|
Name |
Accession |
Description |
Interval |
E-value |
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
13-236 |
2.65e-103 |
|
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: 298.20 E-value: 2.65e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKAAAVVPGGASRQE 92
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 93 SVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTPQT 172
Cdd:COG1211 81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561288322 173 FRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:COG1211 161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
10-236 |
4.48e-95 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 277.78 E-value: 4.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLG-AMRDCIGRYriqKAAAVVPGGA 88
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPdFAELLLAKD---PKVTVVAGGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 89 SRQESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:PRK00155 81 ERQDSVLNGLQALP-DDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAAQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:PRK00155 160 TPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
10-227 |
6.31e-89 |
|
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: 261.69 E-value: 6.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDcIGRYRIQKAAAVVPGGAS 89
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE-LAKYGLSKVVKIVEGGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 90 RQESVFAGVEALP-RDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:cd02516 80 RQDSVLNGLKALPdADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIA 227
Cdd:cd02516 160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
11-231 |
2.09e-79 |
|
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: 237.57 E-value: 2.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 11 CAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKaaaVVPGGASR 90
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK---IVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 91 QESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:TIGR00453 78 QDSVRNGLKALK-DAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
12-233 |
2.15e-69 |
|
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: 212.31 E-value: 2.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 12 AVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQkaaaVVPGGASRQ 91
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQ----LVAGGDTRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 92 ESVFAGVEALPRDAGYLAVHDGARPLVTPEEID-LCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:pfam01128 77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLArLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKK 233
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
13-236 |
2.65e-103 |
|
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: 298.20 E-value: 2.65e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKAAAVVPGGASRQE 92
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 93 SVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTPQT 172
Cdd:COG1211 81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561288322 173 FRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:COG1211 161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
10-236 |
4.48e-95 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 277.78 E-value: 4.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLG-AMRDCIGRYriqKAAAVVPGGA 88
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPdFAELLLAKD---PKVTVVAGGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 89 SRQESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:PRK00155 81 ERQDSVLNGLQALP-DDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAAQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:PRK00155 160 TPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
10-227 |
6.31e-89 |
|
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: 261.69 E-value: 6.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDcIGRYRIQKAAAVVPGGAS 89
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE-LAKYGLSKVVKIVEGGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 90 RQESVFAGVEALP-RDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:cd02516 80 RQDSVLNGLKALPdADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIA 227
Cdd:cd02516 160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
11-231 |
2.09e-79 |
|
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: 237.57 E-value: 2.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 11 CAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKaaaVVPGGASR 90
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK---IVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 91 QESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:TIGR00453 78 QDSVRNGLKALK-DAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
12-233 |
2.15e-69 |
|
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: 212.31 E-value: 2.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 12 AVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQkaaaVVPGGASRQ 91
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQ----LVAGGDTRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 92 ESVFAGVEALPRDAGYLAVHDGARPLVTPEEID-LCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:pfam01128 77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLArLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKK 233
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
13-234 |
4.72e-63 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 197.26 E-value: 4.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKAAAVvPGgASRQE 92
Cdd:PLN02728 28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENIDVPLKFAL-PG-KERQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 93 SVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTPQT 172
Cdd:PLN02728 106 SVFNGLQEVDANSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWEMQTPQV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561288322 173 FRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKR 234
Cdd:PLN02728 186 IKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNER 247
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
13-231 |
3.12e-50 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 163.89 E-value: 3.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRI-QKAAAVVPGGASRQ 91
Cdd:PRK13385 6 IFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVaDQRVEVVKGGTERQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 92 ESVFAGVEALPRDAGYLaVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQrVLSTPDREGLWTVQTPQ 171
Cdd:PRK13385 86 ESVAAGLDRIGNEDVIL-VHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQ-VIETVDRNELWQGQTPQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 172 TFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:PRK13385 164 AFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAIL 223
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
10-231 |
1.47e-44 |
|
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: 153.08 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYriqKAAAVVPGGAS 89
Cdd:PRK09382 6 ISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI---KFVTLVTGGAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 90 RQESVFAGVEALprDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDsgqrvlSTPDREGLWTVQT 169
Cdd:PRK09382 83 RQESVRNALEAL--DSEYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKRAN------ETVDREGLKLIQT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561288322 170 PQTFRMDLYRRALSKaredGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:PRK09382 155 PQLSRTKTLKAAADG----RGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
12-141 |
5.34e-10 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 57.09 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFDGARaVGQVVIVCRKEDlGAMRDCIGRYRIQkaAAVVPGGASRQ 91
Cdd:COG2068 6 AIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAG-LDPVVVVLGADA-EEVAAALAGLGVR--VVVNPDWEEGM 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1561288322 92 -ESVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLcVRDAFKTGASALGTP 141
Cdd:COG2068 80 sSSLRAGLAALPADADAVLVLLGDQPLVTAETLRR-LLAAFRESPASIVAP 129
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
12-132 |
3.10e-09 |
|
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: 54.65 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 12 AVIAAAGRSARMGSGisKQFLPVLGVPAVVRTLRAFDgARAVGQVVIVCRKEDLGAMRDCIGRYRIQkaaaVVPGGASRQ 91
Cdd:TIGR03310 2 AIILAAGLSSRMGQN--KLLLPYKGKTILEHVVDNAL-RLFFDEVILVLGHEADELVALLANHSNIT----LVHNPQYAE 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1561288322 92 ---ESVFAGVEALPRDAGYLAVHdGARPLVTPEEIDLcVRDAFK 132
Cdd:TIGR03310 75 gqsSSIKLGLELPVQSDGYLFLL-GDQPFVTPDIIQL-LLEAFA 116
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
10-141 |
4.96e-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: 51.41 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 10 CCAVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFDGARAvGQVVIVCR---KEDLGAMRDCIGRYRIQKAAAVvpG 86
Cdd:cd04182 1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGL-SRVIVVLGaeaDAVRAALAGLPVVVVINPDWEE--G 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1561288322 87 GASrqeSVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLcVRDAFKTGASALGTP 141
Cdd:cd04182 76 MSS---SLAAGLEALPADADAVLILLADQPLVTAETLRA-LIDAFREDGAGIVAP 126
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
12-65 |
1.33e-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: 44.11 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1561288322 12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFdgARAVGQVVIVCRKEDL 65
Cdd:pfam12804 1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERL--RPAGDEVVVVANDEEV 50
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
12-64 |
2.74e-04 |
|
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: 40.56 E-value: 2.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1561288322 12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFdgARAVGQVVIVCRKED 64
Cdd:COG0746 7 GVILAGGRSRRMGQ--DKALLPLGGRPLLERVLERL--RPQVDEVVIVANRPE 55
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
12-64 |
1.04e-03 |
|
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: 38.71 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1561288322 12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFDGarAVGQVVIVCRKED 64
Cdd:cd02503 3 GVILAGGKSRRMGG--DKALLELGGKPLLEHVLERLKP--LVDEVVISANRDQ 51
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
12-63 |
1.68e-03 |
|
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: 38.37 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1561288322 12 AVIAAAGRSARMGS---GISKQFLPVLGVPAVVRTLRAFDGARaVGQVVIVC--RKE 63
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVTgyKKE 56
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
12-65 |
2.07e-03 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 38.30 E-value: 2.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1561288322 12 AVIAAAGRSARMG---SGISKQFLPVLGVPAVVRTLRAFDGArAVGQVVIVC--RKEDL 65
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTgyKAELI 59
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
10-121 |
2.65e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 38.30 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVcrkedlgamrdciGRYRIQKAAAVVPGGAS 89
Cdd:PRK14353 6 CLAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVV-------------GPGAEAVAAAAAKIAPD 72
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1561288322 90 ----RQE-------SVFAGVEALPRDAGYLAVHDGARPLVTPE 121
Cdd:PRK14353 73 aeifVQKerlgtahAVLAAREALAGGYGDVLVLYGDTPLITAE 115
|
|
|