|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-232 |
3.65e-121 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 343.65 E-value: 3.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 8 VCAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGD-ARFAQLPLANHPQITVVDGGAERA 86
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 87 DSVLAGIQAAGNAPWVLVHDAARPCLHQDDLARLLALSETSkVGGILAAPVRDTMKRAEPGkQAIAHTVDRVDLWHALTP 166
Cdd:PRK00155 84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDG-GGIVDTPDRSGLWAAQTP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549105 167 QFFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYLTRSTH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
10-229 |
1.04e-106 |
|
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: 306.68 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 10 AVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGDA-RFAQLPLanHPQITVVDGGAERADS 88
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTpEFRQLLG--DPSIQLVAGGDTRQDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 89 VLAGIQA-AGNAPWVLVHDAARPCLHQDDLARLLALSETSKVGGILAAPVRDTMKRAEpGKQAIAHTVDRVDLWHALTPQ 167
Cdd:pfam01128 79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658549105 168 FFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
9-227 |
1.12e-98 |
|
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: 286.49 E-value: 1.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 9 CAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGDARFAQLPLANHPQITVVDGGAERADS 88
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 89 VLAGIQAAGNAPWVLVHDAARPCLHQDDLARLLALSETSKvGGILAAPVRDTMKRAEPGKQaIAHTVDRVDLWHALTPQF 168
Cdd:TIGR00453 81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAG-AAILALPVADTLKRVEADGF-VVETVDREGLWAAQTPQA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658549105 169 FPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
11-232 |
2.50e-98 |
|
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: 285.49 E-value: 2.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 11 VVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGD-ARFAQL--PLANHPQITVVDGGAERAD 87
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 88 SVLAGIQAAGNAP-WVLVHDAARPCLHQDDLARLLALSETSkVGGILAAPVRDTMKRAEPGkQAIAHTVDRVDLWHALTP 166
Cdd:COG1211 81 SVRNGLEALPDDDdWVLVHDAARPLVSPELIDRVIEAAREY-GAAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549105 167 QFFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYLTRSTH 232
Cdd:COG1211 159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-223 |
1.06e-85 |
|
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: 253.60 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 8 VCAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGDARFAQ--LPLANHPQITVVDGGAER 85
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 86 ADSVLAGIQAAGNAP--WVLVHDAARPCLHQDDLARLLALSEtSKVGGILAAPVRDTMKRAEpGKQAIAHTVDRVDLWHA 163
Cdd:cd02516 81 QDSVLNGLKALPDADpdIVLIHDAARPFVSPELIDRLIDALK-EYGAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 164 LTPQFFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLA 223
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-232 |
3.65e-121 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 343.65 E-value: 3.65e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 8 VCAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGD-ARFAQLPLANHPQITVVDGGAERA 86
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 87 DSVLAGIQAAGNAPWVLVHDAARPCLHQDDLARLLALSETSkVGGILAAPVRDTMKRAEPGkQAIAHTVDRVDLWHALTP 166
Cdd:PRK00155 84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDG-GGIVDTPDRSGLWAAQTP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549105 167 QFFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYLTRSTH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
10-229 |
1.04e-106 |
|
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: 306.68 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 10 AVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGDA-RFAQLPLanHPQITVVDGGAERADS 88
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTpEFRQLLG--DPSIQLVAGGDTRQDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 89 VLAGIQA-AGNAPWVLVHDAARPCLHQDDLARLLALSETSKVGGILAAPVRDTMKRAEpGKQAIAHTVDRVDLWHALTPQ 167
Cdd:pfam01128 79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658549105 168 FFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
9-227 |
1.12e-98 |
|
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: 286.49 E-value: 1.12e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 9 CAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGDARFAQLPLANHPQITVVDGGAERADS 88
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 89 VLAGIQAAGNAPWVLVHDAARPCLHQDDLARLLALSETSKvGGILAAPVRDTMKRAEPGKQaIAHTVDRVDLWHALTPQF 168
Cdd:TIGR00453 81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAG-AAILALPVADTLKRVEADGF-VVETVDREGLWAAQTPQA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 658549105 169 FPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
11-232 |
2.50e-98 |
|
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: 285.49 E-value: 2.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 11 VVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGD-ARFAQL--PLANHPQITVVDGGAERAD 87
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 88 SVLAGIQAAGNAP-WVLVHDAARPCLHQDDLARLLALSETSkVGGILAAPVRDTMKRAEPGkQAIAHTVDRVDLWHALTP 166
Cdd:COG1211 81 SVRNGLEALPDDDdWVLVHDAARPLVSPELIDRVIEAAREY-GAAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549105 167 QFFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYLTRSTH 232
Cdd:COG1211 159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-223 |
1.06e-85 |
|
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: 253.60 E-value: 1.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 8 VCAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGDARFAQ--LPLANHPQITVVDGGAER 85
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 86 ADSVLAGIQAAGNAP--WVLVHDAARPCLHQDDLARLLALSEtSKVGGILAAPVRDTMKRAEpGKQAIAHTVDRVDLWHA 163
Cdd:cd02516 81 QDSVLNGLKALPDADpdIVLIHDAARPFVSPELIDRLIDALK-EYGAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 164 LTPQFFPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLA 223
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
6-230 |
3.81e-52 |
|
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: 172.72 E-value: 3.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 6 SDVCAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISPGDARFAQLPLANHPQITVVDGGAER 85
Cdd:PRK09382 4 SDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGGATR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 86 ADSVLAGIQAAgNAPWVLVHDAARPCLHQDDLARLL-ALSETSkvgGILAA-PVRDTMKRAEPgkqaiahTVDRVDLWHA 163
Cdd:PRK09382 84 QESVRNALEAL-DSEYVLIHDAARPFVPKELIDRLIeALDKAD---CVLPAlPVADTLKRANE-------TVDREGLKLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658549105 164 LTPQFFPRELlhdcLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLAEFYLTRS 230
Cdd:PRK09382 153 QTPQLSRTKT----LKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLSPS 215
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
14-223 |
5.69e-42 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 142.32 E-value: 5.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 14 AAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIA-----ISPGDARFAQLPLANHpQITVVDGGAERADS 88
Cdd:PRK13385 9 AAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVtqaqeRKHVQDLMKQLNVADQ-RVEVVKGGTERQES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 89 VLAGIQAAGNAPWVLVHDAARPCLHQDDLARLLALSETSKvGGILAAPVRDTMKRAEPGKqaIAHTVDRVDLWHALTPQF 168
Cdd:PRK13385 88 VAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYG-AAICAVEVKDTVKRVKDKQ--VIETVDRNELWQGQTPQA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658549105 169 FPRELLHDCLTRALKEGATITDEASALEYCGFHPELVEGRADNIKVTRPEDLQLA 223
Cdd:PRK13385 165 FELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLA 219
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
2-235 |
5.95e-34 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 122.15 E-value: 5.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 2 AVTFSDVCAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHPRVKRVIIAISP--------------GDARFAq 67
Cdd:PLN02728 19 VVKEKSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPsyrdvfeeavenidVPLKFA- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 68 LPlanhpqitvvdgGAERADSVLAGIQAA-GNAPWVLVHDAARPCLHQDDLARLLalSETSKVGG-ILAAPVRDTMKRAE 145
Cdd:PLN02728 98 LP------------GKERQDSVFNGLQEVdANSELVCIHDSARPLVTSADIEKVL--KDAAVHGAaVLGVPVKATIKEAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 146 PGkQAIAHTVDRVDLWHALTPQFFPRELLHDCLTRALKEGATITDEASALEYCGfHP-ELVEGRADNIKVTRPEDLQLAE 224
Cdd:PLN02728 164 SD-SFVVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALK-HPvFITEGSYTNIKVTTPDDMLVAE 241
|
250
....*....|.
gi 658549105 225 FYLTRSTHQEK 235
Cdd:PLN02728 242 RILNERSDAEV 252
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
6-139 |
7.42e-13 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 64.80 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 6 SDVCAVVPAAGFGRRMQTecPKQYLSIGDKTILEHAVAALLAHpRVKRVIIAISPGDARFAqlPLANHPQITVV---DGG 82
Cdd:COG2068 2 SKVAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAA-GLDPVVVVLGADAEEVA--AALAGLGVRVVvnpDWE 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 658549105 83 AERADSVLAGIQAA-GNAPWVLVHDAARPCLHQDDLARLLALSETSkvGGILAAPVRD 139
Cdd:COG2068 77 EGMSSSLRAGLAALpADADAVLVLLGDQPLVTAETLRRLLAAFRES--PASIVAPTYD 132
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
8-135 |
4.99e-12 |
|
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: 62.58 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 8 VCAVVPAAGFGRRMQTecPKQYLSIGDKTILEHAVAALLAHPRVKrvIIAISPGDARFAQLPLANHPQITVVDGGAER-- 85
Cdd:cd04182 1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSR--VIVVLGAEADAVRAALAGLPVVVVINPDWEEgm 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 658549105 86 ADSVLAGIQAA-GNAPWVLVHDAARPCLHQDDLARLLALSETSKvGGILAA 135
Cdd:cd04182 77 SSSLAAGLEALpADADAVLILLADQPLVTAETLRALIDAFREDG-AGIVAP 126
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
10-139 |
1.61e-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: 57.59 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 10 AVVPAAGFGRRMQTecPKQYLSIGDKTILEHAVAALLAHprVKRVIIaISPGDARFAQLPLANHPQITVVDGGAERADSV 89
Cdd:pfam12804 1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRPA--GDEVVV-VANDEEVLAALAGLGVPVVPDPDPGQGPLAGL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 658549105 90 LAGIQAAGNAPWVLVHDAARPCLHQDDLARLLALSETSkvGGILAAPVRD 139
Cdd:pfam12804 76 LAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEES--GADIVVPVYD 123
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
10-123 |
4.44e-08 |
|
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.
Pssm-ID: 274516 Cd Length: 188 Bit Score: 51.57 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 10 AVVPAAGFGRRMQTecPKQYLSIGDKTILEHAVAALLAHpRVKRVIIAISP-GDARFAQlpLANHPQITVVDGGAER--- 85
Cdd:TIGR03310 2 AIILAAGLSSRMGQ--NKLLLPYKGKTILEHVVDNALRL-FFDEVILVLGHeADELVAL--LANHSNITLVHNPQYAegq 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 658549105 86 ADSVLAGIQAAGNAPWVLVHDAARPCLHQDDLARLLAL 123
Cdd:TIGR03310 77 SSSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLEA 114
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
5-146 |
7.80e-08 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 52.06 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 5 FSDVCAVVPAAGFGRRMQTEcPKQYLSIGDKTILEHAVAALlaHPRVKRVIIAISPGDARFAQLplanHPQITVVDGGAE 84
Cdd:PRK14489 3 ISQIAGVILAGGLSRRMNGR-DKALILLGGKPLIERVVDRL--RPQFARIHLNINRDPARYQDL----FPGLPVYPDILP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658549105 85 RADSVLAGIQAA---GNAPWVLVHDAARPCLhQDDLARLlaLSETSKVGGILAAPVRDTmKRAEP 146
Cdd:PRK14489 76 GFQGPLSGILAGlehADSEYLFVVACDTPFL-PENLVKR--LSKALAIEGADIAVPHDG-ERAHP 136
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
10-59 |
1.89e-07 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 50.15 E-value: 1.89e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 658549105 10 AVVPAAGFGRRMQ--TE-CPKQYLSIGDKTILEHAVAALLAHPrVKRVIIAIS 59
Cdd:COG1208 2 AVILAGGLGTRLRplTDtRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG 53
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
10-60 |
4.41e-07 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 49.12 E-value: 4.41e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 658549105 10 AVVPAAGFGRRMQ--TE-CPKQYLSIGDKTILEHAVAALLAHPrVKRVIIAISP 60
Cdd:cd04181 1 AVILAAGKGTRLRplTDtRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGY 53
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
10-80 |
1.11e-06 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 47.93 E-value: 1.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658549105 10 AVVPAAGFGRRMQ---TECPKQYLSIGDKTILEHAVAALLAHpRVKRVIIAISPGDARFAQLPLANHPQITVVD 80
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAELIEEALARPGPDVTFVY 74
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
10-56 |
1.20e-06 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 48.00 E-value: 1.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 658549105 10 AVVPAAGFGRRMQT---ECPKQYLSIGDKTILEHAVAALLAHpRVKRVII 56
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVI 49
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
10-61 |
1.78e-04 |
|
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.
Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 41.75 E-value: 1.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 658549105 10 AVVPAAGFGRRM--QTEC-PKQYLSIGDKTILEHAVAALLAhPRVKRVIIAISPG 61
Cdd:cd02541 3 AVIPAAGLGTRFlpATKAiPKEMLPIVDKPVIQYIVEEAVA-AGIEDIIIVTGRG 56
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
10-79 |
4.60e-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: 37.11 E-value: 4.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 10 AVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLAHpRVKRVIIAISPGDARFAQlpLANHPQITVV 79
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQVKK--ALANPNVEFV 67
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
10-56 |
5.79e-03 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 36.78 E-value: 5.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 658549105 10 AVVPAAGFGRRMQ--TE-CPKQYLSIGDKTILEHAVaALLAHPRVKRVII 56
Cdd:cd06422 2 AMILAAGLGTRMRplTDtRPKPLVPVAGKPLIDHAL-DRLAAAGIRRIVV 50
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-122 |
7.80e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 36.84 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549105 6 SDVCAVVPAAGFGRRMQTECPKQYLSIGDKTILEHAVAALLA-HPRvkRVIIAISPGDARFAQLPLANHPQITVVD---- 80
Cdd:PRK14352 3 RPTAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGlAPQ--HLVVVVGHDRERVAPAVAELAPEVDIAVqdeq 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 658549105 81 GGAERAdsVLAGIQAAGNAP--WVLVHDAARPCLHQDDLARLLA 122
Cdd:PRK14352 81 PGTGHA--VQCALEALPADFdgTVVVTAGDVPLLDGETLADLVA 122
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
10-40 |
7.92e-03 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 36.34 E-value: 7.92e-03
10 20 30
....*....|....*....|....*....|....
gi 658549105 10 AVVPAAGFGRRMQ--TE-CPKQYLSIGDKTILEH 40
Cdd:cd06426 1 VVIMAGGKGTRLRplTEnTPKPMLKVGGKPILET 34
|
|
| |
