|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-232 |
2.99e-125 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 354.05 E-value: 2.99e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 8 VCAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGD-SRFAQLPLANHPQITVVDGGEERA 86
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 87 DSVLAGIKAVGDAEWVLVHDAARPCLHQDDLARLLTLSETSrTGGILAAPVRDTMKRAEPGKNaIAHTVDRSGLWHALTP 166
Cdd:PRK00155 84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664316 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
10-229 |
2.61e-115 |
|
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: 328.64 E-value: 2.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 10 AVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGD-SRFAQLPLanHPQITVVDGGEERADS 88
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 89 VLAGIKAV-GDAEWVLVHDAARPCLHQDDLARLLTLSETSRTGGILAAPVRDTMKRAEpGKNAIAHTVDRSGLWHALTPQ 167
Cdd:pfam01128 79 VLNGLKALaGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446664316 168 FFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
9-227 |
3.68e-106 |
|
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: 305.37 E-value: 3.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 9 CAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGDSRFAQLPLANHPQITVVDGGEERADS 88
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 89 VLAGIKAVGDAEWVLVHDAARPCLHQDDLARLLTLSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRSGLWHALTPQF 168
Cdd:TIGR00453 81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446664316 169 FPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
11-229 |
2.68e-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: 2.68e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 11 VVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGD-SRFAQL--PLANHPQITVVDGGEERAD 87
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 88 SVLAGIKAV-GDAEWVLVHDAARPCLHQDDLARLLTLSETSRtGGILAAPVRDTMKRAEPGkNAIAHTVDRSGLWHALTP 166
Cdd:COG1211 81 SVRNGLEALpDDDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446664316 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211 159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-223 |
2.50e-91 |
|
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: 267.85 E-value: 2.50e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 8 VCAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGDSRFAQ--LPLANHPQITVVDGGEER 85
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 86 ADSVLAGIKAVG--DAEWVLVHDAARPCLHQDDLARLLTLSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRSGLWHA 163
Cdd:cd02516 81 QDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 164 LTPQFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-232 |
2.99e-125 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 354.05 E-value: 2.99e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 8 VCAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGD-SRFAQLPLANHPQITVVDGGEERA 86
Cdd:PRK00155 4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 87 DSVLAGIKAVGDAEWVLVHDAARPCLHQDDLARLLTLSETSrTGGILAAPVRDTMKRAEPGKNaIAHTVDRSGLWHALTP 166
Cdd:PRK00155 84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664316 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
|
|
| IspD |
pfam01128 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ... |
10-229 |
2.61e-115 |
|
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: 328.64 E-value: 2.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 10 AVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGD-SRFAQLPLanHPQITVVDGGEERADS 88
Cdd:pfam01128 1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 89 VLAGIKAV-GDAEWVLVHDAARPCLHQDDLARLLTLSETSRTGGILAAPVRDTMKRAEpGKNAIAHTVDRSGLWHALTPQ 167
Cdd:pfam01128 79 VLNGLKALaGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446664316 168 FFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
9-227 |
3.68e-106 |
|
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: 305.37 E-value: 3.68e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 9 CAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGDSRFAQLPLANHPQITVVDGGEERADS 88
Cdd:TIGR00453 1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 89 VLAGIKAVGDAEWVLVHDAARPCLHQDDLARLLTLSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRSGLWHALTPQF 168
Cdd:TIGR00453 81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446664316 169 FPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
11-229 |
2.68e-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: 2.68e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 11 VVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGD-SRFAQL--PLANHPQITVVDGGEERAD 87
Cdd:COG1211 1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 88 SVLAGIKAV-GDAEWVLVHDAARPCLHQDDLARLLTLSETSRtGGILAAPVRDTMKRAEPGkNAIAHTVDRSGLWHALTP 166
Cdd:COG1211 81 SVRNGLEALpDDDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446664316 167 QFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211 159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-223 |
2.50e-91 |
|
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: 267.85 E-value: 2.50e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 8 VCAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGDSRFAQ--LPLANHPQITVVDGGEER 85
Cdd:cd02516 1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 86 ADSVLAGIKAVG--DAEWVLVHDAARPCLHQDDLARLLTLSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRSGLWHA 163
Cdd:cd02516 81 QDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 164 LTPQFFPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:cd02516 159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
6-229 |
1.23e-55 |
|
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: 181.97 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 6 IDVCAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISPGDSRFAQLPLANHPQITVVDGGEER 85
Cdd:PRK09382 4 SDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGGATR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 86 ADSVLAGIKAVgDAEWVLVHDAARPCLHQDDLARLL-TLSETSrtgGILAA-PVRDTMKRAEPgknaiahTVDRSGLWHA 163
Cdd:PRK09382 84 QESVRNALEAL-DSEYVLIHDAARPFVPKELIDRLIeALDKAD---CVLPAlPVADTLKRANE-------TVDREGLKLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446664316 164 LTPQFFPRELlhdcLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:PRK09382 153 QTPQLSRTKT----LKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLSP 214
|
|
| PRK13385 |
PRK13385 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional |
14-223 |
6.07e-42 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
Pssm-ID: 184017 Cd Length: 230 Bit Score: 142.32 E-value: 6.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 14 AAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIV-----ISPGDSRFAQLPLANHpQITVVDGGEERADS 88
Cdd:PRK13385 9 AAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVtqaqeRKHVQDLMKQLNVADQ-RVEVVKGGTERQES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 89 VLAGIKAVGDAEWVLVHDAARPCLHQDDLARLLTLSETSRtGGILAAPVRDTMKRAEPGKNAiaHTVDRSGLWHALTPQF 168
Cdd:PRK13385 88 VAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYG-AAICAVEVKDTVKRVKDKQVI--ETVDRNELWQGQTPQA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446664316 169 FPRELLHDCLTRALNEGATITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:PRK13385 165 FELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLA 219
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
7-228 |
2.18e-36 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 128.70 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 7 DVCAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHPRVTRVIIVISP--------------GDSRFAqLPlan 72
Cdd:PLN02728 24 SVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPsyrdvfeeavenidVPLKFA-LP--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 73 hpqitvvdgGEERADSVLAGIKAV-GDAEWVLVHDAARPCLHQDDLARLLtlSETSRTGG-ILAAPVRDTMKRAEPGkNA 150
Cdd:PLN02728 100 ---------GKERQDSVFNGLQEVdANSELVCIHDSARPLVTSADIEKVL--KDAAVHGAaVLGVPVKATIKEANSD-SF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446664316 151 IAHTVDRSGLWHALTPQFFPRELLHDCLTRALNEGATITDEASALEYCGfHP-QLVEGRADNIKVTRPEDLALAEFYLT 228
Cdd:PLN02728 168 VVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALK-HPvFITEGSYTNIKVTTPDDMLVAERILN 245
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
8-139 |
1.75e-15 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 72.12 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 8 VCAVVPAAGYGRRMQTecPKQYLSIGNKTILEHSVHALLAHpRVTRVIIVISPGDSRFAqlPLANHPQITVV---DGGEE 84
Cdd:COG2068 4 VAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAA-GLDPVVVVLGADAEEVA--AALAGLGVRVVvnpDWEEG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446664316 85 RADSVLAGIKAV-GDAEWVLVHDAARPCLHQDDLARLLTLSEtsRTGGILAAPVRD 139
Cdd:COG2068 79 MSSSLRAGLAALpADADAVLVLLGDQPLVTAETLRRLLAAFR--ESPASIVAPTYD 132
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
8-137 |
4.02e-13 |
|
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: 65.27 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 8 VCAVVPAAGYGRRMQTecPKQYLSIGNKTILEHSVHALLAHpRVTRVIIVISPGDSRFAQLpLANHPQITVV--DGGEER 85
Cdd:cd04182 1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAA-GLSRVIVVLGAEADAVRAA-LAGLPVVVVInpDWEEGM 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446664316 86 ADSVLAGIKAV-GDAEWVLVHDAARPCLHQDDLARLLTLSetSRTGGILAAPV 137
Cdd:cd04182 77 SSSLAAGLEALpADADAVLILLADQPLVTAETLRALIDAF--REDGAGIVAPV 127
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
10-174 |
3.62e-11 |
|
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: 59.52 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 10 AVVPAAGYGRRMQTecPKQYLSIGNKTILEHSVHALLAhprVTRVIIVISPGDSRFAQLPLANHPQITVVDGGEERADSV 89
Cdd:pfam12804 1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRP---AGDEVVVVANDEEVLAALAGLGVPVVPDPDPGQGPLAGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 90 LAGIKAVGDAEWVLVHDAARPCLHQDDLARLLtlsetsrtggilaapvrdtmKRAEPGKNAIAHTVDRSGLWHALtpqFF 169
Cdd:pfam12804 76 LAALRAAPGADAVLVLACDMPFLTPELLRRLL--------------------AAAEESGADIVVPVYDGGRGHPL---LY 132
|
....*
gi 446664316 170 PRELL 174
Cdd:pfam12804 133 RRRLL 137
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
10-105 |
4.34e-10 |
|
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: 57.59 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 10 AVVPAAGYGRRMQ--TE-CPKQYLSIGNKTILEHSVHALLAHPrVTRVIIVISP---------GDSRfaqlplANHPQIT 77
Cdd:cd04181 1 AVILAAGKGTRLRplTDtRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYlgeqieeyfGDGS------KFGVNIE 73
|
90 100 110
....*....|....*....|....*....|
gi 446664316 78 VVDGGEER--ADSVLAGIKAVGDAEWVLVH 105
Cdd:cd04181 74 YVVQEEPLgtAGAVRNAEDFLGDDDFLVVN 103
|
|
| matur_MocA_YgfJ |
TIGR03310 |
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ... |
10-121 |
1.59e-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: 55.42 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 10 AVVPAAGYGRRMQTecPKQYLSIGNKTILEHSVHALLAHpRVTRVIIVISPGDSRFAQLpLANHPQITVV---DGGEERA 86
Cdd:TIGR03310 2 AIILAAGLSSRMGQ--NKLLLPYKGKTILEHVVDNALRL-FFDEVILVLGHEADELVAL-LANHSNITLVhnpQYAEGQS 77
|
90 100 110
....*....|....*....|....*....|....*
gi 446664316 87 DSVLAGIKAVGDAEWVLVHDAARPCLHQDDLARLL 121
Cdd:TIGR03310 78 SSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLL 112
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
10-59 |
6.75e-08 |
|
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: 51.69 E-value: 6.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446664316 10 AVVPAAGYGRRMQ--TE-CPKQYLSIGNKTILEHSVHALLAHPrVTRVIIVIS 59
Cdd:COG1208 2 AVILAGGLGTRLRplTDtRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG 53
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
10-80 |
1.14e-07 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 51.01 E-value: 1.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446664316 10 AVVPAAGYGRRMQ---TECPKQYLSIGNKTILEHSVHALLAHpRVTRVIIVISPGDSRFAQLPLANHPQITVVD 80
Cdd:COG1213 2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAELIEEALARPGPDVTFVY 74
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
5-146 |
5.44e-07 |
|
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: 48.26 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 5 NIDVCAVVPAAGYGRRMQTecPKQYLSIGNKTILEHSVHALlaHPRVTRVIIViSPGDSRFAQLPLanhPQITvvdggEE 84
Cdd:COG0746 2 TMPITGVILAGGRSRRMGQ--DKALLPLGGRPLLERVLERL--RPQVDEVVIV-ANRPERYAALGV---PVVP-----DD 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446664316 85 RADS-----VLAGIKAVgDAEWVLVH--DAarPCLHQDDLARLLTLSEtsrTGGILAAPVRDtmKRAEP 146
Cdd:COG0746 69 PPGAgplagILAALEAA-PAEWVLVLacDM--PFLPPDLVRRLLEALE---EGADAVVPRSG--GRLEP 129
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
10-57 |
9.82e-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: 48.00 E-value: 9.82e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446664316 10 AVVPAAGYGRRMQT---ECPKQYLSIGNKTILEHSVHALLAHpRVTRVIIV 57
Cdd:cd02523 1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIV 50
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
10-104 |
1.08e-05 |
|
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: 45.25 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 10 AVVPAAGYGRRMQ----TEcPKQYLSIGNKTILEHSVHAlLAHPRVTRVIIVISPG----------DSRFAQlplanhpQ 75
Cdd:cd04189 3 GLILAGGKGTRLRpltyTR-PKQLIPVAGKPIIQYAIED-LREAGIEDIGIVVGPTgeeikealgdGSRFGV-------R 73
|
90 100 110
....*....|....*....|....*....|.
gi 446664316 76 ITVVDGGEER--ADSVLAGIKAVGDAEWVLV 104
Cdd:cd04189 74 ITYILQEEPLglAHAVLAARDFLGDEPFVVY 104
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-130 |
6.36e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 43.39 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 7 DVCAVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLA-HPRvtRVIIVISPGDSRFAQLPLANHPQITVVDGGEER 85
Cdd:PRK14352 4 PTAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGlAPQ--HLVVVVGHDRERVAPAVAELAPEVDIAVQDEQP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446664316 86 --ADSVLAGIKAVGD--AEWVLVHDAARPCLHQDDLARLLTLSETSRTG 130
Cdd:PRK14352 82 gtGHAVQCALEALPAdfDGTVVVTAGDVPLLDGETLADLVATHTAEGNA 130
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
10-61 |
1.18e-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: 42.13 E-value: 1.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446664316 10 AVVPAAGYGRRM--QTEC-PKQYLSIGNKTILEHSVHALLAhPRVTRVIIVISPG 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 ... |
10-104 |
1.29e-04 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 41.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446664316 10 AVVPAAGYGRRMQTECPKQYLSIGNKTILEHSVHALLAHpRVTRVIIVISPGDSRFAQlpLANHPQITVVDGGEER--AD 87
Cdd:cd02540 1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQVKK--ALANPNVEFVLQEEQLgtGH 77
|
90
....*....|....*...
gi 446664316 88 SVLAGIKAV-GDAEWVLV 104
Cdd:cd02540 78 AVKQALPALkDFEGDVLV 95
|
|
| |
