|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
1-232 |
4.54e-152 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 421.97 E-value: 4.54e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 1 MNYELVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSQLNVAEHRIEIVKG 80
Cdd:PRK13385 1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 81 GSERQYSVAAGLERCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVVNGVVQETVDRENLWQVQ 160
Cdd:PRK13385 81 GTERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVDRNELWQGQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489820092 161 TPQAFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAILGelGGIAND 232
Cdd:PRK13385 161 TPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQ--GDIADD 230
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
8-223 |
3.13e-99 |
|
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: 287.80 E-value: 3.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 8 LAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSQLNvAEHRIEIVKGGSERQYS 87
Cdd:COG1211 3 PAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYG-IDKPVRVVAGGATRQDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 88 VAAGLERCGTE-RVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVV-NGVVQETVDRENLWQVQTPQAF 165
Cdd:COG1211 82 VRNGLEALPDDdDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDdDGRVTETVDRSGLWAAQTPQGF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489820092 166 ELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:COG1211 162 RLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALL 219
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
5-219 |
9.13e-97 |
|
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: 281.33 E-value: 9.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 5 LVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELmsQLNVAEHRIEIVKGGSER 84
Cdd:cd02516 3 AIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL--AKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 QYSVAAGLE--RCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVVN-GVVQETVDRENLWQVQT 161
Cdd:cd02516 81 QDSVLNGLKalPDADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDdGVVVETLDREKLWAAQT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489820092 162 PQAFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLA 219
Cdd:cd02516 161 PQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
5-223 |
2.51e-87 |
|
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: 257.22 E-value: 2.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 5 LVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERkhvkELMSQLNVAEHRIEIVKGGSER 84
Cdd:TIGR00453 2 AVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDT----EFFQKYLVARAVPKIVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 QYSVAAGLERCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRV-VNGVVQETVDRENLWQVQTPQ 163
Cdd:TIGR00453 78 QDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVeADGFVVETVDREGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 164 AFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
5-225 |
1.23e-75 |
|
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: 227.72 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 5 LVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSqlnvaEHRIEIVKGGSER 84
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLG-----DPSIQLVAGGDTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 QYSVAAGLERC-GTERVVLVHDGARPFITLDIIDRLLIGVEQSK-AAICAVKVKDTVKRV-VNGVVQETVDRENLWQVQT 161
Cdd:pfam01128 76 QDSVLNGLKALaGTAKFVLVHDGARPCLPHADLARLLAALETGTqGAILALPVTDTIKRVeADGVVAGTPDRSGLWAAQT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489820092 162 PQAFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAILGE 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 |
4.54e-152 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 421.97 E-value: 4.54e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 1 MNYELVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSQLNVAEHRIEIVKG 80
Cdd:PRK13385 1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 81 GSERQYSVAAGLERCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVVNGVVQETVDRENLWQVQ 160
Cdd:PRK13385 81 GTERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVDRNELWQGQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489820092 161 TPQAFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAILGelGGIAND 232
Cdd:PRK13385 161 TPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQ--GDIADD 230
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-223 |
1.91e-101 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 293.58 E-value: 1.91e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 1 MNYELVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSQlnvAEHRIEIVKG 80
Cdd:PRK00155 2 MMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLA---KDPKVTVVAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 81 GSERQYSVAAGLERCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVV-NGVVQETVDRENLWQV 159
Cdd:PRK00155 79 GAERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDdGGGIVDTPDRSGLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489820092 160 QTPQAFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAIL 222
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
8-223 |
3.13e-99 |
|
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: 287.80 E-value: 3.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 8 LAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSQLNvAEHRIEIVKGGSERQYS 87
Cdd:COG1211 3 PAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYG-IDKPVRVVAGGATRQDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 88 VAAGLERCGTE-RVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVV-NGVVQETVDRENLWQVQTPQAF 165
Cdd:COG1211 82 VRNGLEALPDDdDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDdDGRVTETVDRSGLWAAQTPQGF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489820092 166 ELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:COG1211 162 RLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALL 219
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
5-219 |
9.13e-97 |
|
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: 281.33 E-value: 9.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 5 LVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELmsQLNVAEHRIEIVKGGSER 84
Cdd:cd02516 3 AIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL--AKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 QYSVAAGLE--RCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVVN-GVVQETVDRENLWQVQT 161
Cdd:cd02516 81 QDSVLNGLKalPDADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDdGVVVETLDREKLWAAQT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489820092 162 PQAFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLA 219
Cdd:cd02516 161 PQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
5-223 |
2.51e-87 |
|
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: 257.22 E-value: 2.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 5 LVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERkhvkELMSQLNVAEHRIEIVKGGSER 84
Cdd:TIGR00453 2 AVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDT----EFFQKYLVARAVPKIVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 QYSVAAGLERCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRV-VNGVVQETVDRENLWQVQTPQ 163
Cdd:TIGR00453 78 QDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVeADGFVVETVDREGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 164 AFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAIL 223
Cdd:TIGR00453 158 AFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
5-225 |
1.23e-75 |
|
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: 227.72 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 5 LVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSqlnvaEHRIEIVKGGSER 84
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLG-----DPSIQLVAGGDTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 QYSVAAGLERC-GTERVVLVHDGARPFITLDIIDRLLIGVEQSK-AAICAVKVKDTVKRV-VNGVVQETVDRENLWQVQT 161
Cdd:pfam01128 76 QDSVLNGLKALaGTAKFVLVHDGARPCLPHADLARLLAALETGTqGAILALPVTDTIKRVeADGVVAGTPDRSGLWAAQT 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489820092 162 PQAFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAILGE 225
Cdd:pfam01128 156 PQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
5-224 |
9.62e-53 |
|
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: 174.27 E-value: 9.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 5 LVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERkhvkELMSQLNVAEHRIEIVKGGSER 84
Cdd:PRK09382 8 LVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDI----AYMKKALPEIKFVTLVTGGATR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 QYSVAAGLERCGTERVvLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRvvngvVQETVDRENLWQVQTPQA 164
Cdd:PRK09382 84 QESVRNALEALDSEYV-LIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKR-----ANETVDREGLKLIQTPQL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 165 FELPILRKAhqLARKEQFlgTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAILG 224
Cdd:PRK09382 158 SRTKTLKAA--ADGRGDF--TDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLS 213
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
6-225 |
1.56e-49 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 162.21 E-value: 1.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 6 VFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLADNRCSKVIVVCQEEERKHVKELMSQLNVaehRIEIVKGGSERQ 85
Cdd:PLN02728 28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENIDV---PLKFALPGKERQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 86 YSVAAGLERC-GTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKDTVKRVVNGV-VQETVDRENLWQVQTPQ 163
Cdd:PLN02728 105 DSVFNGLQEVdANSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSfVVKTLDRKRLWEMQTPQ 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489820092 164 AFELPILRKAHQLARKEQFLGTDEASLVERIPCPVAIVQGSYYNIKLTTPEDMPLAKAILGE 225
Cdd:PLN02728 185 VIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNE 246
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
6-137 |
2.91e-10 |
|
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: 56.82 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 6 VFLAAGQGKRMNaqKNKMWLELVGEPIFIHALRpfLADNRCSKVIVVCQEEERKHVkelmsqlnVAEHRIEIVKGGSERQ 85
Cdd:pfam12804 2 VILAGGRSSRMG--GDKALLPLGGKPLLERVLE--RLRPAGDEVVVVANDEEVLAA--------LAGLGVPVVPDPDPGQ 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489820092 86 ---YSVAAGLERCGTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAICAVKVKD 137
Cdd:pfam12804 70 gplAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDG 124
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
8-132 |
1.33e-09 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 55.94 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 8 LAAGQGKRMNAqkNKMWLELVGEPIFIHALRPFLAdNRCSKVIVVCqeeeRKHVKELMSQLnvAEHRIEIV------KG- 80
Cdd:COG2068 9 LAAGASSRMGR--PKLLLPLGGKPLLERAVEAALA-AGLDPVVVVL----GADAEEVAAAL--AGLGVRVVvnpdweEGm 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489820092 81 GSerqySVAAGLERCGTE-RVVLVHDGARPFITLDIIDRLLIGVEQSKAAICA 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; ... |
8-132 |
1.62e-08 |
|
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: 52.56 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 8 LAAGQGKRMNAqkNKMWLELVGEPIFIHALRPFLAdNRCSKVIVVCQEEERkHVKELMSQLNVaehRIEIVKGGSERQ-Y 86
Cdd:cd04182 6 LAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALA-AGLSRVIVVLGAEAD-AVRAALAGLPV---VVVINPDWEEGMsS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489820092 87 SVAAGLERCGTER---VVLVHDgaRPFITLDIIDRLLIGVEQSKAAICA 132
Cdd:cd04182 79 SLAAGLEALPADAdavLILLAD--QPLVTAETLRALIDAFREDGAGIVA 125
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-120 |
3.85e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 47.03 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 6 VFLAAGQGKRMNAQKNKMWLELVGEPIFIH---ALRPFLADN-------RCSKVIVVCQEEERKHVKElMSQLNVAeHRI 75
Cdd:PRK14356 9 LILAAGKGTRMHSDKPKVLQTLLGEPMLRFvyrALRPLFGDNvwtvvghRADMVRAAFPDEDARFVLQ-EQQLGTG-HAL 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489820092 76 EIVKGGSErqysvAAGLERCgtervvLVHDGARPFITLDIIDRLL 120
Cdd:PRK14356 87 QCAWPSLT-----AAGLDRV------LVVNGDTPLVTTDTIDDFL 120
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
8-133 |
8.20e-06 |
|
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: 44.80 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 8 LAAGQGKRMnaQKNKMWLELVGEPIFIHALRpfLADNRCSKVIVVCQEEERkhvkelmsqlnVAEHRIEIVK-------- 79
Cdd:COG0746 10 LAGGRSRRM--GQDKALLPLGGRPLLERVLE--RLRPQVDEVVIVANRPER-----------YAALGVPVVPddppgagp 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489820092 80 -GGserqysVAAGLERCGTERVVLVhdgarPFITLDIIDRLLIGVEQSKAAICAV 133
Cdd:COG0746 75 lAG------ILAALEAAPAEWVLVLac-dmPFLPPDLVRRLLEALEEGADAVVPR 122
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
8-133 |
7.05e-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: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 8 LAAGQGKRMNAqkNKMWLELVGEPIFIHALRpfLADNRCSKVIVVCQEEERKHVKelmSQLNVAEHRIEIvKG---Gser 84
Cdd:cd02503 6 LAGGKSRRMGG--DKALLELGGKPLLEHVLE--RLKPLVDEVVISANRDQERYAL---LGVPVIPDEPPG-KGplaG--- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489820092 85 qysVAAGLERCGTERVVLVH-DGarPFITLDIIDRLLIGVEQSKAAICAV 133
Cdd:cd02503 75 ---ILAALRAAPADWVLVLAcDM--PFLPPELLERLLAAAEEGADAVVPK 119
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-152 |
1.21e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 42.28 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 1 MNYELVFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRPFLA--DNRCskvIVVCQEEERkhVKELMSQL--NVAEHRIE 76
Cdd:PRK14359 1 MKLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAFAisDDVH---VVLHHQKER--IKEAVLEYfpGVIFHTQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 77 IVK----GGSERQYSVAaglercgTERvVLVHDGARPFITLDIIDRLLIGveQSKAAICAVKVKDT--VKRVV--NGVVQ 148
Cdd:PRK14359 76 LENypgtGGALMGIEPK-------HER-VLILNGDMPLVEKDELEKLLEN--DADIVMSVFHLADPkgYGRVVieNGQVK 145
|
....
gi 489820092 149 ETVD 152
Cdd:PRK14359 146 KIVE 149
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-130 |
1.98e-04 |
|
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: 41.35 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489820092 6 VFLAAGQGKRMNAQKNKMWLELVGEPIFIHALRpfLADNRCSKVIVVCQEEERKHVKELmsqlnVAEHRIEIVKggSERQ 85
Cdd:cd02540 2 VILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLD--AARALGPDRIVVVVGHGAEQVKKA-----LANPNVEFVL--QEEQ 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489820092 86 ----YSVAAGLERC-GTERVVLVHDGARPFITLDIIDRLLIGVEQSKAAI 130
Cdd:cd02540 73 lgtgHAVKQALPALkDFEGDVLVLYGDVPLITPETLQRLLEAHREAGADV 122
|
|
| |
