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Conserved domains on  [gi|2100534769|ref|WP_223578045|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Kangiella taiwanensis]

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;
5-231 1.43e-99

D-ribitol-5-phosphate cytidylyltransferase;


:

Pssm-ID: 234670  Cd Length: 227  Bit Score: 288.96  E-value: 1.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   5 RIWAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSD-DYWAKLPFTDNPRVLTTNGGQNR 83
Cdd:PRK00155    3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  84 VDSVLSALQLIRDiegteHDWVMVHDAARPCLSSRHIDDLVHAKESSpDGAILAIGAIDTVKQANQQQVIDKTIDRDTIW 163
Cdd:PRK00155   83 QDSVLNGLQALPD-----DDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGGIVDTPDRSGLW 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2100534769 164 LAQTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWLNH 231
Cdd:PRK00155  157 AAQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-231 1.43e-99

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 288.96  E-value: 1.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   5 RIWAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSD-DYWAKLPFTDNPRVLTTNGGQNR 83
Cdd:PRK00155    3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  84 VDSVLSALQLIRDiegteHDWVMVHDAARPCLSSRHIDDLVHAKESSpDGAILAIGAIDTVKQANQQQVIDKTIDRDTIW 163
Cdd:PRK00155   83 QDSVLNGLQALPD-----DDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGGIVDTPDRSGLW 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2100534769 164 LAQTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWLNH 231
Cdd:PRK00155  157 AAQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-231 6.46e-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: 6.46e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   9 VIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSD-DYWAKL--PFTDNPRVLTTNGGQNRVD 85
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  86 SVLSALQLIRDiegtEHDWVMVHDAARPCLSSRHIDDLVHAKESsPDGAILAIGAIDTVKQANQQQVIDKTIDRDTIWLA 165
Cdd:COG1211    81 SVRNGLEALPD----DDDWVLVHDAARPLVSPELIDRVIEAARE-YGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2100534769 166 QTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWLNH 231
Cdd:COG1211   156 QTPQGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-225 1.17e-85

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: 253.21  E-value: 1.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   6 IWAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSDDYWAK--LPFTDNPRVLTTNGGQNR 83
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  84 VDSVLSALQLIrdiEGTEHDWVMVHDAARPCLSSRHIDDLVHAKESSpDGAILAIGAIDTVKQANQQQVIDKTIDRDTIW 163
Cdd:cd02516    81 QDSVLNGLKAL---PDADPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVDDDGVVVETLDREKLW 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2100534769 164 LAQTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLA 225
Cdd:cd02516   157 AAQTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 7-225 1.36e-75

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: 227.56  E-value: 1.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   7 WAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSDDYWAKLPFTDNPRVLTTNGGQNRVDS 86
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  87 VLSALQLIRDiegteHDWVMVHDAARPCLSSRHIDDLVHAKESsPDGAILAIGAIDTVKQANQQQVIDKTIDRDTIWLAQ 166
Cdd:TIGR00453  81 VRNGLKALKD-----AEFVLVHDAARPFVPKELLDRLLEALRK-AGAAILALPVADTLKRVEADGFVVETVDREGLWAAQ 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2100534769 167 TPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLA 225
Cdd:TIGR00453 155 TPQAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALA 213
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 8-229 5.83e-64

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: 198.06  E-value: 5.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSD-DYWAKLPFtdNPRVLTTNGGQNRVDS 86
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  87 VLSALQLIRDiegtEHDWVMVHDAARPCLSSRHIDDLVHAKESSPDGAILAIGAIDTVKQANQQQVIDKTIDRDTIWLAQ 166
Cdd:pfam01128  79 VLNGLKALAG----TAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100534769 167 TPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWL 229
Cdd:pfam01128 155 TPQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-231 1.43e-99

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 288.96  E-value: 1.43e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   5 RIWAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSD-DYWAKLPFTDNPRVLTTNGGQNR 83
Cdd:PRK00155    3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGAER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  84 VDSVLSALQLIRDiegteHDWVMVHDAARPCLSSRHIDDLVHAKESSpDGAILAIGAIDTVKQANQQQVIDKTIDRDTIW 163
Cdd:PRK00155   83 QDSVLNGLQALPD-----DDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGGIVDTPDRSGLW 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2100534769 164 LAQTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWLNH 231
Cdd:PRK00155  157 AAQTPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKR 224
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-231 6.46e-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: 6.46e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   9 VIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSD-DYWAKL--PFTDNPRVLTTNGGQNRVD 85
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDiEYFEELlaKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  86 SVLSALQLIRDiegtEHDWVMVHDAARPCLSSRHIDDLVHAKESsPDGAILAIGAIDTVKQANQQQVIDKTIDRDTIWLA 165
Cdd:COG1211    81 SVRNGLEALPD----DDDWVLVHDAARPLVSPELIDRVIEAARE-YGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2100534769 166 QTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWLNH 231
Cdd:COG1211   156 QTPQGFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRS 221
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-225 1.17e-85

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: 253.21  E-value: 1.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   6 IWAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSDDYWAK--LPFTDNPRVLTTNGGQNR 83
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKelAKYGLSKVVKIVEGGATR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  84 VDSVLSALQLIrdiEGTEHDWVMVHDAARPCLSSRHIDDLVHAKESSpDGAILAIGAIDTVKQANQQQVIDKTIDRDTIW 163
Cdd:cd02516    81 QDSVLNGLKAL---PDADPDIVLIHDAARPFVSPELIDRLIDALKEY-GAAIPAVPVTDTIKRVDDDGVVVETLDREKLW 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2100534769 164 LAQTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLA 225
Cdd:cd02516   157 AAQTPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 7-225 1.36e-75

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: 227.56  E-value: 1.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   7 WAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSDDYWAKLPFTDNPRVLTTNGGQNRVDS 86
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  87 VLSALQLIRDiegteHDWVMVHDAARPCLSSRHIDDLVHAKESsPDGAILAIGAIDTVKQANQQQVIDKTIDRDTIWLAQ 166
Cdd:TIGR00453  81 VRNGLKALKD-----AEFVLVHDAARPFVPKELLDRLLEALRK-AGAAILALPVADTLKRVEADGFVVETVDREGLWAAQ 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2100534769 167 TPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLA 225
Cdd:TIGR00453 155 TPQAFRTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALA 213
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 8-229 5.83e-64

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: 198.06  E-value: 5.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSD-DYWAKLPFtdNPRVLTTNGGQNRVDS 86
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDtPEFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  87 VLSALQLIRDiegtEHDWVMVHDAARPCLSSRHIDDLVHAKESSPDGAILAIGAIDTVKQANQQQVIDKTIDRDTIWLAQ 166
Cdd:pfam01128  79 VLNGLKALAG----TAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100534769 167 TPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWL 229
Cdd:pfam01128 155 TPQGFRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAIL 217
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 8-234 7.92e-49

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: 164.25  E-value: 7.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPSDDYWAKLPFTDNPRVLTTNGGQNRVDSV 87
Cdd:PRK09382    8 LVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGGATRQESV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  88 LSALQLIRDiegtehDWVMVHDAARPCLSSRHIDDLVHAKESSpDGAILAIGAIDTVKQANqqqvidKTIDRDTIWLAQT 167
Cdd:PRK09382   88 RNALEALDS------EYVLIHDAARPFVPKELIDRLIEALDKA-DCVLPALPVADTLKRAN------ETVDREGLKLIQT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2100534769 168 PQFFPLislsNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWLNHGLD 234
Cdd:PRK09382  155 PQLSRT----KTLKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLLSPSRD 217
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 6-225 3.71e-34

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 122.29  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   6 IWAVIPAAGIGS-RMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVA-----LNPSDDYWAKLPFTDNpRVLTTNG 79
Cdd:PRK13385    2 NYELIFLAAGQGkRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVtqaqeRKHVQDLMKQLNVADQ-RVEVVKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  80 GQNRVDSVLSALQLIrdieGTEhDWVMVHDAARPCLSSRHIDDLVHAKESSpDGAILAIGAIDTVKQANQQQVIDkTIDR 159
Cdd:PRK13385   81 GTERQESVAAGLDRI----GNE-DVILVHDGARPFLTQDIIDRLLEGVAKY-GAAICAVEVKDTVKRVKDKQVIE-TVDR 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2100534769 160 DTIWLAQTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLA 225
Cdd:PRK13385  154 NELWQGQTPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLA 219
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 9-230 1.99e-33

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 120.99  E-value: 1.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   9 VIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVALNPS--DDYWAKLPFTDNPRVLtTNGGQNRVDS 86
Cdd:PLN02728   28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSyrDVFEEAVENIDVPLKF-ALPGKERQDS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  87 VLSALQLIRDieGTEhdWVMVHDAARPCLSSRHIDDLVH-AKESSpdGAILAIGAIDTVKQANQQQVIDKTIDRDTIWLA 165
Cdd:PLN02728  107 VFNGLQEVDA--NSE--LVCIHDSARPLVTSADIEKVLKdAAVHG--AAVLGVPVKATIKEANSDSFVVKTLDRKRLWEM 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2100534769 166 QTPQFFPLISLSNAIEKALAAKAVVTDEASAMEFAGYHPSLVIGSRKNLKVTEQEDLLLASIWLN 230
Cdd:PLN02728  181 QTPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILN 245
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
5-137 1.14e-09

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 55.94  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   5 RIWAVIPAAGIGSRMNSdiPKQYLKIEDKTILEYSINHFLEhSKIHKVVVALNPSDD----YWAKLPFT--DNPRVLTtn 78
Cdd:COG2068     3 KVAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALA-AGLDPVVVVLGADAEevaaALAGLGVRvvVNPDWEE-- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769  79 gGQNrvDSVLSALQ-LIRDIEGtehdwVMVHDAARPCLSSRHIDDLVHAKESSPDGAILA 137
Cdd:COG2068    78 -GMS--SSLRAGLAaLPADADA-----VLVLLGDQPLVTAETLRRLLAAFRESPASIVAP 129
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-137 2.31e-09

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 54.51  E-value: 2.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNSDipKQYLKIEDKTILEYSINHFLEHSkiHKVVVALNPSD--DYWAKLPFtdnPRVLTTNGGQNRVD 85
Cdd:pfam12804   1 AVILAGGRSSRMGGD--KALLPLGGKPLLERVLERLRPAG--DEVVVVANDEEvlAALAGLGV---PVVPDPDPGQGPLA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2100534769  86 SVLSALQLIRDiegteHDWVMVhdAA--RPCLSSRHIDDLVHAKESSPDGAILA 137
Cdd:pfam12804  74 GLLAALRAAPG-----ADAVLV--LAcdMPFLTPELLRRLLAAAEESGADIVVP 120
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-137 9.79e-09

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: 53.33  E-value: 9.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   6 IWAVIPAAGIGSRMNSdiPKQYLKIEDKTILEYSINHFLEhSKIHKVVVALNPSDD----YWAKLPFT--DNPRVLTtng 79
Cdd:cd04182     1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALA-AGLSRVIVVLGAEADavraALAGLPVVvvINPDWEE--- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2100534769  80 GQNrvDSVLSALQ-LIRDIEGtehdwVMVHDAARPCLSSRHIDDLVHAKESSPDGAILA 137
Cdd:cd04182    75 GMS--SSLAAGLEaLPADADA-----VLILLADQPLVTAETLRALIDAFREDGAGIVAP 126
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-78 5.66e-08

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 51.85  E-value: 5.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNS---DIPKQYLKIEDKTILEYSINHFLEHsKIHKVVVALNPS----DDYWAKLP---FTDNPRVLTT 77
Cdd:cd02523     1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVTGYKkeqiEELLKKYPnikFVYNPDYAET 79


                  .
gi 2100534769  78 N 78
Cdd:cd02523    80 N 80
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
8-54 1.30e-07

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 50.62  E-value: 1.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMN---SDIPKQYLKIEDKTILEYSINHFLEHSkIHKVVV 54
Cdd:COG1213     2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVV 50
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-58 1.35e-07

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: 50.27  E-value: 1.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2100534769   8 AVIPAAGIGSRMN---SDIPKQYLKIEDKTILEYSINHFLEHsKIHKVVVALNP 58
Cdd:cd04181     1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGY 53
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 8-57 2.90e-06

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 46.68  E-value: 2.90e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2100534769   8 AVIPAAGIGSRM---NSDIPKQYLKIEDKTILEYSINHfLEHSKIHKVVVALN 57
Cdd:COG1208     2 AVILAGGLGTRLrplTDTRPKPLLPVGGKPLLEHILER-LAAAGITEIVINVG 53
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 8-136 2.47e-05

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: 43.48  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNSDipKQYLKIEDKTILEYSINHFLEHsKIHKVVVALNPSDD-----YWAKLPFTdnpRVLTTNGGQN 82
Cdd:TIGR03310   2 AIILAAGLSSRMGQN--KLLLPYKGKTILEHVVDNALRL-FFDEVILVLGHEADelvalLANHSNIT---LVHNPQYAEG 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2100534769  83 RVDSVLSALQLIRDIEGtehdwVMVHDAARPCLSSRHIDDLVHAKESSPDGAIL 136
Cdd:TIGR03310  76 QSSSIKLGLELPVQSDG-----YLFLLGDQPFVTPDIIQLLLEAFALKNDEIVV 124
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-55 3.59e-05

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 43.27  E-value: 3.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2100534769   8 AVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHFLEHSKIHKVVVA 55
Cdd:cd02540     1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVV 48
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 8-57 2.13e-04

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: 40.96  E-value: 2.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2100534769   8 AVIPAAGIGSRM---NSDIPKQYLKIEDKTILEYSINHFLEHsKIHKVVVALN 57
Cdd:cd06426     1 VVIMAGGKGTRLrplTENTPKPMLKVGGKPILETIIDRFIAQ-GFRNFYISVN 52
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 8-45 2.79e-04

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 40.98  E-value: 2.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2100534769   8 AVIPAAGIGSRM---NSDIPKQYLKIEDKTILEYSINHFLE 45
Cdd:cd02541     3 AVIPAAGLGTRFlpaTKAIPKEMLPIVDKPVIQYIVEEAVA 43
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 8-135 4.87e-04

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: 39.87  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNSDipKQYLKIEDKTILEYSINHFLEHskIHKVVVALNPSDDYWAKLPFtdnPRVLTTNGGQNRVDSV 87
Cdd:cd02503     3 GVILAGGKSRRMGGD--KALLELGGKPLLEHVLERLKPL--VDEVVISANRDQERYALLGV---PVIPDEPPGKGPLAGI 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2100534769  88 LSALQLIRdiegteHDWVMVhdaaRPC----LSSRHIDDLVHAKESSPDGAI 135
Cdd:cd02503    76 LAALRAAP------ADWVLV----LACdmpfLPPELLERLLAAAEEGADAVV 117
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 8-61 7.29e-04

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: 39.47  E-value: 7.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2100534769   8 AVIPAAGIGSRM---NSDIPKQYLKIEDKTILEYSINHFLEHSkIHKVVVALNPSDD 61
Cdd:cd04189     3 GLILAGGKGTRLrplTYTRPKQLIPVAGKPIIQYAIEDLREAG-IEDIGIVVGPTGE 58
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 3-135 1.43e-03

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: 38.25  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   3 SNRIWAVIPAAGIGSRMNSDipKQYLKIEDKTILEYSINHFLEHskIHKVVVALNPSDDYWA-KLPF-TDNPrvlttnGG 80
Cdd:COG0746     2 TMPITGVILAGGRSRRMGQD--KALLPLGGRPLLERVLERLRPQ--VDEVVIVANRPERYAAlGVPVvPDDP------PG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2100534769  81 QNRVDSVLSALQLIRdiegteHDWVMVH--DAarPCLSSRHIDDLVHAKESSPDGAI 135
Cdd:COG0746    72 AGPLAGILAALEAAP------AEWVLVLacDM--PFLPPDLVRRLLEALEEGADAVV 120
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-54 2.46e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.66  E-value: 2.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2100534769   8 AVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHfLEHSKIHKVVV 54
Cdd:PRK14354    5 AIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDS-VKKAGIDKIVT 50
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
8-41 2.97e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 37.96  E-value: 2.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2100534769   8 AVIPAAGIGSRM---NSDIPKQYLKIEDKTILEYSIN 41
Cdd:PRK13389   11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVN 47
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-54 3.02e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 38.08  E-value: 3.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2100534769   8 AVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSINHfLEHSKIHKVVV 54
Cdd:COG1207     5 VVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDA-ARALGPDRIVV 50
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 8-54 3.16e-03

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 37.55  E-value: 3.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2100534769   8 AVIPAAGIGSRMNS---DIPKQYLKIEDKTILEYSINHfLEHSKIHKVVV 54
Cdd:cd06422     2 AMILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALDR-LAAAGIRRIVV 50
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
8-40 6.32e-03

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 36.99  E-value: 6.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2100534769   8 AVIPAAGIGSRMN---SDIPKQYLKIEDKTILEYSI 40
Cdd:COG1209     3 GIILAGGSGTRLRpltLTVSKQLLPVYDKPMIYYPL 38
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-52 6.65e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 37.31  E-value: 6.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2100534769   1 MSSNRIWAVIPAAGIGSRMNSDIPKQYLKIEDKTILEYSIN--HFLEHSKIHKV 52
Cdd:PRK09451    1 MLNSAMSVVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDaaNELGAQHVHLV 54
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 5-121 8.35e-03

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


Pssm-ID: 133006  Cd Length: 223  Bit Score: 36.36  E-value: 8.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100534769   5 RIWAVIPAAGiGSRmnsDIP-KQYLKIEDKTILEYSINHFLEHSKIHKVVVAlnpSDD---------YWAKLPF------ 68
Cdd:cd02513     1 KILAIIPARG-GSK---GIPgKNIRPLGGKPLIAWTIEAALESKLFDRVVVS---TDDeeiaevarkYGAEVPFlrpael 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2100534769  69 -TDNprvlTTNggqnrVDSVLSALQLIRDiEGTEHDWVMVHDAARPCLSSRHID 121
Cdd:cd02513    74 aTDT----ASS-----IDVILHALDQLEE-LGRDFDIVVLLQPTSPLRSAEDID 117
 
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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