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Conserved domains on  [gi|610427333|gb|AHW76209|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Neisseria meningitidis]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10794560)

2-C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-d-erythritol from 2-C-methyl-derythritol 4-phosphate and CTP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-226 9.86e-97

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: 281.10  E-value: 9.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333    6 IALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDTFADKVQTAFPQVRVWKNGGQTRAET 85
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   86 VRNGVAKLletglaAETDNILVHDAARCCLPSEALTRLIEQAGNaAEGGILAIPVADTLKCADG-GNISATVERTSLWQA 164
Cdd:TIGR00453  81 VRNGLKAL------KDAEFVLVHDAARPFVPKELLDRLLEALRK-AGAAILALPVADTLKRVEAdGFVVETVDREGLWAA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 610427333  165 QTPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLL 226
Cdd:TIGR00453 154 QTPQAFRTELLKKALARAKLEGfeITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
 
Name Accession Description Interval E-value
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-226 9.86e-97

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: 281.10  E-value: 9.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333    6 IALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDTFADKVQTAFPQVRVWKNGGQTRAET 85
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   86 VRNGVAKLletglaAETDNILVHDAARCCLPSEALTRLIEQAGNaAEGGILAIPVADTLKCADG-GNISATVERTSLWQA 164
Cdd:TIGR00453  81 VRNGLKAL------KDAEFVLVHDAARPFVPKELLDRLLEALRK-AGAAILALPVADTLKRVEAdGFVVETVDREGLWAA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 610427333  165 QTPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLL 226
Cdd:TIGR00453 154 QTPQAFRTELLKKALARAKLEGfeITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
2-227 1.36e-90

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 265.84  E-value: 1.36e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   2 KRKNIALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDT--FADKVQTAFPQVrVWKNGG 79
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRpdFAELLLAKDPKV-TVVAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  80 QTRAETVRNGVAKLletglaAETDNILVHDAARCCLPSEALTRLIEQAgNAAEGGILAIPVADTLK-CADGGNISATVER 158
Cdd:PRK00155  80 AERQDSVLNGLQAL------PDDDWVLVHDAARPFLTPDDIDRLIEAA-EETGAAILAVPVKDTIKrSDDGGGIVDTPDR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 610427333 159 TSLWQAQTPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLLD 227
Cdd:PRK00155 153 SGLWAAQTPQGFRIELLREALARALAEGktITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILK 223
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 8-228 8.90e-84

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: 248.51  E-value: 8.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   8 LIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPED--TFADKV-QTAFPQVRVWKNGGQTRAE 84
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDieYFEELLaKYGIDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  85 TVRNGVAKlletgLAAETDNILVHDAARCCLPSEALTRLIEQAGnAAEGGILAIPVADTLKCAD-GGNISATVERTSLWQ 163
Cdd:COG1211   81 SVRNGLEA-----LPDDDDWVLVHDAARPLVSPELIDRVIEAAR-EYGAAIPALPVTDTIKRVDdDGRVTETVDRSGLWA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 610427333 164 AQTPQLFRAGLLHRAL--AAENLDGITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLLDA 228
Cdd:COG1211  155 AQTPQGFRLDLLLEAHeaAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-221 1.07e-78

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: 235.50  E-value: 1.07e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   5 NIALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPED-TFADKVQTAFPQVRVWK-NGGQTR 82
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDiDLAKELAKYGLSKVVKIvEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  83 AETVRNGVAKLLEtglaAETDNILVHDAARCCLPSEALTRLIEQAgNAAEGGILAIPVADTLK-CADGGNISATVERTSL 161
Cdd:cd02516   81 QDSVLNGLKALPD----ADPDIVLIHDAARPFVSPELIDRLIDAL-KEYGAAIPAVPVTDTIKrVDDDGVVVETLDREKL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 610427333 162 WQAQTPQLFRAGLLHRAL--AAENLDGITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYI 221
Cdd:cd02516  156 WAAQTPQAFRLDLLLKAHrqASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLAL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 7-218 9.79e-58

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: 182.26  E-value: 9.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333    7 ALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDTFADKVQTAFPQVRVwKNGGQTRAETV 86
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQL-VAGGDTRQDSV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   87 RNGVaklleTGLAAETDNILVHDAARCCLPSEALTRLIEQAGNAAEGGILAIPVADTLKCADG-GNISATVERTSLWQAQ 165
Cdd:pfam01128  80 LNGL-----KALAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEAdGVVAGTPDRSGLWAAQ 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 610427333  166 TPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQD 218
Cdd:pfam01128 155 TPQGFRVDLLLAAHQRGDQPGaeITDDASLVEHAGGSVQVVPGRPDNLKITTPED 209
 
Name Accession Description Interval E-value
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-226 9.86e-97

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: 281.10  E-value: 9.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333    6 IALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDTFADKVQTAFPQVRVWKNGGQTRAET 85
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   86 VRNGVAKLletglaAETDNILVHDAARCCLPSEALTRLIEQAGNaAEGGILAIPVADTLKCADG-GNISATVERTSLWQA 164
Cdd:TIGR00453  81 VRNGLKAL------KDAEFVLVHDAARPFVPKELLDRLLEALRK-AGAAILALPVADTLKRVEAdGFVVETVDREGLWAA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 610427333  165 QTPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLL 226
Cdd:TIGR00453 154 QTPQAFRTELLKKALARAKLEGfeITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
2-227 1.36e-90

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 265.84  E-value: 1.36e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   2 KRKNIALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDT--FADKVQTAFPQVrVWKNGG 79
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRpdFAELLLAKDPKV-TVVAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  80 QTRAETVRNGVAKLletglaAETDNILVHDAARCCLPSEALTRLIEQAgNAAEGGILAIPVADTLK-CADGGNISATVER 158
Cdd:PRK00155  80 AERQDSVLNGLQAL------PDDDWVLVHDAARPFLTPDDIDRLIEAA-EETGAAILAVPVKDTIKrSDDGGGIVDTPDR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 610427333 159 TSLWQAQTPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLLD 227
Cdd:PRK00155 153 SGLWAAQTPQGFRIELLREALARALAEGktITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILK 223
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 8-228 8.90e-84

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: 248.51  E-value: 8.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   8 LIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPED--TFADKV-QTAFPQVRVWKNGGQTRAE 84
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDieYFEELLaKYGIDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  85 TVRNGVAKlletgLAAETDNILVHDAARCCLPSEALTRLIEQAGnAAEGGILAIPVADTLKCAD-GGNISATVERTSLWQ 163
Cdd:COG1211   81 SVRNGLEA-----LPDDDDWVLVHDAARPLVSPELIDRVIEAAR-EYGAAIPALPVTDTIKRVDdDGRVTETVDRSGLWA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 610427333 164 AQTPQLFRAGLLHRAL--AAENLDGITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLLDA 228
Cdd:COG1211  155 AQTPQGFRLDLLLEAHeaAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-221 1.07e-78

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: 235.50  E-value: 1.07e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   5 NIALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPED-TFADKVQTAFPQVRVWK-NGGQTR 82
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDiDLAKELAKYGLSKVVKIvEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  83 AETVRNGVAKLLEtglaAETDNILVHDAARCCLPSEALTRLIEQAgNAAEGGILAIPVADTLK-CADGGNISATVERTSL 161
Cdd:cd02516   81 QDSVLNGLKALPD----ADPDIVLIHDAARPFVSPELIDRLIDAL-KEYGAAIPAVPVTDTIKrVDDDGVVVETLDREKL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 610427333 162 WQAQTPQLFRAGLLHRAL--AAENLDGITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYI 221
Cdd:cd02516  156 WAAQTPQAFRLDLLLKAHrqASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLAL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 7-218 9.79e-58

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: 182.26  E-value: 9.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333    7 ALIPAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDTFADKVQTAFPQVRVwKNGGQTRAETV 86
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQL-VAGGDTRQDSV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   87 RNGVaklleTGLAAETDNILVHDAARCCLPSEALTRLIEQAGNAAEGGILAIPVADTLKCADG-GNISATVERTSLWQAQ 165
Cdd:pfam01128  80 LNGL-----KALAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEAdGVVAGTPDRSGLWAAQ 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 610427333  166 TPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQD 218
Cdd:pfam01128 155 TPQGFRVDLLLAAHQRGDQPGaeITDDASLVEHAGGSVQVVPGRPDNLKITTPED 209
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-218 2.85e-50

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: 167.72  E-value: 2.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   1 MKRKNIALI-PAAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPED-TFADKVQTAFPQVRVWKnG 78
Cdd:PRK09382   1 TLMSDISLViVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDiAYMKKALPEIKFVTLVT-G 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  79 GQTRAETVRNGVAKLletglaaETDNILVHDAARCCLPSEALTRLIEQAGNaAEGGILAIPVADTLKCADggnisATVER 158
Cdd:PRK09382  80 GATRQESVRNALEAL-------DSEYVLIHDAARPFVPKELIDRLIEALDK-ADCVLPALPVADTLKRAN-----ETVDR 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333 159 TSLWQAQTPQLFRAGLLHRalAAENLDGITDEASAVEKLGIRPLLVQGDARNLKLTQPQD 218
Cdd:PRK09382 147 EGLKLIQTPQLSRTKTLKA--AADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKED 204
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 2-227 2.06e-28

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase


Pssm-ID: 215387  Cd Length: 252  Bit Score: 107.51  E-value: 2.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   2 KRKNIALIP-AAGIGARFGADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPedTFADKVQTAFPQVRV---WKN 77
Cdd:PLN02728  21 KEKSVSVILlAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDP--SYRDVFEEAVENIDVplkFAL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  78 GGQTRAETVRNGvakLLETGLAAETdnILVHDAARCCLPSEALTRLIEqagNAAEGG--ILAIPVADTLKCADGGN-ISA 154
Cdd:PLN02728  99 PGKERQDSVFNG---LQEVDANSEL--VCIHDSARPLVTSADIEKVLK---DAAVHGaaVLGVPVKATIKEANSDSfVVK 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 610427333 155 TVERTSLWQAQTPQLFRAGLLHRALAAENLDG--ITDEASAVEKLGIRPLLVQGDARNLKLTQPQDAYIVRLLLD 227
Cdd:PLN02728 171 TLDRKRLWEMQTPQVIKPELLRRGFELVEREGleVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILN 245
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 5-218 3.68e-27

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional


Pssm-ID: 184017  Cd Length: 230  Bit Score: 103.80  E-value: 3.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   5 NIALIPAAGIGARFG-ADKPKQYVEIGSKTVLEHTIGIFERHEAVDlTVVVVSPEdTFADKVQTAFPQVRVWKN------ 77
Cdd:PRK13385   2 NYELIFLAAGQGKRMnAPLNKMWLDLVGEPIFIHALRPFLADNRCS-KIIIVTQA-QERKHVQDLMKQLNVADQrvevvk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  78 GGQTRAETVRNGVAKlletglAAETDNILVHDAARCCLPSEALTRLIEQAGNAaEGGILAIPVADTLKCADGGNISATVE 157
Cdd:PRK13385  80 GGTERQESVAAGLDR------IGNEDVILVHDGARPFLTQDIIDRLLEGVAKY-GAAICAVEVKDTVKRVKDKQVIETVD 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 610427333 158 RTSLWQAQTPQLFRAGLLHRA--LAAENLDGITDEASAVEKLGIRPLLVQGDARNLKLTQPQD 218
Cdd:PRK13385 153 RNELWQGQTPQAFELKILQKAhrLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPED 215
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
7-142 3.23e-08

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 51.70  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   7 ALIPAAGIGARFGAdkPKQYVEIGSKTVLEHTIGIFERHEaVDLTVVVVSPEdtfADKVQTAFPQ--VRVWKN----GGQ 80
Cdd:COG2068    6 AIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAG-LDPVVVVLGAD---AEEVAAALAGlgVRVVVNpdweEGM 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 610427333  81 trAETVRNGVAKlletgLAAETDNILVHDAARCCLPSEALTRLIEQAgnAAEGGILAIPVAD 142
Cdd:COG2068   80 --SSSLRAGLAA-----LPADADAVLVLLGDQPLVTAETLRRLLAAF--RESPASIVAPTYD 132
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
7-77 3.90e-07

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 49.08  E-value: 3.90e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 610427333   7 ALIPAAGIGARFG---ADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVVVSPEDTFADKVQTAFPQVRVWKN 77
Cdd:COG1213    2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPDVTFVYN 75
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 7-54 2.73e-06

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 46.84  E-value: 2.73e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 610427333   7 ALIPAAGIGARFGA---DKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVV 54
Cdd:cd02523    1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT 51
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 7-95 8.88e-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: 41.78  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   7 ALIPAAGIGARFGAdkPKQYVEIGSKTVLEHTIGIFERHEAVDLtVVVVSPEDTFADKVQTAFPQVRV----WKNGgqtR 82
Cdd:cd04182    3 AIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSRV-IVVLGAEADAVRAALAGLPVVVVinpdWEEG---M 76

                         90
                 ....*....|...
gi 610427333  83 AETVRNGVAKLLE 95
Cdd:cd04182   77 SSSLAAGLEALPA 89
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 7-54 1.19e-04

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: 41.80  E-value: 1.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 610427333   7 ALIPAAGIGARFG---ADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVV 54
Cdd:cd04181    1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVV 51
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 7-142 1.92e-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: 40.64  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   7 ALIPAAGIGARFGADKPKqyVEIGSKTVLEHTIGIFerhEAVDLTVVVVSPEdtfaDKVQTAFPQVRVwknggqtrAETV 86
Cdd:cd02503    3 GVILAGGKSRRMGGDKAL--LELGGKPLLEHVLERL---KPLVDEVVISANR----DQERYALLGVPV--------IPDE 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 610427333  87 RNGVAKL--LETGL-AAETDNILVhdAArcC----LPSEALTRLIEQAGNAAEGgilAIPVAD 142
Cdd:cd02503   66 PPGKGPLagILAALrAAPADWVLV--LA--CdmpfLPPELLERLLAAAEEGADA---VVPKSG 121
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-54 4.31e-04

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: 40.14  E-value: 4.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 610427333   7 ALIPAAGIGARFG---ADKPKQYVEIGSKTVLEHTIGIFERHEAVDLTVVV 54
Cdd:COG1208    2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV 52
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 7-142 6.29e-04

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: 39.10  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333    7 ALIPAAGIGARFGADKPkqYVEIGSKTVLEHTIGIFErhEAVDLTVVVVSPEDTFAdkvQTAFPQVRVWKNGGQTR--AE 84
Cdd:pfam12804   1 AVILAGGRSSRMGGDKA--LLPLGGKPLLERVLERLR--PAGDEVVVVANDEEVLA---ALAGLGVPVVPDPDPGQgpLA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 610427333   85 TVRNGVAKlletglAAETDNILVhdaARC---CLPSEALTRLIEQAgnAAEGGILAIPVAD 142
Cdd:pfam12804  74 GLLAALRA------APGADAVLV---LACdmpFLTPELLRRLLAAA--EESGADIVVPVYD 123
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-142 3.69e-03

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: 37.09  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333   1 MKRKNIALIPAAGIGARFGADKPKqyVEIGSKTVLEHTIGIFErhEAVDLTVVVVSPEDTFadkvqtAFPQVRVWknggq 80
Cdd:COG0746    1 MTMPITGVILAGGRSRRMGQDKAL--LPLGGRPLLERVLERLR--PQVDEVVIVANRPERY------AALGVPVV----- 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 610427333  81 trAETVRN-----GVAKLLEtglAAETDNILVhdAArC---CLPSEALTRLIEQAGNAAEggiLAIPVAD 142
Cdd:COG0746   66 --PDDPPGagplaGILAALE---AAPAEWVLV--LA-CdmpFLPPDLVRRLLEALEEGAD---AVVPRSG 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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