|
Name |
Accession |
Description |
Interval |
E-value |
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
45-271 |
1.31e-80 |
|
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: 248.21 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516 81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157412261 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516 154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
|
|
| ISPD_C |
pfam18706 |
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ... |
281-447 |
4.83e-78 |
|
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.
Pssm-ID: 465843 Cd Length: 169 Bit Score: 239.94 E-value: 4.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 281 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 358
Cdd:pfam18706 1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 359 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQDEQKLQESLGQSAAIIAALVKERNS 438
Cdd:pfam18706 81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQDEQKLQESLRQGAAIIAALIKERNP 160
|
....*....
gi 157412261 439 ALVGQLLVA 447
Cdd:pfam18706 161 ALVGQLLVA 169
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
48-278 |
3.31e-58 |
|
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: 190.73 E-value: 3.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 48 VLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYG-HKRISLAEAGATRHR 126
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 127 SIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKH 206
Cdd:COG1211 81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157412261 207 RASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPALWKVTYKQDLCAAEAMIKEK 278
Cdd:COG1211 153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSEDNIKITTPEDLALAEALLRSR 222
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
45-279 |
7.32e-49 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 166.46 E-value: 7.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGATR 124
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGGAER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 125 HRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:PRK00155 83 QDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157412261 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCAAEAMIKEKI 279
Cdd:PRK00155 154 GLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLALAEAILKRRI 226
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
46-273 |
1.32e-43 |
|
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: 152.44 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRygHKRISLAEAGATRH 125
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVA--RAVPKIVAGGDTRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 126 RSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAK 205
Cdd:TIGR00453 79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157412261 206 HRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEA 273
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALAEA 215
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
47-277 |
4.48e-37 |
|
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: 134.88 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 47 AVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIqryGHKRISLAEAGATRHR 126
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 127 SIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTVISPSADGHLDHSLDRA 204
Cdd:pfam01128 78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTIKRVEADGVVAGTPDRS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157412261 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMIKE 277
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
45-271 |
1.31e-80 |
|
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: 248.21 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYGHKRISLAEAGATR 124
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 125 HRSIFNGLKALAEDqpdckltKPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:cd02516 81 QDSVLNGLKALPDA-------DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157412261 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAA 271
Cdd:cd02516 154 KLWAAQTPQAFRLDLLLKAHRQASEEGEEF-TDDASLVEAAGG-KVALVEGSEDNIKITTPEDLALA 218
|
|
| ISPD_C |
pfam18706 |
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the ... |
281-447 |
4.83e-78 |
|
D-ribitol-5-phosphate cytidylyltransferase C-terminal domain; This domain is located at the C-terminal region of ISPD (isoprenoid synthase domain containing protein, EC:2.7.7.40), pfam01128. Structural homologs can be found in two distinct alpha/beta protein families including the seven-stranded NAD(P) (H)-dependent short-chain dehydrogenases/reductases and five-stranded response regulator proteins involved in bacterial sensing systems.
Pssm-ID: 465843 Cd Length: 169 Bit Score: 239.94 E-value: 4.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 281 QEICVVMNTK-DEESVGHLLEEALRKELNCMKITSTVMDHIGGDIRNFI-EQCYSFICVNVVSPDSQETRKLLRILEESS 358
Cdd:pfam18706 1 QEICVVTDTKeDAEHVGHLLEEVLKSELNHVKVTSTSLCPDGSDLQQIIlEQCYNFICVNVKTSDFQETQKLVSMLEESN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 359 LPLLYPVVVVLVHCFDFTSVPLAQKMESLVWIRGLAKEVKERNILLSGLLLNYSQDEQKLQESLGQSAAIIAALVKERNS 438
Cdd:pfam18706 81 LSILYPVVVVSVHLLDFKSVSFSQKMENLMAIREFAKEVKKRNILLYGLLINYSQDEQKLQESLRQGAAIIAALIKERNP 160
|
....*....
gi 157412261 439 ALVGQLLVA 447
Cdd:pfam18706 161 ALVGQLLVA 169
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
48-278 |
3.31e-58 |
|
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: 190.73 E-value: 3.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 48 VLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYG-HKRISLAEAGATRHR 126
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGiDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 127 SIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAKH 206
Cdd:COG1211 81 SVRNGLEALPDD--------DDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157412261 207 RASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClQLALKYCHRkAKLVEGPPALWKVTYKQDLCAAEAMIKEK 278
Cdd:COG1211 153 WAAQTPQGFRLDLLLEAHEAAAADGLEFTDDA-SLVERLGLP-VRLVEGSEDNIKITTPEDLALAEALLRSR 222
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
45-279 |
7.32e-49 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 166.46 E-value: 7.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 45 VAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGATR 124
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK-DPKVTVVAGGAER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 125 HRSIFNGLKALAEDqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRA 204
Cdd:PRK00155 83 QDSVLNGLQALPDD---------DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157412261 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEG-PPALwKVTYKQDLCAAEAMIKEKI 279
Cdd:PRK00155 154 GLWAAQTPQGFRIELLREALARALAEGKTITDDA--SAVERLGKPVRLVEGrYDNI-KITTPEDLALAEAILKRRI 226
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
46-273 |
1.32e-43 |
|
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: 152.44 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRygHKRISLAEAGATRH 125
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVA--RAVPKIVAGGDTRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 126 RSIFNGLKALAEdqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLDRAK 205
Cdd:TIGR00453 79 DSVRNGLKALKD---------AEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157412261 206 HRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEA 273
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEKLGGKVQLVEGDALNFKITTPEDLALAEA 215
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
47-277 |
4.48e-37 |
|
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: 134.88 E-value: 4.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 47 AVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIqryGHKRISLAEAGATRHR 126
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL---GDPSIQLVAGGDTRQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 127 SIFNGLKALAEDQpdckltkpEVVIIHDAVRPFVEEDILLRvVLAAKEHGAAGAIR--PLVSTVISPSADGHLDHSLDRA 204
Cdd:pfam01128 78 SVLNGLKALAGTA--------KFVLVHDGARPCLPHADLAR-LLAALETGTQGAILalPVTDTIKRVEADGVVAGTPDRS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157412261 205 KHRASEMPQAFLFDVIYEAYQQCSDFDLEFGTEClqLALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMIKE 277
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA--SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
44-275 |
9.29e-32 |
|
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: 124.57 E-value: 9.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 44 TVAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYghKRISLAEAGAT 123
Cdd:PRK09382 5 DISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI--KFVTLVTGGAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 124 RHRSIFNGLKALAEdqpdckltkpEVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVIspsadgHLDHSLDR 203
Cdd:PRK09382 83 RQESVRNALEALDS----------EYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLK------RANETVDR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157412261 204 AKHRASEMPQAFLFDVIYEAYQQCSDFdlefgTECLQlALKYCHRKAKLVEGPPALWKVTYKQDLCAAEAMI 275
Cdd:PRK09382 147 EGLKLIQTPQLSRTKTLKAAADGRGDF-----TDDSS-AAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
46-282 |
2.03e-22 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 95.32 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 46 AAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRY--GHKRISLAEAGAT 123
Cdd:PRK13385 4 ELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLnvADQRVEVVKGGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 124 RHRSIFNGLKALAEDQpdckltkpeVVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISpSADGHLDHSLDR 203
Cdd:PRK13385 84 RQESVAAGLDRIGNED---------VILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKR-VKDKQVIETVDR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157412261 204 AKHRASEMPQAFLFDVIYEAYQQCSDfDLEFGTECLQLALKYCHrKAKLVEGPPALWKVTYKQDLCAAEAMIKEKISQE 282
Cdd:PRK13385 154 NELWQGQTPQAFELKILQKAHRLASE-QQFLGTDEASLVERSPH-PVKLVQGSYYNIKLTTPEDMPLAKAILQGDIADD 230
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
43-283 |
6.91e-22 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 94.41 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 43 GTVAAVLPAGGCGERMGVRTPKQFCRVLERPLISYTLQAMERVCWIKDIVVTVTGENMEAMRSIIQRYgHKRISLAEAGA 122
Cdd:PLN02728 23 KSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENI-DVPLKFALPGK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 123 TRHRSIFNGLKALaedQPDCKLtkpevVIIHDAVRPFVEEDILLRVVLAAKEHGAAGAIRPLVSTVISPSADGHLDHSLD 202
Cdd:PLN02728 102 ERQDSVFNGLQEV---DANSEL-----VCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 203 RAKHRASEMPQAFLFDVIYEAYQQCSDFDLEFgTECLQL--ALKychRKAKLVEGPPALWKVTYKQDLCAAEAMIKEKIS 280
Cdd:PLN02728 174 RKRLWEMQTPQVIKPELLRRGFELVEREGLEV-TDDVSIveALK---HPVFITEGSYTNIKVTTPDDMLVAERILNERSD 249
|
...
gi 157412261 281 QEI 283
Cdd:PLN02728 250 AEV 252
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
47-193 |
8.66e-06 |
|
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: 46.42 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 47 AVLPAGGCGERMG---VRTPKQFCRVLERPLISYTLQAMERVcWIKDIVVtVTGENMEAmrsIIQRYG-----HKRISLA 118
Cdd:cd04181 1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARA-GIDEIIL-VVGYLGEQ---IEEYFGdgskfGVNIEYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 119 E-------AGAtrhrsIFNGLKALAEDqpdckltkpEVVIIH-DAVrpfVEEDiLLRVVLAAKEHGAAGAIrpLVSTVIS 190
Cdd:cd04181 76 VqeeplgtAGA-----VRNAEDFLGDD---------DFLVVNgDVL---TDLD-LSELLRFHREKGADATI--AVKEVED 135
|
...
gi 157412261 191 PSA 193
Cdd:cd04181 136 PSR 138
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
47-181 |
2.32e-05 |
|
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: 44.49 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 47 AVLPAGGCGERMGvrTPKQFCRVLERPLISYTLQAMERVCwiKDIVVtVTGEnmEAMRSIIQRYGHKRISLAEAGATRHR 126
Cdd:pfam12804 1 AVILAGGRSSRMG--GDKALLPLGGKPLLERVLERLRPAG--DEVVV-VAND--EEVLAALAGLGVPVVPDPDPGQGPLA 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 157412261 127 SIFNGLKALAEDQPdckltkpeVVIIH-DAvrPFVEEDILLRVVLAAKEHGAAGAI 181
Cdd:pfam12804 74 GLLAALRAAPGADA--------VLVLAcDM--PFLTPELLRRLLAAAEESGADIVV 119
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
47-95 |
2.94e-05 |
|
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: 45.14 E-value: 2.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 157412261 47 AVLPAGGCGERMG---VRTPKQFCRVLERPLISYTLQAMERvCWIKDIVVTV 95
Cdd:COG1208 2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAA-AGITEIVINV 52
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
45-183 |
3.05e-05 |
|
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: 44.47 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 45 VAAVLPAGGCGERMGvrTPKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTGENMEAMRSIIQRYGHKRISLAEA---- 120
Cdd:cd04182 1 IAAIILAAGRSSRMG--GNKLLLPLDGKPLLRHALDAALAAG-LSRVIV-VLGAEADAVRAALAGLPVVVVINPDWeegm 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157412261 121 GAtrhrSIFNGLKALAEDqpdckltkPEVVIIHDAVRPFVEEDILLRVVLAAKEHGaAGAIRP 183
Cdd:cd04182 77 SS----SLAAGLEALPAD--------ADAVLILLADQPLVTAETLRALIDAFREDG-AGIVAP 126
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
51-115 |
6.74e-04 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 40.64 E-value: 6.74e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157412261 51 AGGCGERMGvRTPKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTGENMEAMRSIIQRYGHKRI 115
Cdd:COG2266 2 AGGKGTRLG-GGEKPLLEICGKPMIDRVIDALEESC-IDKIYV-AVSPNTPKTREYLKERGVEVI 63
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
47-97 |
1.09e-03 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 40.61 E-value: 1.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 157412261 47 AVLPAGGCGERMGVRT---PKQFCRVLERPLISYTLQAMERVCwIKDIVVtVTG 97
Cdd:COG1213 2 AVILAAGRGSRLGPLTddiPKCLVEIGGKTLLERQLEALAAAG-IKDIVV-VTG 53
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
47-120 |
3.85e-03 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 38.70 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157412261 47 AVLPAGGCGERMGVRT---PKQFCRVLERPLISYTLQAMeRVCWIKDIVVtVTGENMEAMRSII---QRYG--------H 112
Cdd:cd04189 3 GLILAGGKGTRLRPLTytrPKQLIPVAGKPIIQYAIEDL-REAGIEDIGI-VVGPTGEEIKEALgdgSRFGvrityilqE 80
|
....*...
gi 157412261 113 KRISLAEA 120
Cdd:cd04189 81 EPLGLAHA 88
|
|
| |
