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Conserved domains on  [gi|1523775437|dbj|GCD11209|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Clostridium tagluense]

Protein Classification

IspD/TarI family cytidylyltransferase( domain architecture ID 10118526)

IspD/TarI family cytidylyltransferase such as 2-C-methyl-d-erythritol 4-phosphate cytidylyltransferase (IspD) that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-d-erythritol from 2-C-methyl-derythritol 4-phosphate and CTP, and ribitol-5-phosphate cytidylyltransferase (TarI) that catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate

EC:  2.7.7.-
Gene Ontology:  GO:0070567
PubMed:  12691742|9445404
SCOP:  4002789

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-220 4.01e-111

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: 317.54  E-value: 4.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   4 NCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREeiINKYNFFKVKAVIVGGA 83
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE--LAKYGLSKVVKIVEGGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  84 QRQDSVLNGLKALR--NCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCV 161
Cdd:cd02516    79 TRQDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1523775437 162 QTPQAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEM 220
Cdd:cd02516   159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLAL 217
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-220 4.01e-111

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: 317.54  E-value: 4.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   4 NCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREeiINKYNFFKVKAVIVGGA 83
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE--LAKYGLSKVVKIVEGGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  84 QRQDSVLNGLKALR--NCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCV 161
Cdd:cd02516    79 TRQDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1523775437 162 QTPQAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEM 220
Cdd:cd02516   159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLAL 217
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 7-230 1.29e-110

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: 316.69  E-value: 1.29e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   7 IILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREeIINKYNFFKVKAVIVGGAQRQ 86
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEE-LLAKYGIDKPVRVVAGGATRQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  87 DSVLNGLKALR-NCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCVQTPQ 165
Cdd:COG1211    80 DSVRNGLEALPdDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1523775437 166 AFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILEGSSS 230
Cdd:COG1211   160 GFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-227 1.39e-110

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 316.69  E-value: 1.39e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   1 MSRNCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREEIINKYNffKVKaVIV 80
Cdd:PRK00155    1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDP--KVT-VVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  81 GGAQRQDSVLNGLKALRNCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFC 160
Cdd:PRK00155   78 GGAERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1523775437 161 VQTPQAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILEG 227
Cdd:PRK00155  158 AQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 5-225 3.91e-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: 282.25  E-value: 3.91e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   5 CAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREEIINKYNFfkvkAVIVGGAQ 84
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVP----KIVAGGDT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  85 RQDSVLNGLKALRNCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCVQTP 164
Cdd:TIGR00453  77 RQDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1523775437 165 QAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQIL 225
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 6-226 1.02e-60

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: 189.97  E-value: 1.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   6 AIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREEIINKynffkvKAVIV-GGAQ 84
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDP------SIQLVaGGDT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  85 RQDSVLNGLKALR-NCEIVLIHDGARPFINESIIKNAILYA-NLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCVQ 162
Cdd:pfam01128  75 RQDSVLNGLKALAgTAKFVLVHDGARPCLPHADLARLLAALeTGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1523775437 163 TPQAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILE 226
Cdd:pfam01128 155 TPQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILT 218
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-220 4.01e-111

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: 317.54  E-value: 4.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   4 NCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREeiINKYNFFKVKAVIVGGA 83
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE--LAKYGLSKVVKIVEGGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  84 QRQDSVLNGLKALR--NCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCV 161
Cdd:cd02516    79 TRQDSVLNGLKALPdaDPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1523775437 162 QTPQAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEM 220
Cdd:cd02516   159 QTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLAL 217
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 7-230 1.29e-110

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: 316.69  E-value: 1.29e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   7 IILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREeIINKYNFFKVKAVIVGGAQRQ 86
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEE-LLAKYGIDKPVRVVAGGATRQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  87 DSVLNGLKALR-NCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCVQTPQ 165
Cdd:COG1211    80 DSVRNGLEALPdDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1523775437 166 AFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILEGSSS 230
Cdd:COG1211   160 GFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-227 1.39e-110

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 316.69  E-value: 1.39e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   1 MSRNCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREEIINKYNffKVKaVIV 80
Cdd:PRK00155    1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDP--KVT-VVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  81 GGAQRQDSVLNGLKALRNCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFC 160
Cdd:PRK00155   78 GGAERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1523775437 161 VQTPQAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILEG 227
Cdd:PRK00155  158 AQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 5-225 3.91e-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: 282.25  E-value: 3.91e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   5 CAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREEIINKYNFfkvkAVIVGGAQ 84
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVP----KIVAGGDT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  85 RQDSVLNGLKALRNCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCVQTP 164
Cdd:TIGR00453  77 RQDSVRNGLKALKDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1523775437 165 QAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQIL 225
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 6-226 1.02e-60

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: 189.97  E-value: 1.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   6 AIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREEIINKynffkvKAVIV-GGAQ 84
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDP------SIQLVaGGDT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  85 RQDSVLNGLKALR-NCEIVLIHDGARPFINESIIKNAILYA-NLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCVQ 162
Cdd:pfam01128  75 RQDSVLNGLKALAgTAKFVLVHDGARPCLPHADLARLLAALeTGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1523775437 163 TPQAFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILE 226
Cdd:pfam01128 155 TPQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILT 218
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 7-229 2.41e-59

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 187.25  E-value: 2.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   7 IILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIiVVVAEGEMDYCREEIINKYNffKVKAVIVGGAQRQ 86
Cdd:PLN02728   28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEI-VVVCDPSYRDVFEEAVENID--VPLKFALPGKERQ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  87 DSVLNGLKALR-NCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVDASGFSIETPDREMLFCVQTPQ 165
Cdd:PLN02728  105 DSVFNGLQEVDaNSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWEMQTPQ 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1523775437 166 AFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILEGSS 229
Cdd:PLN02728  185 VIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERS 248
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-220 3.22e-55

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 180.43  E-value: 3.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   1 MSRNCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCReeiiNKYNFFKVKAVIV 80
Cdd:PRK09382    3 MSDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMK----KALPEIKFVTLVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  81 GGAQRQDSVLNGLKALRNcEIVLIHDGARPFINESIIKNAIlyANLygATACGVKPkdTIKIVDASGFSIETPDREMLFC 160
Cdd:PRK09382   79 GGATRQESVRNALEALDS-EYVLIHDAARPFVPKELIDRLI--EAL--DKADCVLP--ALPVADTLKRANETVDREGLKL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437 161 VQTPQAFKYDLILKchMKINEEDIrvTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEM 220
Cdd:PRK09382  152 IQTPQLSRTKTLKA--AADGRGDF--TDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKM 207
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 7-227 2.33e-53

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 171.59  E-value: 2.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   7 IILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCrEEIINKYNFFKVKAVIV-GGAQR 85
Cdd:PRK13385    6 IFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHV-QDLMKQLNVADQRVEVVkGGTER 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437  86 QDSVLNGLKALRNCEIVLIHDGARPFINESIIKNAILYANLYGATACGVKPKDTIKIVdASGFSIETPDREMLFCVQTPQ 165
Cdd:PRK13385   85 QESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRV-KDKQVIETVDRNELWQGQTPQ 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1523775437 166 AFKYDLILKCHMKINEEDIRVTDDTMVVERYGNRVYLYEGSYNNIKITTPEDLEMGKQILEG 227
Cdd:PRK13385  164 AFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQG 225
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-118 5.64e-15

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 70.57  E-value: 5.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   1 MSRNCAIILAAGKGTRMGQsiNKQYLKINKHPILYYTLKAFTQCDCiDEIIVVVAegemdYCREEIINKYNFFKVKAVIV 80
Cdd:COG2068     1 MSKVAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAGL-DPVVVVLG-----ADAEEVAAALAGLGVRVVVN 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1523775437  81 GGAQRQ--DSVLNGLKALRN-CEIVLIHDGARPFINESIIK 118
Cdd:COG2068    73 PDWEEGmsSSLRAGLAALPAdADAVLVLLGDQPLVTAETLR 113
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 6-117 1.80e-11

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: 60.82  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   6 AIILAAGKGTRMGQsiNKQYLKINKHPILYYTLKAFTQCDCiDEIIVVVAEgEMDYCREEIINKYNffkVKAVIVGGAQR 85
Cdd:TIGR03310   2 AIILAAGLSSRMGQ--NKLLLPYKGKTILEHVVDNALRLFF-DEVILVLGH-EADELVALLANHSN---ITLVHNPQYAE 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1523775437  86 --QDSVLNGLKALRNCEIVLIHDGARPFINESII 117
Cdd:TIGR03310  75 gqSSSIKLGLELPVQSDGYLFLLGDQPFVTPDII 108
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 5-118 2.13e-10

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: 57.96  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   5 CAIILAAGKGTRMGQsiNKQYLKINKHPILYYTLKAFTQCDCiDEIIVVVAEGEmdycrEEIINKYNFFKVKAVIVGGAQ 84
Cdd:cd04182     2 AAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGL-SRVIVVLGAEA-----DAVRAALAGLPVVVVINPDWE 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1523775437  85 RQ--DSVLNGLKALRN-CEIVLIHDGARPFINESIIK 118
Cdd:cd04182    74 EGmsSSLAAGLEALPAdADAVLILLADQPLVTAETLR 110
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-104 8.19e-09

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: 52.97  E-value: 8.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   6 AIILAAGKGTRMGQsiNKQYLKINKHPILYYTLKAFTQcdCIDEIIVVVAegemdycREEIINKYNFFKVKaVIVGGAQR 85
Cdd:pfam12804   1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERLRP--AGDEVVVVAN-------DEEVLAALAGLGVP-VVPDPDPG 68

                          90       100
                  ....*....|....*....|..
gi 1523775437  86 Q---DSVLNGLKALRNCEIVLI 104
Cdd:pfam12804  69 QgplAGLLAALRAAPGADAVLV 90
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-112 1.31e-08

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: 53.35  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVaegemDYCREEIINKYNF---FKVKAVI 79
Cdd:cd04181     1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVV-----GYLGEQIEEYFGDgskFGVNIEY 74

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1523775437  80 VggaqRQDSVLNGLKALRNCEIVLIHDgarPFI 112
Cdd:cd04181    75 V----VQEEPLGTAGAVRNAEDFLGDD---DFL 100
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-54 1.87e-08

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: 53.01  E-value: 1.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVV 54
Cdd:cd02523     1 AIILAAGRGSRLRpltEDRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVT 51
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-80 3.96e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 52.17  E-value: 3.96e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVaeGemdYCREEIINKYNFFKVKAVIV 80
Cdd:COG1213     2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVVVT--G---YKAELIEEALARPGPDVTFV 73
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 6-68 1.03e-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: 50.92  E-value: 1.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVAegemdYCREEIIN 68
Cdd:COG1208     2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG-----YLAEQIEE 61
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-58 1.61e-06

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: 46.72  E-value: 1.61e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1523775437   1 MSRNC-AIILAAGKGTRMGQsiNKQYLKINKHPILYYTLKAFTQcdCIDEIIVVVAEGE 58
Cdd:COG0746     1 MTMPItGVILAGGRSRRMGQ--DKALLPLGGRPLLERVLERLRP--QVDEVVIVANRPE 55
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-64 6.95e-06

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 45.64  E-value: 6.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVAEGEMDYCRE 64
Cdd:cd02538     3 GIILAGGSGTRLYpltKVVSKQLLPVYDKPMIYYPLSTLMLAG-IREILIISTPEDLPLFKE 63
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-58 8.72e-06

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 45.25  E-value: 8.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVAEGE 58
Cdd:cd04189     3 GLILAGGKGTRLRpltYTRPKQLIPVAGKPIIQYAIEDLREAG-IEDIGIVVGPTG 57
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-131 9.28e-06

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 45.20  E-value: 9.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   6 AIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCdCIDEIIVVVAEGemdycREEIINKYNFFKVKAVIvggaQR 85
Cdd:cd02540     1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHG-----AEQVKKALANPNVEFVL----QE 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1523775437  86 Q-----DSVLNGLKALRN-CEIVLIHDGARPFINESIIKNAILYANLYGATA 131
Cdd:cd02540    71 EqlgtgHAVKQALPALKDfEGDVLVLYGDVPLITPETLQRLLEAHREAGADV 122
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-57 1.32e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 45.24  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1523775437   1 MSRNC-AIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDCiDEIIVVVAEG 57
Cdd:PRK14353    2 TDRTClAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGP-SRVAVVVGPG 58
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-54 1.50e-05

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 44.70  E-value: 1.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKI-NKhPILYY---TLKAFTqcdcIDEIIVVV 54
Cdd:COG1209     3 GIILAGGSGTRLRpltLTVSKQLLPVyDK-PMIYYplsTLMLAG----IREILIIS 53
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-66 2.85e-05

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: 43.33  E-value: 2.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1523775437   6 AIILAAGKGTRMGQsiNKQYLKINKHPILYYTLKAFTQcdCIDEIIVVVAEGEMDYCREEI 66
Cdd:cd02503     3 GVILAGGKSRRMGG--DKALLELGGKPLLEHVLERLKP--LVDEVVISANRDQERYALLGV 59
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-54 5.38e-05

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 43.48  E-value: 5.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1523775437   5 CAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVV 54
Cdd:COG1207     4 AVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAARALG-PDRIVVVV 52
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-57 6.25e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.17  E-value: 6.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1523775437   1 MSRNCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCdCIDEIIVVVAEG 57
Cdd:PRK14356    3 ASTTGALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALRPL-FGDNVWTVVGHR 58
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-56 6.98e-05

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 42.63  E-value: 6.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1523775437   6 AIILAAGKGTR-----MGQSiNKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVAE 56
Cdd:pfam00483   2 AIILAGGSGTRlwpltRTLA-KPLVPVGGKYPLIDYPLSRLANAG-IREIIVILTQ 55
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 6-80 2.95e-04

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 40.72  E-value: 2.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1523775437   6 AIILAAGKGTRMG---QSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVAEGEMDYCREEIINKYNFFKVKAVIV 80
Cdd:cd04198     3 AVILAGGGGSRLYpltDNIPKALLPVANKPMIWYPLDWLEKAG-FEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEV 79
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-57 4.79e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.59  E-value: 4.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1523775437   3 RNCAIILAAGKGTRMGQSINKQYLKINKHPILYYTLKAFTQCDcIDEIIVVVAEG 57
Cdd:PRK14354    2 NRYAIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVKKAG-IDKIVTVVGHG 55
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-39 7.65e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.97  E-value: 7.65e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1523775437   7 IILAAGKGTRMGQSINKQYLKINKHPILYYTLK 39
Cdd:PRK14359    6 IILAAGKGTRMKSSLPKVLHTICGKPMLFYILK 38
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 9-54 1.77e-03

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 37.95  E-value: 1.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1523775437   9 LAAGKGTRMGqSINKQYLKINKHPILYYTLKAFTQCdCIDEIIVVV 54
Cdd:COG2266     1 MAGGKGTRLG-GGEKPLLEICGKPMIDRVIDALEES-CIDKIYVAV 44
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 6-123 6.94e-03

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 36.55  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1523775437   6 AIILAAGKGTRMgqsINKQYLKINKHPILYYTLKAFTQCDCIDEIIVVVAEGEMDYCREEIINKYNFFKVKAVIVggaqr 85
Cdd:pfam02348   2 AIIPARLGSKRL---PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSG----- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1523775437  86 QDSVLNGLKALRN--CEIVLIHDGARPFINESIIKNAILY 123
Cdd:pfam02348  74 TDRFYEVVKAFLNdhDDIIVNIQGDNPLLQPEVILKAIET 113
 
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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