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Conserved domains on  [gi|933758482|ref|WP_054332300|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Merdimmobilis hominis]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 15-232 6.74e-92

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: 269.31  E-value: 6.74e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  15 IVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSIQKIKTIAVGGKTRQQ 92
Cdd:COG1211    1 IIPAAGSGSRMGAgiPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  93 SVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQTPQV 172
Cdd:COG1211   81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482 173 FEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLE 232
Cdd:COG1211  161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLR 220
 
Name Accession Description Interval E-value
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 15-232 6.74e-92

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: 269.31  E-value: 6.74e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  15 IVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSIQKIKTIAVGGKTRQQ 92
Cdd:COG1211    1 IIPAAGSGSRMGAgiPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  93 SVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQTPQV 172
Cdd:COG1211   81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482 173 FEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLE 232
Cdd:COG1211  161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLR 220
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
10-232 8.46e-86

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 253.90  E-value: 8.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  10 GMVSAIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSiQKIKTIAvGG 87
Cdd:PRK00155   2 MMVYAIIPAAGKGSRMGAdrPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD-PKVTVVA-GG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  88 KTRQQSVFAGVRAASEDAaYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLT 167
Cdd:PRK00155  80 AERQDSVLNGLQALPDDD-WVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933758482 168 QTPQVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLE 232
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILK 223
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 12-223 6.32e-81

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: 241.27  E-value: 6.32e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  12 VSAIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMgDYLALTEDYSIQKIKTIAVGGKT 89
Cdd:cd02516    1 VAAIILAAGSGSRMGAdiPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDI-DLAKELAKYGLSKVVKIVEGGAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  90 RQQSVFAGVRAASE-DAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQ 168
Cdd:cd02516   80 RQDSVLNGLKALPDaDPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 933758482 169 TPQVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPED 223
Cdd:cd02516  160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPED 214
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 13-231 2.33e-68

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: 209.45  E-value: 2.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   13 SAIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYsiqKIKTIAVGGKTR 90
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSgvPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVAR---AVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   91 QQSVFAGVRAAsEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQTP 170
Cdd:TIGR00453  78 QDSVRNGLKAL-KDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933758482  171 QVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALL 231
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 14-232 7.32e-58

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 182.65  E-value: 7.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   14 AIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSIQkiktIAVGGKTRQ 91
Cdd:pfam01128   1 AVIPAAGSGKRMGAgvPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQ----LVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   92 QSVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAA-QREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQTP 170
Cdd:pfam01128  77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLARLLAALeTGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933758482  171 QVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLE 232
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILT 218
 
Name Accession Description Interval E-value
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 15-232 6.74e-92

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: 269.31  E-value: 6.74e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  15 IVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSIQKIKTIAVGGKTRQQ 92
Cdd:COG1211    1 IIPAAGSGSRMGAgiPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  93 SVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQTPQV 172
Cdd:COG1211   81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482 173 FEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLE 232
Cdd:COG1211  161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLR 220
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
10-232 8.46e-86

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 253.90  E-value: 8.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  10 GMVSAIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSiQKIKTIAvGG 87
Cdd:PRK00155   2 MMVYAIIPAAGKGSRMGAdrPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKD-PKVTVVA-GG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  88 KTRQQSVFAGVRAASEDAaYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLT 167
Cdd:PRK00155  80 AERQDSVLNGLQALPDDD-WVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 933758482 168 QTPQVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLE 232
Cdd:PRK00155 159 QTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILK 223
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 12-223 6.32e-81

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: 241.27  E-value: 6.32e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  12 VSAIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMgDYLALTEDYSIQKIKTIAVGGKT 89
Cdd:cd02516    1 VAAIILAAGSGSRMGAdiPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDI-DLAKELAKYGLSKVVKIVEGGAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  90 RQQSVFAGVRAASE-DAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQ 168
Cdd:cd02516   80 RQDSVLNGLKALPDaDPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 933758482 169 TPQVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPED 223
Cdd:cd02516  160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPED 214
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 13-231 2.33e-68

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: 209.45  E-value: 2.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   13 SAIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYsiqKIKTIAVGGKTR 90
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSgvPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVAR---AVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   91 QQSVFAGVRAAsEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQTP 170
Cdd:TIGR00453  78 QDSVRNGLKAL-KDAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 933758482  171 QVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALL 231
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 14-232 7.32e-58

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 182.65  E-value: 7.32e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   14 AIVAAGGSSQRMGE--NKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSIQkiktIAVGGKTRQ 91
Cdd:pfam01128   1 AVIPAAGSGKRMGAgvPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQ----LVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   92 QSVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAA-QREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYLTQTP 170
Cdd:pfam01128  77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLARLLAALeTGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933758482  171 QVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLE 232
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILT 218
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 9-236 2.66e-56

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 179.93  E-value: 2.66e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   9 RGMVSAIVAAGGSSQRMGEN--KLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSIqKIKtIAVG 86
Cdd:PLN02728  22 EKSVSVILLAGGVGKRMGANmpKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENIDV-PLK-FALP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  87 GKTRQQSVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGPDGFILSTPDRDSLYL 166
Cdd:PLN02728 100 GKERQDSVFNGLQEVDANSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWE 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482 167 TQTPQVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALLEYAGE 236
Cdd:PLN02728 180 MQTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERSD 249
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 15-231 6.40e-41

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 139.62  E-value: 6.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  15 IVAAGGSSQRMG--ENKLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYSI--QKIKTIAvGGKTR 90
Cdd:PRK13385   6 IFLAAGQGKRMNapLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVadQRVEVVK-GGTER 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  91 QQSVFAGV-RAASEDAAyyCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAgPDGFILSTPDRDSLYLTQT 169
Cdd:PRK13385  85 QESVAAGLdRIGNEDVI--LVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRV-KDKQVIETVDRNELWQGQT 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933758482 170 PQVFEASLYREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALL 231
Cdd:PRK13385 162 PQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAIL 223
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 12-231 9.39e-36

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: 129.97  E-value: 9.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  12 VSAIVAAGGSSQRMGEN--KLLMELYGIPVLARTLLTLDGCREIDEIILVCREEDMGDYLALTEDYsiqKIKTIAVGGKT 89
Cdd:PRK09382   6 ISLVIVAAGRSTRFSAEvkKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI---KFVTLVTGGAT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  90 RQQSVFAGVRAASEDaaYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKDTIKIAGpdgfilSTPDRDSLYLTQT 169
Cdd:PRK09382  83 RQESVRNALEALDSE--YVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKRAN------ETVDREGLKLIQT 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 933758482 170 PQVFEaslyREAMEAALAAGKEYTDDCQLVEAIGRRVYLAGGDYANIKLTTPEDQIVAEALL 231
Cdd:PRK09382 155 PQLSR----TKTLKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
11-139 2.70e-12

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 63.26  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  11 MVSAIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCReIDEIILVCREEDMgdylALTEDYSIQKIKTIAVGGKTR 90
Cdd:COG2068    3 KVAAIILAAGASSRMGRPKLLLPLGGKPLLERAVEAALAAG-LDPVVVVLGADAE----EVAAALAGLGVRVVVNPDWEE 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 933758482  91 QQ--SVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAA 139
Cdd:COG2068   78 GMssSLRAGLAALPADADAVLVLLGDQPLVTAETLRRLLAAFRESPASIVA 128
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 14-144 6.44e-11

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: 58.75  E-value: 6.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   14 AIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCReiDEIILVCREEDMGDYLAlteDYSIQKIKTIAVGgktrqQS 93
Cdd:pfam12804   1 AVILAGGRSSRMGGDKALLPLGGKPLLERVLERLRPAG--DEVVVVANDEEVLAALA---GLGVPVVPDPDPG-----QG 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 933758482   94 VFAGVRAA---SEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAAVKAKD 144
Cdd:pfam12804  71 PLAGLLAAlraAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDG 124
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 12-139 6.13e-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: 56.80  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482  12 VSAIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCREiDEIILVCREEDmgdyLALTEDYSIQKIKTIAVGGKTRQ 91
Cdd:cd04182    1 IAAIILAAGRSSRMGGNKLLLPLDGKPLLRHALDAALAAGL-SRVIVVLGAEA----DAVRAALAGLPVVVVINPDWEEG 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 933758482  92 Q--SVFAGVRAASEDAAYYCIHDGARPLASRQVIAGVLEAAQREGAATAA 139
Cdd:cd04182   76 MssSLAAGLEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIVA 125
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 12-64 1.84e-08

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: 52.50  E-value: 1.84e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 933758482  12 VSAIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCreIDEIILVCREED 64
Cdd:COG0746    5 ITGVILAGGRSRRMGQDKALLPLGGRPLLERVLERLRPQ--VDEVVIVANRPE 55
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 13-134 2.16e-08

molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA, the GTP:molybdopterin guanylyltransferase. The MocA family is particularly closely related in phylogenetic distribution to other markers of selenium-dependent molybdenum hydroxylases (SDMH), suggesting most SDMH must use MCD rather than molybdopterin guanine dinucleotide.


Pssm-ID: 274516  Cd Length: 188  Bit Score: 52.34  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 933758482   13 SAIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCReIDEIILVCREEDMgdylALTEDYSIQKIKTIAVGGKTRQ- 91
Cdd:TIGR03310   1 DAIILAAGLSSRMGQNKLLLPYKGKTILEHVVDNALRLF-FDEVILVLGHEAD----ELVALLANHSNITLVHNPQYAEg 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 933758482   92 --QSVFAGVRAASEDAAYYCIHdGARPLASRQVIAGVLEAAQREG 134
Cdd:TIGR03310  76 qsSSIKLGLELPVQSDGYLFLL-GDQPFVTPDIIQLLLEAFALKN 119
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 12-64 2.95e-08

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: 51.81  E-value: 2.95e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 933758482  12 VSAIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCreIDEIILVCREED 64
Cdd:cd02503    1 ITGVILAGGKSRRMGGDKALLELGGKPLLEHVLERLKPL--VDEVVISANRDQ 51
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
6-57 2.80e-07

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 49.26  E-value: 2.80e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 933758482   6 KKQRGMVSAIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCREIDEII 57
Cdd:PRK02726   2 KTVKNNLVALILAGGKSSRMGQDKALLPWQGVPLLQRVARIAAACADEVYII 53
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 9-60 7.07e-06

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 45.18  E-value: 7.07e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 933758482   9 RGMVSAIVAAGGSSQRM-GENKLLMELYGIPVLARTLLTLDGcrEIDEIILVC 60
Cdd:PRK00317   1 MPPITGVILAGGRSRRMgGVDKGLQELNGKPLIQHVIERLAP--QVDEIVINA 51
PRK14490 PRK14490
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MobA; ...
 2-68 6.00e-04

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


Pssm-ID: 237728 [Multi-domain]  Cd Length: 369  Bit Score: 40.42  E-value: 6.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 933758482   2 LFQRKKQRGMVSAIVAAGGSSQRMGENKLLMELYGIPVLARTLLTLDGCreIDEIILVCREEDMGDY 68
Cdd:PRK14490 165 HLLGRAEEVPLSGLVLAGGRSSRMGSDKALLSYHESNQLVHTAALLRPH--CQEVFISCRAEQAEQY 229
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 14-64 4.17e-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: 4.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 933758482  14 AIVAAGGSSQRMgENKLLMELYGIPVLARTLLTLDGCREIDEIILVC--REED 64
Cdd:cd02518    2 AIIQARMGSTRL-PGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstNEED 53
 
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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