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Conserved domains on  [gi|496661590|ref|WP_009304083|]
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MULTISPECIES: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Eggerthella]

Protein Classification

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase( domain architecture ID 10011283)

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

EC:  2.7.7.60
Gene Ontology:  GO:0050518|GO:0019288
PubMed:  12691742|9445404
SCOP:  4002789

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
11-240 5.29e-79

D-ribitol-5-phosphate cytidylyltransferase;


:

Pssm-ID: 234670  Cd Length: 227  Bit Score: 236.95  E-value: 5.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  11 FAAILAGGSGTRMGnPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYSPnfacEVTVIAGG 90
Cdd:PRK00155   5 YAIIPAAGKGSRMG-ADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDP----KVTVVAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  91 ATRNDTVTNAVSYIEssfavDDETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRR 170
Cdd:PRK00155  80 AERQDSVLNGLQALP-----DDDWVLV-HDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590 171 DFYQGQTPQSFNLLKLKKLMESLSEEEKELLTDACKVFVLrGEKVSLVFGDPANMKITYPQDMRLASALV 240
Cdd:PRK00155 154 GLWAAQTPQGFRIELLREALARALAEGKTITDDASAVERL-GKPVRLVEGRYDNIKITTPEDLALAEAIL 222
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
11-240 5.29e-79

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 236.95  E-value: 5.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  11 FAAILAGGSGTRMGnPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYSPnfacEVTVIAGG 90
Cdd:PRK00155   5 YAIIPAAGKGSRMG-ADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDP----KVTVVAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  91 ATRNDTVTNAVSYIEssfavDDETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRR 170
Cdd:PRK00155  80 AERQDSVLNGLQALP-----DDDWVLV-HDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590 171 DFYQGQTPQSFNLLKLKKLMESLSEEEKELLTDACKVFVLrGEKVSLVFGDPANMKITYPQDMRLASALV 240
Cdd:PRK00155 154 GLWAAQTPQGFRIELLREALARALAEGKTITDDASAVERL-GKPVRLVEGRYDNIKITTPEDLALAEAIL 222
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 14-240 1.16e-74

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: 225.78  E-value: 1.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  14 ILAGGSGTRMGNpDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYspNFACEVTVIAGGATR 93
Cdd:COG1211    2 IPAAGSGSRMGA-GIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKY--GIDKPVRVVAGGATR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  94 NDTVTNAVSYIESsfavDDETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRRDFY 173
Cdd:COG1211   79 QDSVRNGLEALPD----DDDWVLV-HDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLW 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496661590 174 QGQTPQSFNLLKLKKLMeSLSEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASALV 240
Cdd:COG1211  154 AAQTPQGFRLDLLLEAH-EAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALL 219
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 12-236 8.31e-74

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: 223.55  E-value: 8.31e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  12 AAILAGGSGTRMGNpDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVmarYSPNFACEVTVIAGGA 91
Cdd:cd02516    3 AIILAAGSGSRMGA-DIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL---AKYGLSKVVKIVEGGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  92 TRNDTVTNAVSYIESSfavDDETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRRD 171
Cdd:cd02516   79 TRQDSVLNGLKALPDA---DPDIVLI-HDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREK 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496661590 172 FYQGQTPQSFNLLKLKKLMeSLSEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLA 236
Cdd:cd02516  155 LWAAQTPQAFRLDLLLKAH-RQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 12-239 1.83e-49

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: 161.30  E-value: 1.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   12 AAILAGGSGTRMGnPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWvqqtRDVMARYSPNFAcEVTVIAGGA 91
Cdd:TIGR00453   2 AVIPAAGRGTRFG-SGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDD----TEFFQKYLVARA-VPKIVAGGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   92 TRNDTVTNAVSYIESSfavddETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRRD 171
Cdd:TIGR00453  76 TRQDSVRNGLKALKDA-----EFVLV-HDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496661590  172 FYQGQTPQSFNLLKLKKLMeSLSEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASAL 239
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKAL-ARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEAL 216
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 12-241 1.15e-34

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: 123.33  E-value: 1.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   12 AAILAGGSGTRMGNpDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYSpnfaceVTVIAGGA 91
Cdd:pfam01128   1 AVIPAAGSGKRMGA-GVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPS------IQLVAGGD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   92 TRNDTVTNAVSYIESsfavDDETVLVtHDAVRPFVTHRIILDNLKAARAH-GACDTVIPATDTIVESLDAATISSIPNRR 170
Cdd:pfam01128  74 TRQDSVLNGLKALAG----TAKFVLV-HDGARPCLPHADLARLLAALETGtQGAILALPVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496661590  171 DFYQGQTPQSFNLLKLKKLMESLSEEEKELlTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASALVG 241
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEI-TDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILT 218
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
11-240 5.29e-79

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 236.95  E-value: 5.29e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  11 FAAILAGGSGTRMGnPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYSPnfacEVTVIAGG 90
Cdd:PRK00155   5 YAIIPAAGKGSRMG-ADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAKDP----KVTVVAGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  91 ATRNDTVTNAVSYIEssfavDDETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRR 170
Cdd:PRK00155  80 AERQDSVLNGLQALP-----DDDWVLV-HDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590 171 DFYQGQTPQSFNLLKLKKLMESLSEEEKELLTDACKVFVLrGEKVSLVFGDPANMKITYPQDMRLASALV 240
Cdd:PRK00155 154 GLWAAQTPQGFRIELLREALARALAEGKTITDDASAVERL-GKPVRLVEGRYDNIKITTPEDLALAEAIL 222
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 14-240 1.16e-74

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: 225.78  E-value: 1.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  14 ILAGGSGTRMGNpDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYspNFACEVTVIAGGATR 93
Cdd:COG1211    2 IPAAGSGSRMGA-GIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKY--GIDKPVRVVAGGATR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  94 NDTVTNAVSYIESsfavDDETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRRDFY 173
Cdd:COG1211   79 QDSVRNGLEALPD----DDDWVLV-HDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLW 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496661590 174 QGQTPQSFNLLKLKKLMeSLSEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASALV 240
Cdd:COG1211  154 AAQTPQGFRLDLLLEAH-EAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALL 219
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 12-236 8.31e-74

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: 223.55  E-value: 8.31e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  12 AAILAGGSGTRMGNpDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVmarYSPNFACEVTVIAGGA 91
Cdd:cd02516    3 AIILAAGSGSRMGA-DIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKEL---AKYGLSKVVKIVEGGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  92 TRNDTVTNAVSYIESSfavDDETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRRD 171
Cdd:cd02516   79 TRQDSVLNGLKALPDA---DPDIVLI-HDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREK 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496661590 172 FYQGQTPQSFNLLKLKKLMeSLSEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLA 236
Cdd:cd02516  155 LWAAQTPQAFRLDLLLKAH-RQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 11-241 2.93e-61

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 192.01  E-value: 2.93e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  11 FAAILAGGSGTRMGNPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYspNFACE-VTVIAG 89
Cdd:PRK13385   3 YELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQL--NVADQrVEVVKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  90 GATRNDTVTNAVSYIESsfavddETVLVTHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPnR 169
Cdd:PRK13385  81 GTERQESVAAGLDRIGN------EDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVD-R 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496661590 170 RDFYQGQTPQSFNLLKLKKlMESLSEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASALVG 241
Cdd:PRK13385 154 NELWQGQTPQAFELKILQK-AHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAILQ 224
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 12-239 1.83e-49

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: 161.30  E-value: 1.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   12 AAILAGGSGTRMGnPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWvqqtRDVMARYSPNFAcEVTVIAGGA 91
Cdd:TIGR00453   2 AVIPAAGRGTRFG-SGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDD----TEFFQKYLVARA-VPKIVAGGD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   92 TRNDTVTNAVSYIESSfavddETVLVtHDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTIVESLDAATISSIPNRRD 171
Cdd:TIGR00453  76 TRQDSVRNGLKALKDA-----EFVLV-HDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKRVEADGFVVETVDREG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496661590  172 FYQGQTPQSFNLLKLKKLMeSLSEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASAL 239
Cdd:TIGR00453 150 LWAAQTPQAFRTELLKKAL-ARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEAL 216
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 14-241 4.95e-39

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: 138.83  E-value: 4.95e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  14 ILAGGSGTRMGnPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVqqtrDVMARYSPNFaCEVTVIAGGATR 93
Cdd:PRK09382  10 IVAAGRSTRFS-AEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDI----AYMKKALPEI-KFVTLVTGGATR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  94 NDTVTNAVSYIESSFavddetVLVtHDAVRPFVTHRIIlDNLKAARAHGACdtVIPA---TDTIVesLDAATISsipnRR 170
Cdd:PRK09382  84 QESVRNALEALDSEY------VLI-HDAARPFVPKELI-DRLIEALDKADC--VLPAlpvADTLK--RANETVD----RE 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496661590 171 DFYQGQTPQSFNLLKLKKLmeslsEEEKELLTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASALVG 241
Cdd:PRK09382 148 GLKLIQTPQLSRTKTLKAA-----ADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLS 213
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 12-241 1.15e-34

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: 123.33  E-value: 1.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   12 AAILAGGSGTRMGNpDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRDVMARYSpnfaceVTVIAGGA 91
Cdd:pfam01128   1 AVIPAAGSGKRMGA-GVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPEFRQLLGDPS------IQLVAGGD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   92 TRNDTVTNAVSYIESsfavDDETVLVtHDAVRPFVTHRIILDNLKAARAH-GACDTVIPATDTIVESLDAATISSIPNRR 170
Cdd:pfam01128  74 TRQDSVLNGLKALAG----TAKFVLV-HDGARPCLPHADLARLLAALETGtQGAILALPVTDTIKRVEADGVVAGTPDRS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496661590  171 DFYQGQTPQSFNLLKLKKLMESLSEEEKELlTDACKVFVLRGEKVSLVFGDPANMKITYPQDMRLASALVG 241
Cdd:pfam01128 149 GLWAAQTPQGFRVDLLLAAHQRGDQPGAEI-TDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILT 218
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 3-239 8.03e-27

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 103.66  E-value: 8.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   3 RANEVSNAFAA-------ILAGGSGTRMGnPDKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCPETWvqqtRDVMAR 75
Cdd:PLN02728  11 AADDETSAVVKeksvsviLLAGGVGKRMG-ANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSY----RDVFEE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  76 YSPNFACEVTVIAGGATRNDTVTNAVSyiessfAVDDETVLV-THDAVRPFVTHRIILDNLKAARAHGACDTVIPATDTI 154
Cdd:PLN02728  86 AVENIDVPLKFALPGKERQDSVFNGLQ------EVDANSELVcIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590 155 VESLDAATISSIPNRRDFYQGQTPQ---------SFNLLKLKKLmeslseeekeLLTDACKVFVLRGEKVSLVFGDPANM 225
Cdd:PLN02728 160 KEANSDSFVVKTLDRKRLWEMQTPQvikpellrrGFELVEREGL----------EVTDDVSIVEALKHPVFITEGSYTNI 229

                        250
                 ....*....|....
gi 496661590 226 KITYPQDMRLASAL 239
Cdd:PLN02728 230 KVTTPDDMLVAERI 243
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 12-158 1.18e-07

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: 50.27  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590  12 AAILAGGSGTRMGnpdKPKQFLMLGSKPILVHTVEKFcvTGEFDAVLVLCPETWVQQtrdvmARYSPNFACEVTVIAG-- 89
Cdd:cd02503    3 GVILAGGKSRRMG---GDKALLELGGKPLLEHVLERL--KPLVDEVVISANRDQERY-----ALLGVPVIPDEPPGKGpl 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496661590  90 -GatrndtvtnavsyIESSF-AVDDETVLVThdAV-RPFVThRIILDNLKAARAHGaCDTVIPATDTIVESL 158
Cdd:cd02503   73 aG-------------ILAALrAAPADWVLVL--ACdMPFLP-PELLERLLAAAEEG-ADAVVPKSGGRLQPL 127
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 12-60 2.95e-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: 49.10  E-value: 2.95e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 496661590  12 AAILAGGSGTRMGnpdKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVL 60
Cdd:cd04182    3 AIILAAGRSSRMG---GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVL 48
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 12-152 3.77e-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: 48.34  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   12 AAILAGGSGTRMGnpdKPKQFLMLGSKPILVHTVEKF-------CVTGEFDAVLVLCPETWVQQTRDVMARYSPnfacev 84
Cdd:pfam12804   1 AVILAGGRSSRMG---GDKALLPLGGKPLLERVLERLrpagdevVVVANDEEVLAALAGLGVPVVPDPDPGQGP------ 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496661590   85 tvIAGGATrndtvtnAVSYIEssfavDDETVLVTH-DAvrPFVTHRIIlDNLKAARAHGACDTVIPATD 152
Cdd:pfam12804  72 --LAGLLA-------ALRAAP-----GADAVLVLAcDM--PFLTPELL-RRLLAAAEESGADIVVPVYD 123
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
12-59 4.10e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.00  E-value: 4.10e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 496661590  12 AAILAGGSGTRMGnpdKPKQFLMLGSKPILVHTVEKFCVTGeFDAVLV 59
Cdd:COG2068    6 AIILAAGASSRMG---RPKLLLPLGGKPLLERAVEAALAAG-LDPVVV 49
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 11-71 1.54e-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: 1.54e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496661590  11 FAAILAGGSGTR---MGNPDKPKQFLML-GSKPILVHTVEKFCVTGEFDAVLVLCPETWVQQTRD 71
Cdd:cd02509    2 YPVILAGGSGTRlwpLSRESYPKQFLKLfGDKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVRE 66
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 12-48 2.31e-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: 47.07  E-value: 2.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 496661590  12 AAILAGGSGTRMGnP---DKPKQFLMLGSKPILVHTVEKF 48
Cdd:COG1208    2 AVILAGGLGTRLR-PltdTRPKPLLPVGGKPLLEHILERL 40
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
11-61 2.58e-06

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 47.37  E-value: 2.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496661590  11 FAAILAGGSGTR---MGNPDKPKQFL-MLGSKPILVHTVEKFCVTGEFDAVLVLC 61
Cdd:COG0836    4 YPVILAGGSGTRlwpLSRESYPKQFLpLLGEKSLLQQTVERLAGLVPPENILVVT 58
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 12-63 5.16e-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: 45.57  E-value: 5.16e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496661590  12 AAILAGGSGTRMGnpdKPKQFLMLGSKPILVHTVEKfcVTGEFDAVLVLCPE 63
Cdd:COG0746    7 GVILAGGRSRRMG---QDKALLPLGGRPLLERVLER--LRPQVDEVVIVANR 53
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 12-84 3.93e-05

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 43.25  E-value: 3.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496661590  12 AAILAGGSGTRMGNPDKPkqFLMLGSKPILVHTVEKfcVTGEFDAVLVLCPetwvqqtRDvMARYSPnFACEV 84
Cdd:PRK00317   6 GVILAGGRSRRMGGVDKG--LQELNGKPLIQHVIER--LAPQVDEIVINAN-------RN-LARYAA-FGLPV 65
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 12-60 2.18e-04

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: 41.03  E-value: 2.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496661590  12 AAILAGGSGTRMGnP---DKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVL 60
Cdd:cd04181    1 AVILAAGKGTRLR-PltdTRPKPLLPIAGKPILEYIIERLARAGIDEIILVV 51
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 11-48 2.28e-04

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: 40.73  E-value: 2.28e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 496661590   11 FAAILAGGSGTRMGNPDKPKQFlmLGSKPILVHTVEKF 48
Cdd:TIGR02665   2 SGVILAGGRARRMGGRDKGLVE--LGGKPLIEHVLARL 37
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 12-48 2.66e-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: 41.06  E-value: 2.66e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 496661590  12 AAILAGGSGTRMGNP--DKPKQFLMLGSKPILVHTVEKF 48
Cdd:cd02523    1 AIILAAGRGSRLRPLteDRPKCLLEINGKPLLERQIETL 39
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 12-43 3.14e-04

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: 41.02  E-value: 3.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 496661590  12 AAILAGGSGTRM--GNPDKPKQFLMLGSKPILVH 43
Cdd:cd02524    1 VVILAGGLGTRLseETELKPKPMVEIGGRPILWH 34
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 12-87 3.25e-04

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 40.70  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496661590   12 AAILAGGSGTR-----MGNPdkPKQFLMLGSKPILVHTVEKfCVTGEFDAVLVLCpetwVQQTRDVMARY---SPNFACE 83
Cdd:pfam00483   2 AIILAGGSGTRlwpltRTLA--KPLVPVGGKYPLIDYPLSR-LANAGIREIIVIL----TQEHRFMLNELlgdGSKFGVQ 74


                  ....
gi 496661590   84 VTVI 87
Cdd:pfam00483  75 ITYA 78
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 12-48 4.87e-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: 4.87e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 496661590  12 AAILAGGSGTRMGNPDKPkqFLMLGSKPILVHTVEKF 48
Cdd:PRK14489   8 GVILAGGLSRRMNGRDKA--LILLGGKPLIERVVDRL 42
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
12-48 5.51e-04

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 40.22  E-value: 5.51e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 496661590  12 AAILAGGSGTRMGNP--DKPKQFLMLGSKPILVHTVEKF 48
Cdd:COG1213    2 AVILAAGRGSRLGPLtdDIPKCLVEIGGKTLLERQLEAL 40
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 12-62 1.64e-03

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: 38.70  E-value: 1.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496661590  12 AAILAGGSGTRMGnP---DKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVLCP 62
Cdd:cd04189    3 GLILAGGKGTRLR-PltyTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGP 55
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 15-46 3.39e-03

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 37.18  E-value: 3.39e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 496661590  15 LAGGSGTRMGNPDKPkqFLMLGSKPILVHTVE 46
Cdd:COG2266    1 MAGGKGTRLGGGEKP--LLEICGKPMIDRVID 30
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 12-84 3.48e-03

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: 37.58  E-value: 3.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496661590  12 AAILAGGSGTRMgNP---DKPKQFLMLGSKPILVHTVEKFCVTGEFDAVLVL--CPETWVQQTRDVMARYSPNFACEV 84
Cdd:cd06425    3 ALILVGGYGTRL-RPltlTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVnyRPEDMVPFLKEYEKKLGIKITFSI 79
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 14-49 8.44e-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: 36.34  E-value: 8.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 496661590  14 ILAGGSGTRMGnP---DKPKQFLMLGSKPILVHTVEKFC 49
Cdd:cd06426    3 IMAGGKGTRLR-PlteNTPKPMLKVGGKPILETIIDRFI 40
 
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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