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Conserved domains on  [gi|446168303|ref|WP_000246158|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Escherichia coli]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10011283)

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

EC:  2.7.7.60
Gene Ontology:  GO:0050518|GO:0019288
PubMed:  12691742|9445404
SCOP:  4002789

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-232 3.18e-123

D-ribitol-5-phosphate cytidylyltransferase;


:

Pssm-ID: 234670  Cd Length: 227  Bit Score: 348.66  E-value: 3.18e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLANHPQITVVDGGDERA 86
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  87 DSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEPGKNaIAHTVDRNGLWHALTP 166
Cdd:PRK00155  84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446168303 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-232 3.18e-123

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 348.66  E-value: 3.18e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLANHPQITVVDGGDERA 86
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  87 DSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEPGKNaIAHTVDRNGLWHALTP 166
Cdd:PRK00155  84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446168303 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 10-229 8.83e-116

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: 329.80  E-value: 8.83e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   10 AVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLanHPQITVVDGGDERADS 88
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   89 VLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQ 167
Cdd:pfam01128  79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446168303  168 FFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 9-227 2.98e-105

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: 303.05  E-value: 2.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303    9 CAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGGDERADS 88
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   89 VLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQF 168
Cdd:TIGR00453  81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446168303  169 FPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 11-229 2.57e-101

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: 293.19  E-value: 2.57e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  11 VVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQL--PLANHPQITVVDGGDERAD 87
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  88 SVLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRtGGILAAPVRDTMKRAEPGkNAIAHTVDRNGLWHALTP 166
Cdd:COG1211   81 SVRNGLEAlPDDDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446168303 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211  159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-223 2.36e-89

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 262.84  E-value: 2.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQ--LPLANHPQITVVDGGDER 85
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  86 ADSVLAGLKA--AGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHA 163
Cdd:cd02516   81 QDSVLNGLKAlpDADPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303 164 LTPQFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:cd02516  159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-232 3.18e-123

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 348.66  E-value: 3.18e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLANHPQITVVDGGDERA 86
Cdd:PRK00155   4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAERQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  87 DSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEPGKNaIAHTVDRNGLWHALTP 166
Cdd:PRK00155  84 DSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGG-IVDTPDRSGLWAAQTP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446168303 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTRTIH 232
Cdd:PRK00155 162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 10-229 8.83e-116

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: 329.80  E-value: 8.83e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   10 AVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQLPLanHPQITVVDGGDERADS 88
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   89 VLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQ 167
Cdd:pfam01128  79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVE-ADGVVAGTPDRSGLWAAQTPQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446168303  168 FFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:pfam01128 158 GFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 9-227 2.98e-105

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: 303.05  E-value: 2.98e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303    9 CAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGGDERADS 88
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   89 VLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHALTPQF 168
Cdd:TIGR00453  81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKA-GAAILALPVADTLKRVE-ADGFVVETVDREGLWAAQTPQA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446168303  169 FPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYL 227
Cdd:TIGR00453 159 FRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 11-229 2.57e-101

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: 293.19  E-value: 2.57e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  11 VVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGD-SRFAQL--PLANHPQITVVDGGDERAD 87
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  88 SVLAGLKA-AGDAQWVLVHDAARPCLHQDDLARLLALSETSRtGGILAAPVRDTMKRAEPGkNAIAHTVDRNGLWHALTP 166
Cdd:COG1211   81 SVRNGLEAlPDDDDWVLVHDAARPLVSPELIDRVIEAAREYG-AAIPALPVTDTIKRVDDD-GRVTETVDRSGLWAAQTP 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446168303 167 QFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:COG1211  159 QGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-223 2.36e-89

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 262.84  E-value: 2.36e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   8 VCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQ--LPLANHPQITVVDGGDER 85
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  86 ADSVLAGLKA--AGDAQWVLVHDAARPCLHQDDLARLLALSETSrTGGILAAPVRDTMKRAEpGKNAIAHTVDRNGLWHA 163
Cdd:cd02516   81 QDSVLNGLKAlpDADPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVD-DDGVVVETLDREKLWAA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303 164 LTPQFFPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:cd02516  159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-229 1.48e-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: 179.27  E-value: 1.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   3 TTHLDVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISPGDSRFAQLPLANHPQITVVDGG 82
Cdd:PRK09382   1 TLMSDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  83 DERADSVLAGLKAAgDAQWVLVHDAARPCLHQDDLARLL-ALSETSrtgGILAA-PVRDTMKRAEPgknaiahTVDRNGL 160
Cdd:PRK09382  81 ATRQESVRNALEAL-DSEYVLIHDAARPFVPKELIDRLIeALDKAD---CVLPAlPVADTLKRANE-------TVDREGL 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446168303 161 WHALTPQFFPRELlhdcLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALAEFYLTR 229
Cdd:PRK09382 150 KLIQTPQLSRTKT----LKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLSP 214
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 14-223 1.71e-41

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 141.16  E-value: 1.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  14 AAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIA-----ISPGDSRFAQLPLANHpQITVVDGGDERADS 88
Cdd:PRK13385   9 AAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVtqaqeRKHVQDLMKQLNVADQ-RVEVVKGGTERQES 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  89 VLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLALSETSRtGGILAAPVRDTMKRAEPGKNAiaHTVDRNGLWHALTPQF 168
Cdd:PRK13385  88 VAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYG-AAICAVEVKDTVKRVKDKQVI--ETVDRNELWQGQTPQA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446168303 169 FPRELLHDCLTRALNEGAAITDEASALEYCGFHPQLVEGRADNIKVTRPEDLALA 223
Cdd:PRK13385 165 FELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLA 219
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 7-228 2.13e-36

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 128.70  E-value: 2.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   7 DVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLAHPRVKRVVIAISP--------------GDSRFAqLPlan 72
Cdd:PLN02728  24 SVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPsyrdvfeeavenidVPLKFA-LP--- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303  73 hpqitvvdgGDERADSVLAGLKAA-GDAQWVLVHDAARPCLHQDDLARLLalSETSRTGG-ILAAPVRDTMKRAEPGkNA 150
Cdd:PLN02728 100 ---------GKERQDSVFNGLQEVdANSELVCIHDSARPLVTSADIEKVL--KDAAVHGAaVLGVPVKATIKEANSD-SF 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446168303 151 IAHTVDRNGLWHALTPQFFPRELLHDCLTRALNEGAAITDEASALEYCGfHP-QLVEGRADNIKVTRPEDLALAEFYLT 228
Cdd:PLN02728 168 VVKTLDRKRLWEMQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALK-HPvFITEGSYTNIKVTTPDDMLVAERILN 245
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
8-139 8.55e-13

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 64.80  E-value: 8.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   8 VCAVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHpRVKRVVIAISPGDSRFAqlPLANHPQITVV---DGGDE 84
Cdd:COG2068    4 VAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAA-GLDPVVVVLGADAEEVA--AALAGLGVRVVvnpDWEEG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446168303  85 RADSVLAGLKAA-GDAQWVLVHDAARPCLHQDDLARLLALSEtsRTGGILAAPVRD 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 6.79e-11

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: 59.50  E-value: 6.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   8 VCAVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHPRVKrvVIAISPGDSRFAQLPLANHPQITVVDGGDER-- 85
Cdd:cd04182    1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGLSR--VIVVLGAEADAVRAALAGLPVVVVINPDWEEgm 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446168303  86 ADSVLAGLKAA-GDAQWVLVHDAARPCLHQDDLARLLALSetSRTGGILAAPV 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 4.02e-10

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: 56.82  E-value: 4.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   10 AVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHprVKRVVIaISPGDSRFAQLPLANHPQITVVDGGDERADSV 89
Cdd:pfam12804   1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRPA--GDEVVV-VANDEEVLAALAGLGVPVVPDPDPGQGPLAGL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   90 LAGLKAAGDAQWVLVHDAARPCLHQDDLARLLAlsetsrtggilaapvrdtmkRAEPGKNAIAHTVDRNGLWHALtpqFF 169
Cdd:pfam12804  76 LAALRAAPGADAVLVLACDMPFLTPELLRRLLA--------------------AAEESGADIVVPVYDGGRGHPL---LY 132


                  ....*
gi 446168303  170 PRELL 174
Cdd:pfam12804 133 RRRLL 137
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 10-123 1.11e-08

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: 53.11  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   10 AVVPAAGFGRRMQTecPKQYLSIGNQTILEHSVYALLAHpRVKRVVIAISPGDSRFAQLpLANHPQITVVDGGDER---A 86
Cdd:TIGR03310   2 AIILAAGLSSRMGQ--NKLLLPYKGKTILEHVVDNALRL-FFDEVILVLGHEADELVAL-LANHSNITLVHNPQYAegqS 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446168303   87 DSVLAGLKAAGDAQWVLVHDAARPCLHQDDLARLLAL 123
Cdd:TIGR03310  78 SSIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLEA 114
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 10-59 6.79e-07

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: 48.61  E-value: 6.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446168303  10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNQTILEHSVYALLAHPrVKRVVIAIS 59
Cdd:COG1208    2 AVILAGGLGTRLRplTDtRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG 53
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
10-80 1.98e-06

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 47.16  E-value: 1.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446168303  10 AVVPAAGFGRRMQ---TECPKQYLSIGNQTILEHSVYALLAHpRVKRVVIAISPGDSRFAQLPLANHPQITVVD 80
Cdd:COG1213    2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAELIEEALARPGPDVTFVY 74
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 10-60 2.08e-06

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 47.19  E-value: 2.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446168303  10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNQTILEHSVYALLAHPrVKRVVIAISP 60
Cdd:cd04181    1 AVILAAGKGTRLRplTDtRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGY 53
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 10-56 2.67e-05

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: 43.76  E-value: 2.67e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446168303  10 AVVPAAGFGRRMQT---ECPKQYLSIGNQTILEHSVYALLAHpRVKRVVI 56
Cdd:cd02523    1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVI 49
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-130 2.79e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 38.38  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168303   7 DVCAVVPAAGFGRRMQTECPKQYLSIGNQTILEHSVYALLA-HPRvkRVVIAISPGDSRFAQLPLANHPQITVVD----G 81
Cdd:PRK14352   4 PTAVIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAAGlAPQ--HLVVVVGHDRERVAPAVAELAPEVDIAVqdeqP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446168303  82 GDERAdsVLAGLKAAGD--AQWVLVHDAARPCLHQDDLARLLALSETSRTG 130
Cdd:PRK14352  82 GTGHA--VQCALEALPAdfDGTVVVTAGDVPLLDGETLADLVATHTAEGNA 130
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 10-56 5.23e-03

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 36.78  E-value: 5.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446168303  10 AVVPAAGFGRRMQ--TE-CPKQYLSIGNQTILEHSVyALLAHPRVKRVVI 56
Cdd:cd06422    2 AMILAAGLGTRMRplTDtRPKPLVPVAGKPLIDHAL-DRLAAAGIRRIVV 50
 
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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