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Conserved domains on  [gi|446561133|ref|WP_000638479|]
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MULTISPECIES: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Staphylococcus]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10793796)

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
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-238 2.33e-129

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


:

Pssm-ID: 184017  Cd Length: 230  Bit Score: 364.58  E-value: 2.33e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   1 MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNITDQRVKVVAG 80
Cdd:PRK13385   1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  81 GTDRNETIMNIIDYirnvngINNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPvR 160
Cdd:PRK13385  81 GTERQESVAAGLDR------IGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVD-R 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133 161 NEMYQGQTPQSFNIKLLQDSYRaLSSAQKEILSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD 238
Cdd:PRK13385 154 NELWQGQTPQAFELKILQKAHR-LASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQGDIADD 230
 
Name Accession Description Interval E-value
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-238 2.33e-129

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 364.58  E-value: 2.33e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   1 MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNITDQRVKVVAG 80
Cdd:PRK13385   1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  81 GTDRNETIMNIIDYirnvngINNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPvR 160
Cdd:PRK13385  81 GTERQESVAAGLDR------IGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVD-R 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133 161 NEMYQGQTPQSFNIKLLQDSYRaLSSAQKEILSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD 238
Cdd:PRK13385 154 NELWQGQTPQAFELKILQKAHR-LASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQGDIADD 230
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-233 2.25e-78

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: 235.02  E-value: 2.25e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGNvPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNItDQRVKVVAGGTDRN 85
Cdd:COG1211    2 IPAAGSGSRMGA-GIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGI-DKPVRVVAGGATRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  86 ETIMNIIDYIRNvnginNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQ 165
Cdd:COG1211   80 DSVRNGLEALPD-----DDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133 166 GQTPQSFNIKLLQDSYRALSSAQKEIlSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAIIQG 233
Cdd:COG1211  155 AQTPQGFRLDLLLEAHEAAAADGLEF-TDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 2-227 1.28e-73

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: 222.78  E-value: 1.28e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   2 IYAGILAGGIGSRMGNvPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNitDQRVKVVAGG 81
Cdd:cd02516    1 VAAIILAAGSGSRMGA-DIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGL--SKVVKIVEGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  82 TDRNETIMNIIDYIRNvngiNNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRN 161
Cdd:cd02516   78 ATRQDSVLNGLKALPD----ADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446561133 162 EMYQGQTPQSFNIKLLQDSYRALsSAQKEILSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVA 227
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQA-SEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-230 1.96e-46

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: 153.60  E-value: 1.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133    6 ILAGGIGSRMGnVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYnitdQRVKVVAGGTDRN 85
Cdd:TIGR00453   4 IPAAGRGTRFG-SGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVAR----AVPKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   86 ETIMNIIDYIRNVnginndDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQ 165
Cdd:TIGR00453  79 DSVRNGLKALKDA------EFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWA 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446561133  166 GQTPQSFNIKLLQDSYRALSSAQKEILSDAckIIVE-SGHPVKLVRGELYNIKVTTPYDLKVANAI 230
Cdd:TIGR00453 153 AQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEkLGGKVQLVEGDALNFKITTPEDLALAEAL 216
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 6-231 4.53e-39

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: 134.50  E-value: 4.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133    6 ILAGGIGSRMGnVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILkkyniTDQRVKVVAGGTDRN 85
Cdd:pfam01128   3 IPAAGSGKRMG-AGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL-----GDPSIQLVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   86 ETIMNIIdyirnvNGINNDDVIV-THDAVRPFLTQRIIKENIEVAEK-YGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEM 163
Cdd:pfam01128  77 DSVLNGL------KALAGTAKFVlVHDGARPCLPHADLARLLAALETgTQGAILALPVTDTIKRVEADGVVAGTPDRSGL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133  164 YQGQTPQSFNIKLLQDSYRALSSAQKEILSDAcKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAII 231
Cdd:pfam01128 151 WAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA-SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
 
Name Accession Description Interval E-value
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-238 2.33e-129

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 364.58  E-value: 2.33e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   1 MIYAGILAGGIGSRMGNVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNITDQRVKVVAG 80
Cdd:PRK13385   1 MNYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRVEVVKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  81 GTDRNETIMNIIDYirnvngINNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPvR 160
Cdd:PRK13385  81 GTERQESVAAGLDR------IGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVD-R 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133 161 NEMYQGQTPQSFNIKLLQDSYRaLSSAQKEILSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAIIQGDIADD 238
Cdd:PRK13385 154 NELWQGQTPQAFELKILQKAHR-LASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQGDIADD 230
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-233 2.24e-94

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 275.86  E-value: 2.24e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   1 MIYAGILAGGIGSRMGnVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYnitDQRVKVVAG 80
Cdd:PRK00155   3 MVYAIIPAAGKGSRMG-ADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK---DPKVTVVAG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  81 GTDRNETIMNIIdyirnvNGINNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVR 160
Cdd:PRK00155  79 GAERQDSVLNGL------QALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446561133 161 NEMYQGQTPQSFNIKLLQDSYRALSSAQKEILSDACKiiVES-GHPVKLVRGELYNIKVTTPYDLKVANAIIQG 233
Cdd:PRK00155 153 SGLWAAQTPQGFRIELLREALARALAEGKTITDDASA--VERlGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-233 2.25e-78

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: 235.02  E-value: 2.25e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGNvPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNItDQRVKVVAGGTDRN 85
Cdd:COG1211    2 IPAAGSGSRMGA-GIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGI-DKPVRVVAGGATRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  86 ETIMNIIDYIRNvnginNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQ 165
Cdd:COG1211   80 DSVRNGLEALPD-----DDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133 166 GQTPQSFNIKLLQDSYRALSSAQKEIlSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAIIQG 233
Cdd:COG1211  155 AQTPQGFRLDLLLEAHEAAAADGLEF-TDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 2-227 1.28e-73

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: 222.78  E-value: 1.28e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   2 IYAGILAGGIGSRMGNvPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNitDQRVKVVAGG 81
Cdd:cd02516    1 VAAIILAAGSGSRMGA-DIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGL--SKVVKIVEGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  82 TDRNETIMNIIDYIRNvngiNNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRN 161
Cdd:cd02516   78 ATRQDSVLNGLKALPD----ADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDRE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446561133 162 EMYQGQTPQSFNIKLLQDSYRALsSAQKEILSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVA 227
Cdd:cd02516  154 KLWAAQTPQAFRLDLLLKAHRQA-SEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-230 1.96e-46

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: 153.60  E-value: 1.96e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133    6 ILAGGIGSRMGnVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYnitdQRVKVVAGGTDRN 85
Cdd:TIGR00453   4 IPAAGRGTRFG-SGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVAR----AVPKIVAGGDTRQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   86 ETIMNIIDYIRNVnginndDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQ 165
Cdd:TIGR00453  79 DSVRNGLKALKDA------EFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWA 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446561133  166 GQTPQSFNIKLLQDSYRALSSAQKEILSDAckIIVE-SGHPVKLVRGELYNIKVTTPYDLKVANAI 230
Cdd:TIGR00453 153 AQTPQAFRTELLKKALARAKLEGFEITDDA--SAVEkLGGKVQLVEGDALNFKITTPEDLALAEAL 216
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 6-231 4.53e-39

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: 134.50  E-value: 4.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133    6 ILAGGIGSRMGnVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILkkyniTDQRVKVVAGGTDRN 85
Cdd:pfam01128   3 IPAAGSGKRMG-AGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLL-----GDPSIQLVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   86 ETIMNIIdyirnvNGINNDDVIV-THDAVRPFLTQRIIKENIEVAEK-YGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEM 163
Cdd:pfam01128  77 DSVLNGL------KALAGTAKFVlVHDGARPCLPHADLARLLAALETgTQGAILALPVTDTIKRVEADGVVAGTPDRSGL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133  164 YQGQTPQSFNIKLLQDSYRALSSAQKEILSDAcKIIVESGHPVKLVRGELYNIKVTTPYDLKVANAII 231
Cdd:pfam01128 151 WAAQTPQGFRVDLLLAAHQRGDQPGAEITDDA-SLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 6-232 1.76e-28

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 107.90  E-value: 1.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGnVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYNItdqRVKVVAGGTDRN 85
Cdd:PLN02728  29 LLAGGVGKRMG-ANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENIDV---PLKFALPGKERQ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  86 ETIMNIIDYIRNvnginNDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNIHSIPVRNEMYQ 165
Cdd:PLN02728 105 DSVFNGLQEVDA-----NSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWE 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446561133 166 GQTPQSFNIKLLQDSYRALSSAQKEILSDACkiIVES-GHPVKLVRGELYNIKVTTPYDLKVANAIIQ 232
Cdd:PLN02728 180 MQTPQVIKPELLRRGFELVEREGLEVTDDVS--IVEAlKHPVFITEGSYTNIKVTTPDDMLVAERILN 245
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 6-229 2.56e-26

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: 104.54  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGnVPLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQDILKKYnitdQRVKVVAGGTDRN 85
Cdd:PRK09382  10 IVAAGRSTRFS-AEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI----KFVTLVTGGATRQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  86 ETIMNIIDYIRnvnginnDDVIVTHDAVRPFLTQRIIKENIEVAEKYGAVDTVIEAIDTIVMSKDKQNihsipvRNEMYQ 165
Cdd:PRK09382  85 ESVRNALEALD-------SEYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKRANETVD------REGLKL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446561133 166 GQTPQSFNIKLLQdsyRALSSaqKEILSDACKIIVESGHPVKLVRGELYNIKVTTPYDLKVANA 229
Cdd:PRK09382 152 IQTPQLSRTKTLK---AAADG--RGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADL 210
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-71 4.59e-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: 47.96  E-value: 4.59e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446561133    6 ILAGGIGSRMGnvpLPKQFLDIDNKPILIHTIEkfILVSEFNEIIIATPAqwiSHTQDILKKYNIT 71
Cdd:pfam12804   3 ILAGGRSSRMG---GDKALLPLGGKPLLERVLE--RLRPAGDEVVVVAND---EEVLAALAGLGVP 60
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-56 6.01e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 48.23  E-value: 6.01e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446561133   1 MIYAGILAGGIGSRMGnvpLPKQFLDIDNKPILIHTIEKFiLVSEFNEIIIATPAQ 56
Cdd:COG2068    3 KVAAIILAAGASSRMG---RPKLLLPLGGKPLLERAVEAA-LAAGLDPVVVVLGAD 54
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-56 8.85e-07

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: 47.55  E-value: 8.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446561133   6 ILAGGIGSRMGnvpLPKQFLDIDNKPILIHTIEKFiLVSEFNEIIIATPAQ 56
Cdd:cd04182    5 ILAAGRSSRMG---GNKLLLPLDGKPLLRHALDAA-LAAGLSRVIVVLGAE 51
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 2-70 1.24e-06

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: 47.96  E-value: 1.24e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446561133   2 IYAGILAGGIGSRMGnvPL-----PKQFLDI-DNKPILIHTIEKFILVSEFNEIIIATPAQWISHTQD----ILKKYNI 70
Cdd:cd02509    1 IYPVILAGGSGTRLW--PLsresyPKQFLKLfGDKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREqlpeGLPEENI 77
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-51 2.10e-06

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 46.72  E-value: 2.10e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446561133   1 MIYAGILAGGIGSRMGNVplPKQFLDIDNKPILIHTIEKfiLVSEFNEIII 51
Cdd:PRK00317   3 PITGVILAGGRSRRMGGV--DKGLQELNGKPLIQHVIER--LAPQVDEIVI 49
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-53 4.04e-06

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 46.98  E-value: 4.04e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446561133   1 MIYAGILAGGIGSRMGnvPL-----PKQFLDI-DNKPILIHTIEKFILVSEFNEIIIAT 53
Cdd:COG0836    2 MIYPVILAGGSGTRLW--PLsresyPKQFLPLlGEKSLLQQTVERLAGLVPPENILVVT 58
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 6-53 4.08e-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: 46.30  E-value: 4.08e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446561133   6 ILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEkfILVSE-FNEIIIAT 53
Cdd:COG1208    4 ILAGGLGTRLR--PLtdtrPKPLLPVGGKPLLEHILE--RLAAAgITEIVINV 52
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 2-54 4.11e-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: 45.95  E-value: 4.11e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446561133   2 IYAGILAGGIGSRMGNvplPKQFLDIDNKPILIHTIEKFILVseFNEIIIATP 54
Cdd:COG0746    5 ITGVILAGGRSRRMGQ---DKALLPLGGRPLLERVLERLRPQ--VDEVVIVAN 52
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-53 1.45e-05

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 44.85  E-value: 1.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGNV--PLPKQFLDIDNKPILIHTIEKFILVSeFNEIIIAT 53
Cdd:COG1213    4 ILAAGRGSRLGPLtdDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVVVT 52
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-53 1.88e-05

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: 44.11  E-value: 1.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446561133   6 ILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEKFILVSeFNEIIIAT 53
Cdd:cd04181    3 ILAAGKGTRLR--PLtdtrPKPLLPIAGKPILEYIIERLARAG-IDEIILVV 51
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 2-53 2.94e-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: 2.94e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446561133   2 IYAGILAGGIGSRMGNvplPKQFLDIDNKPILIHTIEKFILVseFNEIIIAT 53
Cdd:cd02503    1 ITGVILAGGKSRRMGG---DKALLELGGKPLLEHVLERLKPL--VDEVVISA 47
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-68 5.78e-05

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 42.94  E-value: 5.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446561133   6 ILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEKFILVSeFNEIIIAtpaqwISHTQDILKKY 68
Cdd:cd04189    5 ILAGGKGTRLR--PLtytrPKQLIPVAGKPIIQYAIEDLREAG-IEDIGIV-----VGPTGEEIKEA 63
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 11-114 4.11e-04

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 40.33  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  11 IGSRMGNVPLP-KQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWIshtQDILKKYNItdqrvKVVA------GGTD 83
Cdd:PRK13368   7 IPARYGSSRLPgKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRI---EDAVEAFGG-----KVVMtsddhlSGTD 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446561133  84 RNETIMNII--DYIRNVNGinnDDVIVTHDAVR 114
Cdd:PRK13368  79 RLAEVMLKIeaDIYINVQG---DEPMIRPRDID 108
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 6-68 4.68e-04

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 40.27  E-value: 4.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446561133   6 ILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEKFILVSeFNEIIIAtpaqwISHTQDILKKY 68
Cdd:cd06425    5 ILVGGYGTRLR--PLtltvPKPLVEFCNKPMIEHQIEALAKAG-VKEIILA-----VNYRPEDMVPF 63
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-53 5.50e-04

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: 39.91  E-value: 5.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGNVP--LPKQFLDIDNKPILIHTIEKFILVSeFNEIIIAT 53
Cdd:cd02523    3 ILAAGRGSRLRPLTedRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVT 51
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 2-64 5.52e-04

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 40.51  E-value: 5.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446561133   2 IYAGILAGGIGSRMGNVplPKQFLDIDNKPILIHTIEKFIlvSEFNEIIIA---TPAQWISHTQDI 64
Cdd:PRK14489   6 IAGVILAGGLSRRMNGR--DKALILLGGKPLIERVVDRLR--PQFARIHLNinrDPARYQDLFPGL 67
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-63 6.82e-04

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: 39.48  E-value: 6.82e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446561133   6 ILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEKFILVSeFNEIIIAT---PAQWISHTQD 63
Cdd:cd06422    4 ILAAGLGTRMR--PLtdtrPKPLVPVAGKPLIDHALDRLAAAG-IRRIVVNThhlADQIEAHLGD 65
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 1-139 1.33e-03

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 38.67  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   1 MIYAGILAGGiGSRmgnvPLP-KQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWIshtQDILKKYN--ITDQRVKV 77
Cdd:cd02513    1 KILAIIPARG-GSK----GIPgKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEI---AEVARKYGaeVPFLRPAE 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446561133  78 VAGG-TDRNETIMNIIDYIRNVNGINndDVIVTHDAVRPFLTQRIIKENIEVAEKYGAvDTVI 139
Cdd:cd02513   73 LATDtASSIDVILHALDQLEELGRDF--DIVVLLQPTSPLRSAEDIDEAIELLLSEGA-DSVF 132
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 6-40 2.32e-03

molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing enzymes, including nitrate reductase and dimethylsulfoxide reductase, the cofactor is molybdopterin-guanine dinucleotide. The family described here contains MobA, molybdenum cofactor guanylyltransferase, from the Proteobacteria only. MobA can reconstitute molybdopterin-guanine dinucleotide biosynthesis without the product of the neighboring gene MobB. The probable MobA proteins of other lineages differ sufficiently that they are not included in scope of this family. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274249  Cd Length: 186  Bit Score: 37.65  E-value: 2.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446561133    6 ILAGGIGSRMGNVplPKQFLDIDNKPILIHTIEKF 40
Cdd:TIGR02665   5 ILAGGRARRMGGR--DKGLVELGGKPLIEHVLARL 37
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-54 2.78e-03

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 38.15  E-value: 2.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446561133   6 ILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEKFILvSEFNEI-IIATP 54
Cdd:COG1209    5 ILAGGSGTRLR--PLtltvSKQLLPVYDKPMIYYPLSTLML-AGIREIlIISTP 55
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-53 3.38e-03

NTP_trnasferase_like_2 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: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 37.49  E-value: 3.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446561133   6 ILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEKFILvSEFNEIIIAT 53
Cdd:cd06426    3 IMAGGKGTRLR--PLtentPKPMLKVGGKPILETIIDRFIA-QGFRNFYISV 51
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 11-144 4.40e-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: 37.45  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  11 IGSRMGNVPLP-KQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWIshtQDILKKYNItdqrvKVV------AGGTD 83
Cdd:cd02517    6 IPARYASSRLPgKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERI---ADAVESFGG-----KVVmtspdhPSGTD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446561133  84 R----NETIMNIIDYIRNVNGinnddvivthDAvrPFLTQRIIKENIEVAEKYGAVD--TVIEAIDT 144
Cdd:cd02517   78 RiaevAEKLDADDDIVVNVQG----------DE--PLIPPEMIDQVVAALKDDPGVDmaTLATPISD 132
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 4-52 5.42e-03

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 37.17  E-value: 5.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446561133   4 AGILAGGIGSRMGNVP--LPKQFLDIDNKPILIHtIEKFILVSEFNEIIIA 52
Cdd:cd02524    1 VVILAGGLGTRLSEETelKPKPMVEIGGRPILWH-IMKIYSHYGHNDFILC 50
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 11-134 5.54e-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: 37.17  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  11 IGSRMGNVPLP-KQFLDIDNKPILIHTIEKFILVSEFNEIIIATPaqwISHTQDILKKYNiTDQRVKVVAGgtDRNETIM 89
Cdd:cd02518    4 IQARMGSTRLPgKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATS---TNEEDDPLEALA-KKLGVKVFRG--SEEDVLG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446561133  90 NIIDYIRNVNGinndDVIV--THDAvrPFLTQRIIKENIEVAEKYGA 134
Cdd:cd02518   78 RYYQAAEEYNA----DVVVriTGDC--PLIDPEIIDAVIRLFLKSGA 118
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 6-113 5.56e-03

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: 36.87  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGNV--PLPKQFLDIDNKPILIHTIEkFILVSEFNEIIIATPAQWISHTQDILKKYNITDQRVKVVAggTD 83
Cdd:cd04198    5 ILAGGGGSRLYPLtdNIPKALLPVANKPMIWYPLD-WLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEV--TI 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446561133  84 RNETIMNIIDYIRNV-NGINNDDVIVTHDAV 113
Cdd:cd04198   82 VLDEDMGTADSLRHIrKKIKKDFLVLSCDLI 112
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 2-68 8.23e-03

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. 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 epsilon shares sequence similarity with gamma 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: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 36.46  E-value: 8.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446561133   2 IYAGILAGGIGSRMGnvPL----PKQFLDIDNKPILIHTIEKFILvSEFNEIIIATPaqwiSHTQDILKKY 68
Cdd:cd02507    1 FQAVVLADGFGSRFL--PLtsdiPKALLPVANVPLIDYTLEWLEK-AGVEEVFVVCC----EHSQAIIEHL 64
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 6-53 8.37e-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: 36.38  E-value: 8.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446561133   6 ILAGGIGSRMGNV--PLPKQFLDIDNKPILIHTIEKfiLVSE-FNEIIIAT 53
Cdd:cd06915    3 ILAGGLGTRLRSVvkDLPKPLAPVAGRPFLEYLLEY--LARQgISRIVLSV 51
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-235 8.68e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 36.89  E-value: 8.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133   6 ILAGGIGSRMGNVpLPKQFLDIDNKPILIHTIEKFILVSEFNEIIIATPAQWIS------------HTQDI--------- 64
Cdd:PRK14359   7 ILAAGKGTRMKSS-LPKVLHTICGKPMLFYILKEAFAISDDVHVVLHHQKERIKeavleyfpgvifHTQDLenypgtgga 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133  65 LKKYNITDQRVKVVAGGtdrnetiMNII--DYIRNVNGINNDDVIVTHDAVRPFLTQRIIKENievaekyGAVDTVIEAI 142
Cdd:PRK14359  86 LMGIEPKHERVLILNGD-------MPLVekDELEKLLENDADIVMSVFHLADPKGYGRVVIEN-------GQVKKIVEQK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446561133 143 DTivmSKDKQNIHSipVRNEMYQgqtpqsFNIKLLQDSYRALS--SAQKEI-LSDACKIIVESGHPVKLVRGELYNIK-V 218
Cdd:PRK14359 152 DA---NEEELKIKS--VNAGVYL------FDRKLLEEYLPLLKnqNAQKEYyLTDIIALAIEKGETIKAVFVDEENFMgV 220

                        250
                 ....*....|....*..
gi 446561133 219 TTPYDLKVANAIIQGDI 235
Cdd:PRK14359 221 NSKFELAKAEEIMQERI 237
 
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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