.77e-07

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 50.00  E-value: 7.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   5 NYDVQALERQARAVRRHIirLNANSPAGGHTGADLSQVELLTALYFrILNVAPDRIAdegRDIYIQSKGHAV--GCYYCV 82
Cdd:PRK12315  14 KLSLDELEQLASEIRTAL--LEKDSAHGGHVGPNLGVVELTIALHY-VFNSPKDKIV---WDVSHQSYPHKMltGRKEAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  83 LAEAGFfpvDWLSTYQHANSHlpghpvrqktpgiELNTGALGH---GLPVAVGLALAAKKNHSARRVFLITGDGELAEGS 159
Cdd:PRK12315  88 LDPDHY---DDVTGYTNPEES-------------EHDFFTVGHtstSIALATGLAKARDLKGEKGNIIAVIGDGSLSGGL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 160 NWEAALAAAHYGlDNLIII-ND------KNNLQLAGPTREIMNTDPLAEK--WKAFG---MTVTEcqGNNMASVVATLEG 227
Cdd:PRK12315 152 ALEGLNNAAELK-SNLIIIvNDnqmsiaENHGGLYKNLKELRDTNGQSENnlFKAMGldyRYVED--GNDIESLIEAFKE 228

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 695765934 228 LKQEGKPNVIIANTTKGAGISF-IQGRPEWHHRVP 261
Cdd:PRK12315 229 VKDIDHPIVLHIHTLKGKGYQPaEENKEAFHWHMP 263
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 121-241 4.18e-06

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 46.05  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 121 GALGHGLPVAVGLALAakknHSARRVFLITGDGelaeGSNW--EAALAAAHYGLDNL-IIINDKNNLQLAGPTREIMNTD 197
Cdd:cd02002   49 GGLGWGLPAAVGAALA----NPDRKVVAIIGDG----SFMYtiQALWTAARYGLPVTvVILNNRGYGALRSFLKRVGPEG 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695765934 198 PLAEKWKAFG--------MTVTECQGnNMASVVATLEGLKQ-------EGKPNVIIANT 241
Cdd:cd02002  121 PGENAPDGLDlldpgidfAAIAKAFG-VEAERVETPEELDEalrealaEGGPALIEVVV 178
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
 5-190 4.79e-06

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 47.59  E-value: 4.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934   5 NYDVQALERQARAVRRHIIrlNANSPAGGHTGADLSQVELLTALYFrILNVAPDRIAdegRDIYIQSKGHAVgcyycVLA 84
Cdd:PLN02582  45 NLSVKELKQLADELRSDVI--FNVSKTGGHLGSSLGVVELTVALHY-VFNAPQDKIL---WDVGHQSYPHKI-----LTG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  85 EAGFFPvdwlsTYQHANShLPGHPVRQKTPGIELNTG----ALGHGLPVAVGLALAAKKNHsarrVFLITGDGELAEGSN 160
Cdd:PLN02582 114 RRDKMH-----TMRQTNG-LSGFTKRAESEYDCFGTGhsstTISAGLGMAVGRDLKGKKNN----VVAVIGDGAMTAGQA 183

                        170       180       190
                 ....*....|....*....|....*....|
gi 695765934 161 WEAALAAAHYGLDNLIIINDKNNLQLagPT 190
Cdd:PLN02582 184 YEAMNNAGYLDSDMIVILNDNKQVSL--PT 211
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
 130-262 2.60e-05

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 45.07  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 130 AVGLALAAK-KNHSARRVFLITGDGELAEGSNWEAALAAAHYGLDNLIIINDkNNLQLAGPTREIMN------TDPLAEk 202
Cdd:PRK05444 126 ALGMAKARDlKGGEDRKVVAVIGDGALTGGMAFEALNNAGDLKSDLIVILND-NEMSISPNVGALSNylarlrSSTLFE- 203

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765934 203 wkAFGMT----VtecQGNNMASVVATLEGLKQEGKPNVIIANTTKGAGISFIQGRPEWHHRVPK 262
Cdd:PRK05444 204 --ELGFNyigpI---DGHDLDALIETLKNAKDLKGPVLLHVVTKKGKGYAPAEADPIKYHGVGK 262
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 90-153 1.48e-04

Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.


Pssm-ID: 238962 [Multi-domain]  Cd Length: 172  Bit Score: 41.36  E-value: 1.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695765934  90 PVDWLSTYqhanshlpghpVRQKTPGIELNTGALGHgLPVAVGLALAAKKNHSARRVFLITGDG 153
Cdd:cd02004   25 TMDWARYI-----------LRPRKPRHRLDAGTFGT-LGVGLGYAIAAALARPDKRVVLVEGDG 76
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
 121-178 1.81e-04

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 42.63  E-value: 1.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 121 GALGHGLPVAVGLALAakknHSARRVFLITGDGElaegSNW--EAALAAAHYGLDNLIII 178
Cdd:PRK07092 407 GGLGYGLPAAVGVALA----QPGRRVIGLIGDGS----AMYsiQALWSAAQLKLPVTFVI 458
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 121-237 2.50e-04

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439799 [Multi-domain]  Cd Length: 548  Bit Score: 42.07  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 121 GALGHGLPVAVGLALAakknHSARRVFLITGDG-------ELAegsnweaalAAAHYGLDNLIII-ND------KNNLQL 186
Cdd:COG0028  412 GTMGYGLPAAIGAKLA----RPDRPVVAITGDGgfqmnlqELA---------TAVRYGLPVKVVVlNNgglgmvRQWQEL 478

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934 187 AGPTR----EIMNTD--PLAEkwkAFG---MTVTecqgnNMASVVATLEGLKQEGKPNVI 237
Cdd:COG0028  479 FYGGRysgtDLPNPDfaKLAE---AFGakgERVE-----TPEELEAALEEALASDGPALI 530
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
121-180 2.53e-04

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 40.26  E-value: 2.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695765934  121 GALGHGLPVAVGLALAAKKnhsaRRVFLITGDGELaeGSNWEAALAAAHYGLD-NLIIIND 180
Cdd:pfam02775  28 GTMGYGLPAAIGAKLARPD----RPVVAIAGDGGF--QMNLQELATAVRYNLPiTVVVLNN 82
PRK13012 PRK13012
2-oxoacid dehydrogenase subunit E1; Provisional
 139-191 4.07e-04

2-oxoacid dehydrogenase subunit E1; Provisional


Pssm-ID: 237267 [Multi-domain]  Cd Length: 896  Bit Score: 41.46  E-value: 4.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 695765934 139 KNHSARRVFLITGDGELAEGSNWEAALAAAHYGLDNLI-IINdkNNLQ-LAGPTR 191
Cdd:PRK13012 228 KDTSGRKVWGFFGDGEMDEPESIAALSLAAREGLDNLVfVIN--CNLQrLDGPVR 280
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 121-186 9.76e-04

Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.


Pssm-ID: 238973 [Multi-domain]  Cd Length: 186  Bit Score: 39.02  E-value: 9.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695765934 121 GALGHGLPVAVGLALAAKKnhsaRRVFLITGDG-------ELAegsnweaalAAAHYGLDNLIIINDKNNLQL 186
Cdd:cd02015   50 GTMGFGLPAAIGAKVARPD----KTVICIDGDGsfqmniqELA---------TAAQYNLPVKIVILNNGSLGM 109
PRK08155 PRK08155
acetolactate synthase large subunit;
121-186 1.86e-03

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 39.31  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695765934 121 GALGHGLPVAVGLALAAkknhSARRVFLITGDGELAegSNWEAALAAAHYGLDNLIIINDKNNLQL 186
Cdd:PRK08155 419 GTMGFGLPAAIGAALAN----PERKVLCFSGDGSLM--MNIQEMATAAENQLDVKIILMNNEALGL 478
PRK08327 PRK08327
thiamine pyrophosphate-requiring protein;
73-193 2.38e-03

thiamine pyrophosphate-requiring protein;


Pssm-ID: 236243 [Multi-domain]  Cd Length: 569  Bit Score: 39.21  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695765934  73 GHAVGCYYCVLAEAGFFPvdwlstyQHANSHLPGhpvrqkTPGIELNTGALGHGLPVAVGLALAAKKnhsaRRVFLITGD 152
Cdd:PRK08327 395 GEVADEYDAIVTEYPFVP-------RQARLNKPG------SYFGDGSAGGLGWALGAALGAKLATPD----RLVIATVGD 457

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 695765934 153 GELAEGsNWEAALAAAH-YGLDNLIIINDkNNLQLA--GPTREI 193
Cdd:PRK08327 458 GSFIFG-VPEAAHWVAErYGLPVLVVVFN-NGGWLAvkEAVLEV 499
TPP_PDC_IPDC cd02005
Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of ...
 121-153 3.53e-03

Thiamine pyrophosphate (TPP) family, PDC_IPDC subfamily, TPP-binding module; composed of proteins similar to pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC, a key enzyme in alcoholic fermentation, catalyzes the conversion of pyruvate to acetaldehyde and CO2. It is able to utilize other 2-oxo acids as substrates. In plants and various plant-associated bacteria, IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway, a tryptophan-dependent biosynthetic route to indole-3-acetaldehyde (IAA). IPDC catalyzes the decarboxylation of IPA to IAA. Both PDC and IPDC depend on TPP and Mg2+ as cofactors.


Pssm-ID: 238963 [Multi-domain]  Cd Length: 183  Bit Score: 37.51  E-value: 3.53e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 695765934 121 GALGHGLPVAVGLALAAKKnhsaRRVFLITGDG 153
Cdd:cd02005   50 GSIGYSVPAALGAALAAPD----RRVILLVGDG 78
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 121-178 4.14e-03

Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.


Pssm-ID: 239469 [Multi-domain]  Cd Length: 179  Bit Score: 37.27  E-value: 4.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695765934 121 GALGHGLPVAVGLALAAKknhsaRRVFLITGDGELAEGSNweaALA-AAHYGLDNLIII 178
Cdd:cd03372   42 GSMGLASSIGLGLALAQP-----RKVIVIDGDGSLLMNLG---ALAtIAAEKPKNLIIV 92
PDC1 COG3961
TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate ...
 121-153 5.64e-03

TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase [Carbohydrate transport and metabolism, Coenzyme transport and metabolism, General function prediction only]; TPP-dependent 2-oxoacid decarboxylase, includes indolepyruvate decarboxylase is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 443161 [Multi-domain]  Cd Length: 545  Bit Score: 37.83  E-value: 5.64e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 695765934 121 GALGHGLPVAVGLALAAKKnhsaRRVFLITGDG 153
Cdd:COG3961  408 GSIGYTLPAALGAALAAPD----RRVILLVGDG 436
DXP_synthase_N pfam13292
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ...
 130-180 8.02e-03

1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).


Pssm-ID: 463832 [Multi-domain]  Cd Length: 274  Bit Score: 37.00  E-value: 8.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 695765934  130 AVGLALAAKKNHSARRVFLITGDGELAEGSNWEAALAAAHYGLDNLIIIND 180
Cdd:pfam13292 120 ALGMAVARDLKGEDRKVVAVIGDGALTGGMAFEALNNAGHLKKDLIVILND 170
aceE PRK09405
pyruvate dehydrogenase subunit E1; Reviewed
 139-191 8.18e-03

pyruvate dehydrogenase subunit E1; Reviewed


Pssm-ID: 236500 [Multi-domain]  Cd Length: 891  Bit Score: 37.43  E-value: 8.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 695765934 139 KNHSARRV--FLitGDGELAEGSNWEAALAAAHYGLDNLI-IINdkNNLQ-LAGPTR 191
Cdd:PRK09405 220 KDTSDQKVwaFL--GDGEMDEPESLGAISLAAREKLDNLIfVIN--CNLQrLDGPVR 272
AceE COG2609
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ...
 139-191 8.42e-03

Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]; Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 442021 [Multi-domain]  Cd Length: 891  Bit Score: 37.36  E-value: 8.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695765934 139 KNHSARRV--FLitGDGELAE----GsnweaALA-AAHYGLDNLI-IINdkNNLQ-LAGPTR 191
Cdd:COG2609  221 KDTSDRKVwaFL--GDGEMDEpeslG-----AISlAAREKLDNLIfVIN--CNLQrLDGPVR 273
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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