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Conserved domains on  [gi|1561288322|gb|QAT50462|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Caproiciproducens sp. NJN-50]

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]; ...
 13-236 2.65e-103

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: 298.20  E-value: 2.65e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKAAAVVPGGASRQE 92
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  93 SVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTPQT 172
Cdd:COG1211    81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561288322 173 FRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:COG1211   161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
 
Name Accession Description Interval E-value
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 13-236 2.65e-103

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: 298.20  E-value: 2.65e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKAAAVVPGGASRQE 92
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  93 SVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTPQT 172
Cdd:COG1211    81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561288322 173 FRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:COG1211   161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
10-236 4.48e-95

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 277.78  E-value: 4.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLG-AMRDCIGRYriqKAAAVVPGGA 88
Cdd:PRK00155    4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPdFAELLLAKD---PKVTVVAGGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  89 SRQESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:PRK00155   81 ERQDSVLNGLQALP-DDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAAQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:PRK00155  160 TPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 10-227 6.31e-89

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 261.69  E-value: 6.31e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDcIGRYRIQKAAAVVPGGAS 89
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE-LAKYGLSKVVKIVEGGAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  90 RQESVFAGVEALP-RDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:cd02516    80 RQDSVLNGLKALPdADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIA 227
Cdd:cd02516   160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 11-231 2.09e-79

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: 237.57  E-value: 2.09e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  11 CAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKaaaVVPGGASR 90
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK---IVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  91 QESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:TIGR00453  78 QDSVRNGLKALK-DAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 12-233 2.15e-69

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: 212.31  E-value: 2.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  12 AVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQkaaaVVPGGASRQ 91
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQ----LVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  92 ESVFAGVEALPRDAGYLAVHDGARPLVTPEEID-LCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:pfam01128  77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLArLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKK 233
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
 
Name Accession Description Interval E-value
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 13-236 2.65e-103

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: 298.20  E-value: 2.65e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKAAAVVPGGASRQE 92
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  93 SVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTPQT 172
Cdd:COG1211    81 SVRNGLEALPDDDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQG 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1561288322 173 FRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:COG1211   161 FRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
10-236 4.48e-95

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 277.78  E-value: 4.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLG-AMRDCIGRYriqKAAAVVPGGA 88
Cdd:PRK00155    4 VYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPdFAELLLAKD---PKVTVVAGGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  89 SRQESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:PRK00155   81 ERQDSVLNGLQALP-DDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAAQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKREG 236
Cdd:PRK00155  160 TPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 10-227 6.31e-89

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 261.69  E-value: 6.31e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDcIGRYRIQKAAAVVPGGAS 89
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE-LAKYGLSKVVKIVEGGAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  90 RQESVFAGVEALP-RDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQ 168
Cdd:cd02516    80 RQDSVLNGLKALPdADPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1561288322 169 TPQTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIA 227
Cdd:cd02516   160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 11-231 2.09e-79

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: 237.57  E-value: 2.09e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  11 CAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKaaaVVPGGASR 90
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPK---IVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  91 QESVFAGVEALPrDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:TIGR00453  78 QDSVRNGLKALK-DAEFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:TIGR00453 157 QAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 12-233 2.15e-69

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: 212.31  E-value: 2.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  12 AVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQkaaaVVPGGASRQ 91
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPSIQ----LVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  92 ESVFAGVEALPRDAGYLAVHDGARPLVTPEEID-LCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTP 170
Cdd:pfam01128  77 DSVLNGLKALAGTAKFVLVHDGARPCLPHADLArLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1561288322 171 QTFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKK 233
Cdd:pfam01128 157 QGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 13-234 4.72e-63

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 197.26  E-value: 4.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRIQKAAAVvPGgASRQE 92
Cdd:PLN02728   28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENIDVPLKFAL-PG-KERQD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  93 SVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQRVLSTPDREGLWTVQTPQT 172
Cdd:PLN02728  106 SVFNGLQEVDANSELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWEMQTPQV 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561288322 173 FRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAILKKR 234
Cdd:PLN02728  186 IKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNER 247
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 13-231 3.12e-50

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 163.89  E-value: 3.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  13 VIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYRI-QKAAAVVPGGASRQ 91
Cdd:PRK13385    6 IFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVaDQRVEVVKGGTERQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  92 ESVFAGVEALPRDAGYLaVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDSGQrVLSTPDREGLWTVQTPQ 171
Cdd:PRK13385   86 ESVAAGLDRIGNEDVIL-VHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQ-VIETVDRNELWQGQTPQ 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322 172 TFRMDLYRRALSKAREDGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:PRK13385  164 AFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAIL 223
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 10-231 1.47e-44

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: 153.08  E-value: 1.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVCRKEDLGAMRDCIGRYriqKAAAVVPGGAS 89
Cdd:PRK09382    6 ISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEI---KFVTLVTGGAT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  90 RQESVFAGVEALprDAGYLAVHDGARPLVTPEEIDLCVRDAFKTGASALGTPLKDTVKRIDsgqrvlSTPDREGLWTVQT 169
Cdd:PRK09382   83 RQESVRNALEAL--DSEYVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKRAN------ETVDREGLKLIQT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1561288322 170 PQTFRMDLYRRALSKaredGKDYTDDCQLVERIGVRVHLCRGSYENIKLTTPEDLVIAEAIL 231
Cdd:PRK09382  155 PQLSRTKTLKAAADG----RGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
12-141 5.34e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 57.09  E-value: 5.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFDGARaVGQVVIVCRKEDlGAMRDCIGRYRIQkaAAVVPGGASRQ 91
Cdd:COG2068     6 AIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAG-LDPVVVVLGADA-EEVAAALAGLGVR--VVVNPDWEEGM 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1561288322  92 -ESVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLcVRDAFKTGASALGTP 141
Cdd:COG2068    80 sSSLRAGLAALPADADAVLVLLGDQPLVTAETLRR-LLAAFRESPASIVAP 129
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 12-132 3.10e-09

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: 54.65  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  12 AVIAAAGRSARMGSGisKQFLPVLGVPAVVRTLRAFDgARAVGQVVIVCRKEDLGAMRDCIGRYRIQkaaaVVPGGASRQ 91
Cdd:TIGR03310   2 AIILAAGLSSRMGQN--KLLLPYKGKTILEHVVDNAL-RLFFDEVILVLGHEADELVALLANHSNIT----LVHNPQYAE 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1561288322  92 ---ESVFAGVEALPRDAGYLAVHdGARPLVTPEEIDLcVRDAFK 132
Cdd:TIGR03310  75 gqsSSIKLGLELPVQSDGYLFLL-GDQPFVTPDIIQL-LLEAFA 116
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 10-141 4.96e-08

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 51.41  E-value: 4.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  10 CCAVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFDGARAvGQVVIVCR---KEDLGAMRDCIGRYRIQKAAAVvpG 86
Cdd:cd04182     1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGL-SRVIVVLGaeaDAVRAALAGLPVVVVINPDWEE--G 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1561288322  87 GASrqeSVFAGVEALPRDAGYLAVHDGARPLVTPEEIDLcVRDAFKTGASALGTP 141
Cdd:cd04182    76 MSS---SLAAGLEALPADADAVLILLADQPLVTAETLRA-LIDAFREDGAGIVAP 126
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 12-65 1.33e-05

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: 44.11  E-value: 1.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1561288322  12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFdgARAVGQVVIVCRKEDL 65
Cdd:pfam12804   1 AVILAGGRSSRMGG--DKALLPLGGKPLLERVLERL--RPAGDEVVVVANDEEV 50
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 12-64 2.74e-04

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 40.56  E-value: 2.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1561288322  12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFdgARAVGQVVIVCRKED 64
Cdd:COG0746     7 GVILAGGRSRRMGQ--DKALLPLGGRPLLERVLERL--RPQVDEVVIVANRPE 55
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 12-64 1.04e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 38.71  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1561288322  12 AVIAAAGRSARMGSgiSKQFLPVLGVPAVVRTLRAFDGarAVGQVVIVCRKED 64
Cdd:cd02503     3 GVILAGGKSRRMGG--DKALLELGGKPLLEHVLERLKP--LVDEVVISANRDQ 51
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 12-63 1.68e-03

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: 38.37  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1561288322  12 AVIAAAGRSARMGS---GISKQFLPVLGVPAVVRTLRAFDGARaVGQVVIVC--RKE 63
Cdd:cd02523     1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVTgyKKE 56
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
12-65 2.07e-03

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 38.30  E-value: 2.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1561288322  12 AVIAAAGRSARMG---SGISKQFLPVLGVPAVVRTLRAFDGArAVGQVVIVC--RKEDL 65
Cdd:COG1213     2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTgyKAELI 59
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-121 2.65e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.30  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561288322  10 CCAVIAAAGRSARMGSGISKQFLPVLGVPAVVRTLRAFDGARAVGQVVIVcrkedlgamrdciGRYRIQKAAAVVPGGAS 89
Cdd:PRK14353    6 CLAIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVV-------------GPGAEAVAAAAAKIAPD 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1561288322  90 ----RQE-------SVFAGVEALPRDAGYLAVHDGARPLVTPE 121
Cdd:PRK14353   73 aeifVQKerlgtahAVLAAREALAGGYGDVLVLYGDTPLITAE 115
 
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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