|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-226 |
1.65e-116 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 331.33 E-value: 1.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNSEIIKRHlfKGIKLVPGG 80
Cdd:PRK00155 2 MMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD--PKVTVVAGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 81 KERQDSVYNGLRACdPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAV 160
Cdd:PRK00155 80 AERQDSVLNGLQAL-PDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998496109 161 QTPQVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILSR 226
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
6-226 |
2.04e-116 |
|
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: 330.94 E-value: 2.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 6 IIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNSEIIKRHLFKGIKLVPGGKERQD 85
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 86 SVYNGLRACDPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQTPQV 165
Cdd:COG1211 81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998496109 166 FRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILSR 226
Cdd:COG1211 161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
3-220 |
2.09e-106 |
|
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: 305.60 E-value: 2.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 3 VSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNsEIIKRHLFKGIKLVPGGKE 82
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAK-ELAKYGLSKVVKIVEGGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 83 RQDSVYNGLRACDPQ-TDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQ 161
Cdd:cd02516 80 RQDSVLNGLKALPDAdPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998496109 162 TPQVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIA 220
Cdd:cd02516 160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
4-224 |
2.91e-89 |
|
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: 262.22 E-value: 2.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 4 SAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNSEIIKRHLFKgikLVPGGKER 83
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK---IVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 84 QDSVYNGLRACdPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQTP 163
Cdd:TIGR00453 78 QDSVRNGLKAL-KDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998496109 164 QVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESIL 224
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
5-226 |
1.58e-78 |
|
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: 235.04 E-value: 1.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 5 AIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYcnseIIKRHLFKGIKLVPGGKERQ 84
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPE----FRQLLGDPSIQLVAGGDTRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 85 DSVYNGLRACDPQTDFVIIHDGVRPLINQDIVIKALSTAE-IYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQTP 163
Cdd:pfam01128 77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLARLLAALEtGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998496109 164 QVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILSR 226
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-226 |
1.65e-116 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 331.33 E-value: 1.65e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNSEIIKRHlfKGIKLVPGG 80
Cdd:PRK00155 2 MMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD--PKVTVVAGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 81 KERQDSVYNGLRACdPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAV 160
Cdd:PRK00155 80 AERQDSVLNGLQAL-PDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998496109 161 QTPQVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILSR 226
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
6-226 |
2.04e-116 |
|
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: 330.94 E-value: 2.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 6 IIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNSEIIKRHLFKGIKLVPGGKERQD 85
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 86 SVYNGLRACDPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQTPQV 165
Cdd:COG1211 81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998496109 166 FRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILSR 226
Cdd:COG1211 161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
3-220 |
2.09e-106 |
|
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: 305.60 E-value: 2.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 3 VSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNsEIIKRHLFKGIKLVPGGKE 82
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAK-ELAKYGLSKVVKIVEGGAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 83 RQDSVYNGLRACDPQ-TDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQ 161
Cdd:cd02516 80 RQDSVLNGLKALPDAdPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1998496109 162 TPQVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIA 220
Cdd:cd02516 160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
4-224 |
2.91e-89 |
|
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: 262.22 E-value: 2.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 4 SAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNSEIIKRHLFKgikLVPGGKER 83
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK---IVAGGDTR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 84 QDSVYNGLRACdPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQTP 163
Cdd:TIGR00453 78 QDSVRNGLKAL-KDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998496109 164 QVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESIL 224
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
5-226 |
1.58e-78 |
|
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: 235.04 E-value: 1.58e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 5 AIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYcnseIIKRHLFKGIKLVPGGKERQ 84
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPE----FRQLLGDPSIQLVAGGDTRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 85 DSVYNGLRACDPQTDFVIIHDGVRPLINQDIVIKALSTAE-IYGACGVAVPVKDTIKVVDEKGFVKNTPDRDRLWAVQTP 163
Cdd:pfam01128 77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLARLLAALEtGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998496109 164 QVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILSR 226
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
3-225 |
1.92e-71 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 218.06 E-value: 1.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 3 VSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVvgsnemeyCNSeiIKRHLFKGI-------- 74
Cdd:PLN02728 25 VSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVV--------CDP--SYRDVFEEAvenidvpl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 75 KLVPGGKERQDSVYNGLRACDPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKGFVKNTPDR 154
Cdd:PLN02728 95 KFALPGKERQDSVFNGLQEVDANSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998496109 155 DRLWAVQTPQVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILS 225
Cdd:PLN02728 175 KRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILN 245
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
1-224 |
5.63e-63 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 195.86 E-value: 5.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYCNSEIIKRHLFKG-IKLVPG 79
Cdd:PRK13385 1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQrVEVVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 80 GKERQDSVYNGLRACDPQtDFVIIHDGVRPLINQDIVIKALSTAEIYGACGVAVPVKDTIKVVDEKgFVKNTPDRDRLWA 159
Cdd:PRK13385 81 GTERQESVAAGLDRIGNE-DVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDK-QVIETVDRNELWQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998496109 160 VQTPQVFRYPLILKAHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESIL 224
Cdd:PRK13385 159 GQTPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAIL 223
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
1-226 |
2.31e-54 |
|
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: 178.12 E-value: 2.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKRINEIILVVGSNEMEYcnseiIKRHL--FKGIKLVP 78
Cdd:PRK09382 4 SDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAY-----MKKALpeIKFVTLVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 79 GGKERQDSVYNGLRACDpqTDFVIIHDGVRPLINQDI---VIKALSTAEiygaCGV-AVPVKDTIKVVDEkgfvknTPDR 154
Cdd:PRK09382 79 GGATRQESVRNALEALD--SEYVLIHDAARPFVPKELidrLIEALDKAD----CVLpALPVADTLKRANE------TVDR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998496109 155 DRLWAVQTPQVFRYPLILKAHEraREQEFigTDDTVLVERLGERVKIIEGSYENIKITTPEDLTIAESILSR 226
Cdd:PRK09382 147 EGLKLIQTPQLSRTKTLKAAAD--GRGDF--TDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLSP 214
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-137 |
4.12e-11 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 59.79 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 1 MKVSAIIAAAGHGQRMGAaiSKQFLNLKGKPIIVHTLDVFYRIkRINEIILVVGSNEmeycnSEIIKRHLFKGIKLV--P 78
Cdd:COG2068 2 SKVAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAA-GLDPVVVVLGADA-----EEVAAALAGLGVRVVvnP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 79 GGKERQ-DSVYNGLRACDPQTDFVIIHDGVRPLINQDIVIKALSTAEIYGAcGVAVPVKD 137
Cdd:COG2068 74 DWEEGMsSSLRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPA-SIVAPTYD 132
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
4-115 |
3.20e-10 |
|
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: 57.35 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 4 SAIIAAAGHGQRMGAaiSKQFLNLKGKPIIVHTLDVFYRIkRINEIILVVGSNEME----YCNSeiikrhlfKGIKLVPG 79
Cdd:TIGR03310 1 DAIILAAGLSSRMGQ--NKLLLPYKGKTILEHVVDNALRL-FFDEVILVLGHEADElvalLANH--------SNITLVHN 69
|
90 100 110
....*....|....*....|....*....|....*....
gi 1998496109 80 GKERQ---DSVYNGLRACDPQTDFVIIHdGVRPLINQDI 115
Cdd:TIGR03310 70 PQYAEgqsSSIKLGLELPVQSDGYLFLL-GDQPFVTPDI 107
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-135 |
2.03e-09 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 54.87 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 3 VSAIIAAAGHGQRMGAaiSKQFLNLKGKPIIVHTLDVFYRIkRINEIILVVGSNEmeycnsEIIKRHLfKGIKLVPGGKE 82
Cdd:cd04182 1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAA-GLSRVIVVLGAEA------DAVRAAL-AGLPVVVVINP 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998496109 83 RQ-----DSVYNGLRACDPQTDFVIIHDGVRPLINQDIvIKALSTAEIYGACGVAVPV 135
Cdd:cd04182 71 DWeegmsSSLAAGLEALPADADAVLILLADQPLVTAET-LRALIDAFREDGAGIVAPV 127
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
5-54 |
3.29e-07 |
|
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: 49.15 E-value: 3.29e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1998496109 5 AIIAAAGHGQRMGA---AISKQFLNLKGKPIIVHTLDVFYRIKrINEIILVVG 54
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVTG 52
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
5-137 |
7.18e-07 |
|
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: 47.57 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 5 AIIAAAGHGQRMGAaiSKQFLNLKGKPIIVHTLDvfyRIKRINEIILVVGSNEmeycnsEIIKRHLFKGIKLVPGGKERQ 84
Cdd:pfam12804 1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLE---RLRPAGDEVVVVANDE------EVLAALAGLGVPVVPDPDPGQ 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1998496109 85 ---DSVYNGLRACDPQTDFVIIH-DgvRPLINQDIVIKALSTAEIYGaCGVAVPVKD 137
Cdd:pfam12804 70 gplAGLLAALRAAPGADAVLVLAcD--MPFLTPELLRRLLAAAEESG-ADIVVPVYD 123
|
|
| glmU |
PRK14359 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-224 |
2.38e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 47.68 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYrikRINEIILVVGSNEMEYCnSEIIKRHlFKGIKLVpgg 80
Cdd:PRK14359 1 MKLSIIILAAGKGTRMKSSLPKVLHTICGKPMLFYILKEAF---AISDDVHVVLHHQKERI-KEAVLEY-FPGVIFH--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 81 keRQDSV-YNG----LRACDPQTDFVIIHDGVRPLI-----------NQDIVIKALSTAEIYGACGVAVPVKDTIKVVDE 144
Cdd:PRK14359 73 --TQDLEnYPGtggaLMGIEPKHERVLILNGDMPLVekdelekllenDADIVMSVFHLADPKGYGRVVIENGQVKKIVEQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 145 KGfvKNTPDRD------RLWAVQTPQVFRY-PLIlkaHERAREQEFIGTDDTVLVERLGERVKIIEGSYENIK-ITTPED 216
Cdd:PRK14359 151 KD--ANEEELKiksvnaGVYLFDRKLLEEYlPLL---KNQNAQKEYYLTDIIALAIEKGETIKAVFVDEENFMgVNSKFE 225
|
....*...
gi 1998496109 217 LTIAESIL 224
Cdd:PRK14359 226 LAKAEEIM 233
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-76 |
6.43e-06 |
|
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: 45.53 E-value: 6.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1998496109 5 AIIAAAGHGQRMG---AAISKQFLNLKGKPIIVHTLDvfyRIKR--INEIILVVGsnemeYcNSEIIKRHLFKGIKL 76
Cdd:COG1208 2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILE---RLAAagITEIVINVG-----Y-LAEQIEEYFGDGSRF 69
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-76 |
1.20e-05 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 44.85 E-value: 1.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998496109 5 AIIAAAGHGQRMG---AAISKQFLNLKGKPIIVHTLDVFYRIKrINEIILVVGsnemeYCNSEIIKRHLFKGIKL 76
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVVVTG-----YKAELIEEALARPGPDV 70
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
5-73 |
1.30e-05 |
|
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: 44.49 E-value: 1.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998496109 5 AIIAAAGHGQRMG---AAISKQFLNLKGKPIIVHTLDVFYRIKrINEIILVVGSnemeycNSEIIKRHLFKG 73
Cdd:cd04181 1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGY------LGEQIEEYFGDG 65
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-60 |
6.58e-05 |
|
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: 42.10 E-value: 6.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 1 MKVSAIIAAAGHGQRMGAaiSKQFLNLKGKPIIVHTLDvfyRIKRINEIILVVGSNEMEY 60
Cdd:COG0746 3 MPITGVILAGGRSRRMGQ--DKALLPLGGRPLLERVLE---RLRPQVDEVVIVANRPERY 57
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-59 |
6.79e-05 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 42.77 E-value: 6.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998496109 1 MKvsAIIAAAGHGQRMG---AAISKQFLNLKGKPIIVHTLDVFYRIKrINEIILVVGSNEME 59
Cdd:COG1209 1 MK--GIILAGGSGTRLRpltLTVSKQLLPVYDKPMIYYPLSTLMLAG-IREILIISTPEDGP 59
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
1-56 |
3.22e-04 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 40.17 E-value: 3.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAiSKQFLNLKGKPIIVHTLDVFyrIKRINEIILVVGSN 56
Cdd:PRK00317 2 PPITGVILAGGRSRRMGGV-DKGLQELNGKPLIQHVIERL--APQVDEIVINANRN 54
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
3-135 |
4.19e-04 |
|
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: 39.87 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998496109 3 VSAIIAAAGHGQRMGAAisKQFLNLKGKPIIVHTLDvfyRIKRINEIILVVGSNEmeycnseiIKRHLFKGIKLVPggKE 82
Cdd:cd02503 1 ITGVILAGGKSRRMGGD--KALLELGGKPLLEHVLE---RLKPLVDEVVISANRD--------QERYALLGVPVIP--DE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1998496109 83 RQDS-----VYNGLRACDPQTDFVIIHDGvrPLINQDIvIKALSTAEIYGaCGVAVPV 135
Cdd:cd02503 66 PPGKgplagILAALRAAPADWVLVLACDM--PFLPPEL-LERLLAAAEEG-ADAVVPK 119
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
5-54 |
1.54e-03 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 38.65 E-value: 1.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1998496109 5 AIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKrINEIILVVG 54
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALG-PDRIVVVVG 49
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-54 |
2.56e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 38.27 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKrINEIILVVG 54
Cdd:PRK14354 1 MNRYAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAG-IDKIVTVVG 53
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
1-54 |
3.40e-03 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 38.08 E-value: 3.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLDVFYRIKrINEIILVVG 54
Cdd:COG1207 1 SPLAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALG-PDRIVVVVG 53
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-38 |
7.58e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 36.93 E-value: 7.58e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1998496109 1 MKVSAIIAAAGHGQRMGAAISKQFLNLKGKPIIVHTLD 38
Cdd:PRK09451 4 SAMSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVID 41
|
|
| |
