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Conserved domains on  [gi|489866536|ref|WP_003770120|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Listeria innocua]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10793796)

2-C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-d-erythritol from 2-C-methyl-derythritol 4-phosphate and CTP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-232 9.05e-153

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional


:

Pssm-ID: 184017  Cd Length: 230  Bit Score: 423.51  E-value: 9.05e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   1 MNYELIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMQQLDVAEDRVEVVKG 80
Cdd:PRK13385   1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  81 GSERQYSVAAGLECCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHDVVKETVDRDNLWQVQ 160
Cdd:PRK13385  81 GTERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVDRNELWQGQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489866536 161 TPQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAILGelGGKVND 232
Cdd:PRK13385 161 TPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQ--GDIADD 230
 
Name Accession Description Interval E-value
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-232 9.05e-153

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional


Pssm-ID: 184017  Cd Length: 230  Bit Score: 423.51  E-value: 9.05e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   1 MNYELIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMQQLDVAEDRVEVVKG 80
Cdd:PRK13385   1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  81 GSERQYSVAAGLECCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHDVVKETVDRDNLWQVQ 160
Cdd:PRK13385  81 GTERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVDRNELWQGQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489866536 161 TPQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAILGelGGKVND 232
Cdd:PRK13385 161 TPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQ--GDIADD 230
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-223 1.44e-97

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 283.56  E-value: 1.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   6 IFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMQQLDvAEDRVEVVKGGSERQ 85
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYG-IDKPVRVVAGGATRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  86 YSVAAGLECCGLDS-VVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHD-VVKETVDRDNLWQVQTPQ 163
Cdd:COG1211   80 DSVRNGLEALPDDDdWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDgRVTETVDRSGLWAAQTPQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536 164 AFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:COG1211  160 GFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALL 219
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-219 7.88e-94

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 274.02  E-value: 7.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   5 LIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLmqQLDVAEDRVEVVKGGSER 84
Cdd:cd02516    3 AIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL--AKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  85 QYSVAAGLECCGL--DSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVI-HDVVKETVDRDNLWQVQT 161
Cdd:cd02516   81 QDSVLNGLKALPDadPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDdDGVVVETLDREKLWAAQT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489866536 162 PQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLA 219
Cdd:cd02516  161 PQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 5-223 1.28e-83

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 247.97  E-value: 1.28e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536    5 LIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHvrklMQQLDVAEDRVEVVKGGSER 84
Cdd:TIGR00453   2 AVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEF----FQKYLVARAVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   85 QYSVAAGLECCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHD-VVKETVDRDNLWQVQTPQ 163
Cdd:TIGR00453  78 QDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADgFVVETVDREGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  164 AFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 5-225 1.10e-70

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 215.39  E-value: 1.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536    5 LIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMqqldvAEDRVEVVKGGSER 84
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL-----GDPSIQLVAGGDTR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   85 QYSVAAGLECC-GLDSVVLVHDGARPFVTLDIIDRLLLGVKQNK-AAICAVQVKDTVKRVIHD-VVKETVDRDNLWQVQT 161
Cdd:pfam01128  76 QDSVLNGLKALaGTAKFVLVHDGARPCLPHADLARLLAALETGTqGAILALPVTDTIKRVEADgVVAGTPDRSGLWAAQT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489866536  162 PQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAILGE 225
Cdd:pfam01128 156 PQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
 
Name Accession Description Interval E-value
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-232 9.05e-153

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional


Pssm-ID: 184017  Cd Length: 230  Bit Score: 423.51  E-value: 9.05e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   1 MNYELIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMQQLDVAEDRVEVVKG 80
Cdd:PRK13385   1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  81 GSERQYSVAAGLECCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHDVVKETVDRDNLWQVQ 160
Cdd:PRK13385  81 GTERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVDRNELWQGQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489866536 161 TPQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAILGelGGKVND 232
Cdd:PRK13385 161 TPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQ--GDIADD 230
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-223 1.36e-101

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 293.96  E-value: 1.36e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   1 MNYELIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMQQLDvaeDRVEVVKG 80
Cdd:PRK00155   2 MMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD---PKVTVVAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  81 GSERQYSVAAGLECCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRV-IHDVVKETVDRDNLWQV 159
Cdd:PRK00155  79 GAERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSdDGGGIVDTPDRSGLWAA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489866536 160 QTPQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAIL 222
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-223 1.44e-97

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 283.56  E-value: 1.44e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   6 IFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMQQLDvAEDRVEVVKGGSERQ 85
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYG-IDKPVRVVAGGATRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  86 YSVAAGLECCGLDS-VVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHD-VVKETVDRDNLWQVQTPQ 163
Cdd:COG1211   80 DSVRNGLEALPDDDdWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDgRVTETVDRSGLWAAQTPQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536 164 AFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:COG1211  160 GFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALL 219
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-219 7.88e-94

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 274.02  E-value: 7.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   5 LIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLmqQLDVAEDRVEVVKGGSER 84
Cdd:cd02516    3 AIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL--AKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  85 QYSVAAGLECCGL--DSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVI-HDVVKETVDRDNLWQVQT 161
Cdd:cd02516   81 QDSVLNGLKALPDadPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDdDGVVVETLDREKLWAAQT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489866536 162 PQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLA 219
Cdd:cd02516  161 PQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 5-223 1.28e-83

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 247.97  E-value: 1.28e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536    5 LIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHvrklMQQLDVAEDRVEVVKGGSER 84
Cdd:TIGR00453   2 AVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEF----FQKYLVARAVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   85 QYSVAAGLECCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHD-VVKETVDRDNLWQVQTPQ 163
Cdd:TIGR00453  78 QDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADgFVVETVDREGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  164 AFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 5-225 1.10e-70

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 215.39  E-value: 1.10e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536    5 LIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKHVRKLMqqldvAEDRVEVVKGGSER 84
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL-----GDPSIQLVAGGDTR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   85 QYSVAAGLECC-GLDSVVLVHDGARPFVTLDIIDRLLLGVKQNK-AAICAVQVKDTVKRVIHD-VVKETVDRDNLWQVQT 161
Cdd:pfam01128  76 QDSVLNGLKALaGTAKFVLVHDGARPCLPHADLARLLAALETGTqGAILALPVTDTIKRVEADgVVAGTPDRSGLWAAQT 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489866536  162 PQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAILGE 225
Cdd:pfam01128 156 PQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 6-230 4.53e-54

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase


Pssm-ID: 215387  Cd Length: 252  Bit Score: 174.15  E-value: 4.53e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   6 IFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERkhvrklmqqlDVAEDRVEVVKG----- 80
Cdd:PLN02728  28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYR----------DVFEEAVENIDVplkfa 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  81 --GSERQYSVAAGLECCGLDS-VVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRVIHDV-VKETVDRDNL 156
Cdd:PLN02728  98 lpGKERQDSVFNGLQEVDANSeLVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSfVVKTLDRKRL 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489866536 157 WQVQTPQAFELHILQKAHRLAKKDQFLGTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAILGELGGKV 230
Cdd:PLN02728 178 WEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERSDAE 251
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 5-224 2.55e-49

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 165.41  E-value: 2.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   5 LIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRPFLADNRCSKVIVVCQETERKhvrkLMQQLDVAEDRVEVVKGGSER 84
Cdd:PRK09382   8 LVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIA----YMKKALPEIKFVTLVTGGATR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536  85 QYSVAAGLEccGLDS-VVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKDTVKRvihdvVKETVDRDNLWQVQTPQ 163
Cdd:PRK09382  84 QESVRNALE--ALDSeYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKR-----ANETVDREGLKLIQTPQ 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489866536 164 AFELHILQKAhrLAKKDQFlgTDEASLVERIPYPVAIVQGSYYNIKLTTPEDMPLAKAILG 224
Cdd:PRK09382 157 LSRTKTLKAA--ADGRGDF--TDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLS 213
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
8-132 4.41e-09

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 54.40  E-value: 4.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   8 LAAGQGKRMNAekNKMWLDLVGEPIFIHALRPFLAdNRCSKVIVVCqeteRKHVRKLMQQLdvAEDRVEVV------KG- 80
Cdd:COG2068    9 LAAGASSRMGR--PKLLLPLGGKPLLERAVEAALA-AGLDPVVVVL----GADAEEVAAAL--AGLGVRVVvnpdweEGm 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489866536  81 GSerqySVAAGLECCGLD-SVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICA 132
Cdd:COG2068   80 SS----SLRAGLAALPADaDAVLVLLGDQPLVTAETLRRLLAAFRESPASIVA 128
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-132 6.07e-09

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 53.72  E-value: 6.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   6 IFLAAGQGKRMNAekNKMWLDLVGEPIFIHALRPFLAdNRCSKVIVVCQEtERKHVRKLMQQLDVaedRVEVVKGGSERQ 85
Cdd:cd04182    4 IILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALA-AGLSRVIVVLGA-EADAVRAALAGLPV---VVVINPDWEEGM 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489866536  86 -YSVAAGLECCGLDS---VVLVHDgaRPFVTLDIIDRLLLGVKQNKAAICA 132
Cdd:cd04182   77 sSSLAAGLEALPADAdavLILLAD--QPLVTAETLRALIDAFREDGAGIVA 125
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-137 2.36e-08

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 51.81  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536    6 IFLAAGQGKRMNaeKNKMWLDLVGEPIFIHALRpfLADNRCSKVIVVCQETERKHvrklmqqlDVAEDRVEVVKGGSERQ 85
Cdd:pfam12804   2 VILAGGRSSRMG--GDKALLPLGGKPLLERVLE--RLRPAGDEVVVVANDEEVLA--------ALAGLGVPVVPDPDPGQ 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489866536   86 ---YSVAAGLECCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAICAVQVKD 137
Cdd:pfam12804  70 gplAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDG 124
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-120 4.45e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 46.64  E-value: 4.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   8 LAAGQGKRMNAEKNKMWLDLVGEPIFIH---ALRPFLADNrcskVIVVCqeterKHVRKLMQQLDVAEDRVEVVKggsER 84
Cdd:PRK14356  11 LAAGKGTRMHSDKPKVLQTLLGEPMLRFvyrALRPLFGDN----VWTVV-----GHRADMVRAAFPDEDARFVLQ---EQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489866536  85 QYSVAAGLECC-------GLDSVVLVhDGARPFVTLDIIDRLL 120
Cdd:PRK14356  79 QLGTGHALQCAwpsltaaGLDRVLVV-NGDTPLVTTDTIDDFL 120
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 8-134 5.99e-05

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 42.18  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   8 LAAGQGKRMNAEKNKmwLDLVGEPIFIHALRpfLADNRCSKVIVVCQETERKHVRKlmqQLDVAEDRVEvVKG---Gser 84
Cdd:cd02503    6 LAGGKSRRMGGDKAL--LELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYALL---GVPVIPDEPP-GKGplaG--- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489866536  85 qysVAAGLECCGLDSVVLVH-DGarPFVTLDIIDRLLLGVKQNKAAICAVQ 134
Cdd:cd02503   75 ---ILAALRAAPADWVLVLAcDM--PFLPPELLERLLAAAEEGADAVVPKS 120
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-130 1.47e-03

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 38.65  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   6 IFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALRpfLADNRCSKVIVVCQETERKHVRKLmqqldVAEDRVEVVKggSERQ 85
Cdd:cd02540    2 VILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLD--AARALGPDRIVVVVGHGAEQVKKA-----LANPNVEFVL--QEEQ 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489866536  86 ----YSVAAGLE-CCGLDSVVLVHDGARPFVTLDIIDRLLLGVKQNKAAI 130
Cdd:cd02540   73 lgtgHAVKQALPaLKDFEGDVLVLYGDVPLITPETLQRLLEAHREAGADV 122
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 8-133 2.32e-03

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 37.86  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489866536   8 LAAGQGKRMNAekNKMWLDLVGEPIFIHALRpfLADNRCSKVIVVCqeteRKHVRKLMQQLDVAEDRVEVvKG---Gser 84
Cdd:COG0746   10 LAGGRSRRMGQ--DKALLPLGGRPLLERVLE--RLRPQVDEVVIVA----NRPERYAALGVPVVPDDPPG-AGplaG--- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489866536  85 qysVAAGLECCGLDSVVLVhdgarPFVTLDIIDRLLLGVKQNKAAICAV 133
Cdd:COG0746   78 ---ILAALEAAPAEWVLVLac-dmPFLPPDLVRRLLEALEEGADAVVPR 122
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-38 7.65e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 36.89  E-value: 7.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 489866536   1 MNYELIFLAAGQGKRMNAEKNKMWLDLVGEPIFIHALR 38
Cdd:PRK14359   1 MKLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILK 38
 
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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