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Conserved domains on  [gi|2035185386|ref|WP_211430787|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Chloracidobacterium aggregatum]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10003116)

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 COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-228 5.97e-94

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: 274.31  E-value: 5.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   6 IVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLETFPVEKPITAVAGGAERQE 85
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  86 SVRLALAAVPDAASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLV-QDGLAYETPPRSTLYAVQTPQA 164
Cdd:COG1211    81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVdDDGRVTETVDRSGLWAAQTPQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035185386 165 FETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFLWQRLAR 228
Cdd:COG1211   161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
 
Name Accession Description Interval E-value
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-228 5.97e-94

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: 274.31  E-value: 5.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   6 IVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLETFPVEKPITAVAGGAERQE 85
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  86 SVRLALAAVPDAASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLV-QDGLAYETPPRSTLYAVQTPQA 164
Cdd:COG1211    81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVdDDGRVTETVDRSGLWAAQTPQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035185386 165 FETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFLWQRLAR 228
Cdd:COG1211   161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-225 1.68e-89

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 263.15  E-value: 1.68e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLetFPVEKPITAVAGGAER 83
Cdd:PRK00155    5 YAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELL--LAKDPKVTVVAGGAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  84 QESVRLALAAVPDAaSVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLV-QDGLAYETPPRSTLYAVQTP 162
Cdd:PRK00155   83 QDSVLNGLQALPDD-DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSdDGGGIVDTPDRSGLWAAQTP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035185386 163 QAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFLWQR 225
Cdd:PRK00155  162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-219 1.67e-84

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: 250.13  E-value: 1.67e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFdALLETFPVEKPITAVAGGAER 83
Cdd:cd02516     2 AAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLA-KELAKYGLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  84 QESVRLALAAVPDA-ASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLV-QDGLAYETPPRSTLYAVQT 161
Cdd:cd02516    81 QDSVLNGLKALPDAdPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVdDDGVVVETLDREKLWAAQT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2035185386 162 PQAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLA 219
Cdd:cd02516   161 PQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 4-222 2.25e-69

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: 211.76  E-value: 2.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLetfPVEKPITAVAGGAER 83
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYL---VARAVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  84 QESVRLALAAVPDAaSVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLVQ-DGLAYETPPRSTLYAVQTP 162
Cdd:TIGR00453  78 QDSVRNGLKALKDA-EFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEaDGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386 163 QAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFL 222
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEAL 216
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 5-225 1.71e-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: 184.19  E-value: 1.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLetfpVEKPITAVAGGAERQ 84
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL----GDPSIQLVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  85 ESVRLALAAVPDAASVVVVHDAVRPF-ATTELITATIAAARADRAAVVGHPATDTIKLVQ-DGLAYETPPRSTLYAVQTP 162
Cdd:pfam01128  77 DSVLNGLKALAGTAKFVLVHDGARPClPHADLARLLAALETGTQGAILALPVTDTIKRVEaDGVVAGTPDRSGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035185386 163 QAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFLWQR 225
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
 
Name Accession Description Interval E-value
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-228 5.97e-94

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: 274.31  E-value: 5.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   6 IVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLETFPVEKPITAVAGGAERQE 85
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  86 SVRLALAAVPDAASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLV-QDGLAYETPPRSTLYAVQTPQA 164
Cdd:COG1211    81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVdDDGRVTETVDRSGLWAAQTPQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035185386 165 FETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFLWQRLAR 228
Cdd:COG1211   161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
4-225 1.68e-89

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 263.15  E-value: 1.68e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLetFPVEKPITAVAGGAER 83
Cdd:PRK00155    5 YAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELL--LAKDPKVTVVAGGAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  84 QESVRLALAAVPDAaSVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLV-QDGLAYETPPRSTLYAVQTP 162
Cdd:PRK00155   83 QDSVLNGLQALPDD-DWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSdDGGGIVDTPDRSGLWAAQTP 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035185386 163 QAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFLWQR 225
Cdd:PRK00155  162 QGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-219 1.67e-84

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: 250.13  E-value: 1.67e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFdALLETFPVEKPITAVAGGAER 83
Cdd:cd02516     2 AAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLA-KELAKYGLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  84 QESVRLALAAVPDA-ASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLV-QDGLAYETPPRSTLYAVQT 161
Cdd:cd02516    81 QDSVLNGLKALPDAdPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVdDDGVVVETLDREKLWAAQT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2035185386 162 PQAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLA 219
Cdd:cd02516   161 PQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 4-222 2.25e-69

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: 211.76  E-value: 2.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLetfPVEKPITAVAGGAER 83
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYL---VARAVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  84 QESVRLALAAVPDAaSVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLVQ-DGLAYETPPRSTLYAVQTP 162
Cdd:TIGR00453  78 QDSVRNGLKALKDA-EFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEaDGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386 163 QAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFL 222
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEAL 216
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 5-225 1.71e-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: 184.19  E-value: 1.71e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLetfpVEKPITAVAGGAERQ 84
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL----GDPSIQLVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  85 ESVRLALAAVPDAASVVVVHDAVRPF-ATTELITATIAAARADRAAVVGHPATDTIKLVQ-DGLAYETPPRSTLYAVQTP 162
Cdd:pfam01128  77 DSVLNGLKALAGTAKFVLVHDGARPClPHADLARLLAALETGTQGAILALPVTDTIKRVEaDGVVAGTPDRSGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035185386 163 QAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFLWQR 225
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-219 7.78e-53

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 170.05  E-value: 7.78e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   1 MTAVAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLETFPV-EKPITAVAG 79
Cdd:PRK13385    1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVaDQRVEVVKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  80 GAERQESVRLALAAVpDAASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLVQDGLAYETPPRSTLYAV 159
Cdd:PRK13385   81 GTERQESVAAGLDRI-GNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVDRNELWQG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386 160 QTPQAFETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLA 219
Cdd:PRK13385  160 QTPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLA 219
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 6-220 2.88e-46

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 154.12  E-value: 2.88e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   6 IVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLEtfPVEKPITAVAGGAERQE 85
Cdd:PLN02728   28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVE--NIDVPLKFALPGKERQD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  86 SVRLALAAVPDAASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKLVQDGLAY-ETPPRSTLYAVQTPQA 164
Cdd:PLN02728  106 SVFNGLQEVDANSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVvKTLDRKRLWEMQTPQV 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2035185386 165 FETGLLRDAHARAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLAD 220
Cdd:PLN02728  186 IKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAE 241
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-222 1.16e-41

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: 145.38  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   1 MTAVAIVPAGGLGARFGADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLETFpveKPITAVAGG 80
Cdd:PRK09382    4 SDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI---KFVTLVTGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386  81 AERQESVRLALAAVpdAASVVVVHDAVRPFATTELITATIAAARADRAAVVGHPATDTIKlvqdgLAYETPPRSTLYAVQ 160
Cdd:PRK09382   81 ATRQESVRNALEAL--DSEYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLK-----RANETVDREGLKLIQ 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035185386 161 TPQAFETGLLRdahaRAAAEQVTATDDAMLVERLGVPVRIVPGPRWNLKITHPDDLPLADFL 222
Cdd:PRK09382  154 TPQLSRTKTLK----AAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLL 211
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-104 3.79e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 57.48  E-value: 3.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   1 MTAVAIVPAGGLGARFGadRPKQFLELAGCPIIIHTLRRLAACPdASHIVVALPPTARPVfDALLETFPVEkpiTAVAGG 80
Cdd:COG2068     2 SKVAAIILAAGASSRMG--RPKLLLPLGGKPLLERAVEAALAAG-LDPVVVVLGADAEEV-AAALAGLGVR---VVVNPD 74

                          90       100
                  ....*....|....*....|....*.
gi 2035185386  81 AERQ--ESVRLALAAVPDAASVVVVH 104
Cdd:COG2068    75 WEEGmsSSLRAGLAALPADADAVLVL 100
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 4-103 1.64e-08

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 52.56  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGadRPKQFLELAGCPIIIHTLRRLAACPdASHIVVALPPTARPVfDALLETFPVekpITAVAGGAER 83
Cdd:cd04182     2 AAIILAAGRSSRMG--GNKLLLPLDGKPLLRHALDAALAAG-LSRVIVVLGAEADAV-RAALAGLPV---VVVINPDWEE 74

                          90       100
                  ....*....|....*....|..
gi 2035185386  84 Q--ESVRLALAAVPDAASVVVV 103
Cdd:cd04182    75 GmsSSLAAGLEALPADADAVLI 96
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-103 1.18e-07

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 49.89  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFGadRPKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDALLETFPVEKPITAVAGGaerq 84
Cdd:pfam12804   1 AVILAGGRSSRMG--GDKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLAALAGLGVPVVPDPDPGQGPLAG---- 74

                          90
                  ....*....|....*....
gi 2035185386  85 esVRLALAAVPDAASVVVV 103
Cdd:pfam12804  75 --LLAALRAAPGADAVLVL 91
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 5-53 2.53e-06

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 46.68  E-value: 2.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2035185386   5 AIVPAGGLGARFG---ADRPKQFLELAGCPIIIHTLRRLAACpDASHIVVAL 53
Cdd:COG1208     2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINV 52
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-75 4.64e-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: 46.03  E-value: 4.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035185386   5 AIVPAGGLGARFG---ADRPKQFLELAGCPIIIHTLRRLAACpDASHIVVALPPTARPVFDALLETFPVEKPIT 75
Cdd:cd04181     1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGYLGEQIEEYFGDGSKFGVNIE 73
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-51 1.01e-05

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 45.23  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFG---ADRPKQFLELAGCPIIIHTLRRLAACpDASHIVV 51
Cdd:COG1213     2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVV 50
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-51 1.09e-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: 44.92  E-value: 1.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFGA---DRPKQFLELAGCPIIIHTLRRLAACpDASHIVV 51
Cdd:cd02523     1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVI 49
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
4-80 9.12e-05

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 41.94  E-value: 9.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   4 VAIVPAGGLGARFGADrpKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDA----LLETFPVEKPITAVAG 79
Cdd:PRK02726    9 VALILAGGKSSRMGQD--KALLPWQGVPLLQRVARIAAACADEVYIITPWPERYQSLLPPgchwLREPPPSQGPLVAFAQ 86


                  .
gi 2035185386  80 G 80
Cdd:PRK02726   87 G 87
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
4-51 1.29e-04

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 42.36  E-value: 1.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2035185386   4 VAIVPAGGLGARF----GADRPKQFLELAGC-PIIIHTLRRLAACPDASHIVV 51
Cdd:COG0836     4 YPVILAGGSGTRLwplsRESYPKQFLPLLGEkSLLQQTVERLAGLVPPENILV 56
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-58 3.41e-04

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 40.18  E-value: 3.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2035185386   1 MTAVAIVPAGGLGARFGADrpKQFLELAGCPIIIHTLRRLAacPDASHIVVALPPTAR 58
Cdd:COG0746     3 MPITGVILAGGRSRRMGQD--KALLPLGGRPLLERVLERLR--PQVDEVVIVANRPER 56
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 4-52 4.14e-04

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 40.64  E-value: 4.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2035185386   4 VAIVPAGGLGARF----GADRPKQFLELAGC-PIIIHTLRRLAACPDASHIVVA 52
Cdd:cd02509     2 YPVILAGGSGTRLwplsRESYPKQFLKLFGDkSLLQQTLDRLKGLVPPDRILVV 55
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 6-53 4.52e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 40.31  E-value: 4.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2035185386   6 IVPAGGLGARF---GADRPKQFLELAGCPIIIHTLRRLAACPDASHIVVAL 53
Cdd:cd04183     2 IIPMAGLGSRFkkaGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICR 52
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 5-109 9.12e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 39.01  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFGAdRPKQFLELAGCPIIIHTLRRLAacPDASHIVV-------ALPPTARPVFDALLETFPveKPITAV 77
Cdd:PRK00317    6 GVILAGGRSRRMGG-VDKGLQELNGKPLIQHVIERLA--PQVDEIVInanrnlaRYAAFGLPVIPDSLADFP--GPLAGI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2035185386  78 AGGAERQES------------------VRLALAAVPDAASVVVVHDAVRP 109
Cdd:PRK00317   81 LAGLKQARTewvlvvpcdtpfippdlvARLAQAAGKDDADVAWAHDGGRL 130
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 4-52 1.81e-03

SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.


Pssm-ID: 133011  Cd Length: 233  Bit Score: 38.32  E-value: 1.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2035185386   4 VAIVpagglGARFGADR-P-KQFLELAGCPIIIHTLRRLAACPDASHIVVA 52
Cdd:cd02518     1 VAII-----QARMGSTRlPgKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIA 46
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 5-94 2.09e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 37.94  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFGADrpKQFLELAGCPIIIHTLRRLAACPDASHIVVALPPTARPVFDA--LLETFPVEKPITAVAGGAE 82
Cdd:cd02503     3 GVILAGGKSRRMGGD--KALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYALLGVpvIPDEPPGKGPLAGILAALR 80

                          90
                  ....*....|..
gi 2035185386  83 RQESVRLALAAV 94
Cdd:cd02503    81 AAPADWVLVLAC 92
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-51 3.81e-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: 37.17  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2035185386   5 AIVPAGGLGARFG---ADRPKQFLELAGCPIIIHTLRRLAACPdASHIVV 51
Cdd:cd06422     2 AMILAAGLGTRMRpltDTRPKPLVPVAGKPLIDHALDRLAAAG-IRRIVV 50
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-52 4.34e-03

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 37.25  E-value: 4.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2035185386   1 MTAVAIVPAgglgaRFGADR-P-KQFLELAGCPIIIHTLRRLAACPDASHIVVA 52
Cdd:PRK13368    1 MKVVVVIPA-----RYGSSRlPgKPLLDILGKPMIQHVYERAAQAAGVEEVYVA 49
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 4-52 7.41e-03

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 36.68  E-value: 7.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2035185386   4 VAIVPAgglgaRFGADR-P-KQFLELAGCPIIIHTLRRLAACPDASHIVVA 52
Cdd:cd02517     3 IVVIPA-----RYASSRlPgKPLADIAGKPMIQHVYERAKKAKGLDEVVVA 48
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-53 9.62e-03

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 35.99  E-value: 9.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2035185386   5 AIVPAGGLGARFGA---DRPKQFLELAGCPIIIHTLRRLAAcPDASHIVVAL 53
Cdd:cd06915     1 AVILAGGLGTRLRSvvkDLPKPLAPVAGRPFLEYLLEYLAR-QGISRIVLSV 51
 
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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