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Conserved domains on  [gi|2527125095|ref|WP_288219123|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [uncultured Clostridium sp.]

Protein Classification

IspD/TarI family cytidylyltransferase( domain architecture ID 10118526)

IspD/TarI family cytidylyltransferase such as 2-C-methyl-d-erythritol 4-phosphate cytidylyltransferase (IspD) that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-d-erythritol from 2-C-methyl-derythritol 4-phosphate and CTP, and ribitol-5-phosphate cytidylyltransferase (TarI) that catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate

EC:  2.7.7.-
Gene Ontology:  GO:0070567
PubMed:  12691742|9445404
SCOP:  4002789

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 2-223 6.90e-99

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: 286.73  E-value: 6.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   2 NIAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKiWIRKFGLNKVRGIVNGGDT 81
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAK-ELAKYGLSKVVKIVEGGAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  82 RQESVYNAIRALDGEctEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELYL 161
Cdd:cd02516    80 RQDSVLNGLKALPDA--DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527125095 162 GQTPQSFKYKLIKEAHEVSIERQTqDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLL 223
Cdd:cd02516   158 AQTPQAFRLDLLLKAHRQASEEGE-EFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 2-223 6.90e-99

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: 286.73  E-value: 6.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   2 NIAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKiWIRKFGLNKVRGIVNGGDT 81
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAK-ELAKYGLSKVVKIVEGGAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  82 RQESVYNAIRALDGEctEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELYL 161
Cdd:cd02516    80 RQDSVLNGLKALPDA--DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527125095 162 GQTPQSFKYKLIKEAHEVSIERQTqDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLL 223
Cdd:cd02516   158 AQTPQAFRLDLLLKAHRQASEEGE-EFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-228 6.23e-98

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: 284.71  E-value: 6.23e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   5 IILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKIWIRKFGLNKVRGIVNGGDTRQE 84
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  85 SVYNAIRALDGectEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELYLGQT 164
Cdd:COG1211    81 SVRNGLEALPD---DDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQT 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527125095 165 PQSFKYKLIKEAHEVSIERQtQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLKSVIK 228
Cdd:COG1211   158 PQGFRLDLLLEAHEAAAADG-LEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLR 220
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-228 4.16e-94

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 275.09  E-value: 4.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   1 MNIAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKIWIRKFglNKVRGIVNGGD 80
Cdd:PRK00155    3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK--DPKVTVVAGGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  81 TRQESVYNAIRALDgectEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELY 160
Cdd:PRK00155   81 ERQDSVLNGLQALP----DDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLW 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527125095 161 LGQTPQSFKYKLIKEAHEvSIERQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLKSVIK 228
Cdd:PRK00155  157 AAQTPQGFRIELLREALA-RALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILK 223
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-224 6.19e-72

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: 218.31  E-value: 6.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   3 IAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKiWIRKFGlnKVRGIVNGGDTR 82
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQ-KYLVAR--AVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  83 QESVYNAIRALDGEctedDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIV-KSINNETIDTIPkRSELYL 161
Cdd:TIGR00453  78 QDSVRNGLKALKDA----EFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKrVEADGFVVETVD-REGLWA 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527125095 162 GQTPQSFKYKLIKEAHEVSiERQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLK 224
Cdd:TIGR00453 153 AQTPQAFRTELLKKALARA-KLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAE 214
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 4-222 1.76e-50

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: 163.77  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCksewQEDLKIWIRKFGLNKVRGIVNGGDTRQ 83
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAV----SPDDTPEFRQLLGDPSIQLVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  84 ESVYNAIRALDGectEDDILVIHDSARPLISQRIINENISGAKEH-GAVDTVIPSADTIVKSINNETIDTIPKRSELYLG 162
Cdd:pfam01128  77 DSVLNGLKALAG---TAKFVLVHDGARPCLPHADLARLLAALETGtQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095 163 QTPQSFKYKLIKEAHEVSiERQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLL 222
Cdd:pfam01128 154 QTPQGFRVDLLLAAHQRG-DQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLAL 212
 
Name Accession Description Interval E-value
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 2-223 6.90e-99

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: 286.73  E-value: 6.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   2 NIAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKiWIRKFGLNKVRGIVNGGDT 81
Cdd:cd02516     1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAK-ELAKYGLSKVVKIVEGGAT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  82 RQESVYNAIRALDGEctEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELYL 161
Cdd:cd02516    80 RQDSVLNGLKALPDA--DPDIVLIHDAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527125095 162 GQTPQSFKYKLIKEAHEVSIERQTqDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLL 223
Cdd:cd02516   158 AQTPQAFRLDLLLKAHRQASEEGE-EFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-228 6.23e-98

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: 284.71  E-value: 6.23e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   5 IILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKIWIRKFGLNKVRGIVNGGDTRQE 84
Cdd:COG1211     1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVAGGATRQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  85 SVYNAIRALDGectEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELYLGQT 164
Cdd:COG1211    81 SVRNGLEALPD---DDDWVLVHDAARPLVSPELIDRVIEAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQT 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527125095 165 PQSFKYKLIKEAHEVSIERQtQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLKSVIK 228
Cdd:COG1211   158 PQGFRLDLLLEAHEAAAADG-LEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLR 220
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-228 4.16e-94

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 275.09  E-value: 4.16e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   1 MNIAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKIWIRKFglNKVRGIVNGGD 80
Cdd:PRK00155    3 MVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELLLAK--DPKVTVVAGGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  81 TRQESVYNAIRALDgectEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELY 160
Cdd:PRK00155   81 ERQDSVLNGLQALP----DDDWVLVHDAARPFLTPDDIDRLIEAAEETGAAILAVPVKDTIKRSDDGGGIVDTPDRSGLW 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2527125095 161 LGQTPQSFKYKLIKEAHEvSIERQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLKSVIK 228
Cdd:PRK00155  157 AAQTPQGFRIELLREALA-RALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILK 223
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-224 6.19e-72

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: 218.31  E-value: 6.19e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   3 IAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKiWIRKFGlnKVRGIVNGGDTR 82
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQ-KYLVAR--AVPKIVAGGDTR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  83 QESVYNAIRALDGEctedDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIV-KSINNETIDTIPkRSELYL 161
Cdd:TIGR00453  78 QDSVRNGLKALKDA----EFVLVHDAARPFVPKELLDRLLEALRKAGAAILALPVADTLKrVEADGFVVETVD-REGLWA 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527125095 162 GQTPQSFKYKLIKEAHEVSiERQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLK 224
Cdd:TIGR00453 153 AQTPQAFRTELLKKALARA-KLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAE 214
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 1-227 1.04e-56

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 180.07  E-value: 1.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   1 MNIA-IILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKIWIRKFGLNKVR-GIVNG 78
Cdd:PRK13385    1 MNYElIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTQAQERKHVQDLMKQLNVADQRvEVVKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  79 GDTRQESVYNAIraldGECTEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPkRSE 158
Cdd:PRK13385   81 GTERQESVAAGL----DRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKYGAAICAVEVKDTVKRVKDKQVIETVD-RNE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2527125095 159 LYLGQTPQSFKYKLIKEAHEVSIERQtQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLKSVI 227
Cdd:PRK13385  156 LWQGQTPQAFELKILQKAHRLASEQQ-FLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAIL 223
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 4-222 1.76e-50

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: 163.77  E-value: 1.76e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCksewQEDLKIWIRKFGLNKVRGIVNGGDTRQ 83
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAV----SPDDTPEFRQLLGDPSIQLVAGGDTRQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  84 ESVYNAIRALDGectEDDILVIHDSARPLISQRIINENISGAKEH-GAVDTVIPSADTIVKSINNETIDTIPKRSELYLG 162
Cdd:pfam01128  77 DSVLNGLKALAG---TAKFVLVHDGARPCLPHADLARLLAALETGtQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095 163 QTPQSFKYKLIKEAHEVSiERQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLL 222
Cdd:pfam01128 154 QTPQGFRVDLLLAAHQRG-DQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLAL 212
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 4-223 1.69e-48

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: 163.48  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKiwiRKFGLNKVRGIVNGGDTRQ 83
Cdd:PRK09382    8 LVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMK---KALPEIKFVTLVTGGATRQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  84 ESVYNAIRALDGEcteddILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSinNETIDtipkRSELYLGQ 163
Cdd:PRK09382   85 ESVRNALEALDSE-----YVLIHDAARPFVPKELIDRLIEALDKADCVLPALPVADTLKRA--NETVD----REGLKLIQ 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095 164 TPQSFKYKLIKEAHEvsierQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLL 223
Cdd:PRK09382  154 TPQLSRTKTLKAAAD-----GRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMA 208
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 5-235 5.22e-46

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 153.35  E-value: 5.22e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   5 IILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLKiwIRKFGLNKVRGIVNGGDTRQE 84
Cdd:PLN02728   28 ILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFE--EAVENIDVPLKFALPGKERQD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  85 SVYNAIRALDGECtedDILVIHDSARPLISQRIINENISGAKEHGAVDTVIPSADTIVKSINNETIDTIPKRSELYLGQT 164
Cdd:PLN02728  106 SVFNGLQEVDANS---ELVCIHDSARPLVTSADIEKVLKDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWEMQT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527125095 165 PQSFKYKLIKEAHEVsIERQTQDATDDCQLVLALNKDVYLVNGDKLNFKITTFEDLLLLKSVIKISKIEVI 235
Cdd:PLN02728  183 PQVIKPELLRRGFEL-VEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERILNERSDAEV 252
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 4-139 1.50e-11

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 60.67  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDipKQFIDIYGKPMIIHTLESFdvNPEIDKIMVVCKsewQEDLKIWIRKFGLNKVRgivnggDTRQ 83
Cdd:pfam12804   1 AVILAGGRSSRMGGD--KALLPLGGKPLLERVLERL--RPAGDEVVVVAN---DEEVLAALAGLGVPVVP------DPDP 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527125095  84 E-----SVYNAIRALDGectEDDILVIH-DSarPLISQRIINENISGAKEHGAvDTVIPSAD 139
Cdd:pfam12804  68 GqgplaGLLAALRAAPG---ADAVLVLAcDM--PFLTPELLRRLLAAAEESGA-DIVVPVYD 123
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 4-53 3.70e-09

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: 54.43  E-value: 3.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDipKQFIDIYGKPMIIHTLESFDvnPEIDKIMVVCK 53
Cdd:COG0746     7 GVILAGGRSRRMGQD--KALLPLGGRPLLERVLERLR--PQVDEVVIVAN 52
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 4-59 4.77e-09

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: 54.12  E-value: 4.77e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2527125095   4 AIILAGGSGTRMGSDipKQFIDIYGKPMIIHTLESFDvnPEIDKIMVVCKSEWQED 59
Cdd:cd02503     3 GVILAGGKSRRMGGD--KALLELGGKPLLEHVLERLK--PLVDEVVISANRDQERY 54
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 4-130 6.75e-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: 53.72  E-value: 6.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSdiPKQFIDIYGKPMIIHTLESFdVNPEIDKIMVVCKSEwQEDLKIWIRKFGlnkVRGIVNggdTRQ 83
Cdd:cd04182     3 AIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAA-LAAGLSRVIVVLGAE-ADAVRAALAGLP---VVVVIN---PDW 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2527125095  84 E-----SVYNAIRALDGECteDDILVIH-DsaRPLISQRIINENISGAKEHGA 130
Cdd:cd04182    73 EegmssSLAAGLEALPADA--DAVLILLaD--QPLVTAETLRALIDAFREDGA 121
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-55 1.58e-08

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 53.92  E-value: 1.58e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   1 MNIAIILAGGSGTRM----GSDIPKQFIDIYG-KPMIIHTLESFDVNPEIDKIMVVCKSE 55
Cdd:COG0836     2 MIYPVILAGGSGTRLwplsRESYPKQFLPLLGeKSLLQQTVERLAGLVPPENILVVTNEE 61
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-69 8.17e-08

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 50.57  E-value: 8.17e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   1 MNIAIILAGGSGTRM-GSDipKQFIDIYGKPMIIHTLESFDvnPEIDKIMVVCKsewqEDLKIWiRKFGL 69
Cdd:PRK00317    3 PITGVILAGGRSRRMgGVD--KGLQELNGKPLIQHVIERLA--PQVDEIVINAN----RNLARY-AAFGL 63
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
4-51 1.15e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 50.54  E-value: 1.15e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2527125095   4 AIILAGGSGTRMGSdiPKQFIDIYGKPMIIHTLESFdVNPEIDKIMVV 51
Cdd:COG2068     6 AIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAA-LAAGLDPVVVV 50
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
4-51 1.47e-07

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 50.86  E-value: 1.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2527125095   4 AIILAGGSGTRM-----GsdIPKQFIDIYGKPMIIHTLESFdVNPEIDKIMVV 51
Cdd:COG1209     3 GIILAGGSGTRLrpltlT--VSKQLLPVYDKPMIYYPLSTL-MLAGIREILII 52
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-52 1.53e-07

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: 50.54  E-value: 1.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2527125095   4 AIILAGGSGTRMG---SDIPKQFIDIYGKPMIIHTLESFdVNPEIDKIMVVC 52
Cdd:COG1208     2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERL-AAAGITEIVINV 52
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-135 2.11e-07

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: 49.82  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLES-FDVNPeiDKIMVVCksewqedlkiwirKFGLNKVRGIVNGGDTR 82
Cdd:cd02540     1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAaRALGP--DRIVVVV-------------GHGAEQVKKALANPNVE 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527125095  83 ---QES-------VYNAIRALDGEctEDDILVIH-DSarPLISQRIINENISGAKEHGAVDTVI 135
Cdd:cd02540    66 fvlQEEqlgtghaVKQALPALKDF--EGDVLVLYgDV--PLITPETLQRLLEAHREAGADVTVL 125
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 4-52 2.41e-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: 49.89  E-value: 2.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2527125095   4 AIILAGGSGTRMG---SDIPKQFIDIYGKPMIIHTLESFDVNPeIDKIMVVC 52
Cdd:cd04181     1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVV 51
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-105 4.33e-07

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 49.17  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   5 IILAGGSGTR---MGSDIPKQFIDIYGKPMIIHTLESFDvNPEIDKIMVVCKSEWQEDLKIWIR-KFGLNKVRGIVNGGD 80
Cdd:cd04183     2 IIPMAGLGSRfkkAGYTYPKPLIEVDGKPMIEWVIESLA-KIFDSRFIFICRDEHNTKFHLDESlKLLAPNATVVELDGE 80

                          90       100
                  ....*....|....*....|....*..
gi 2527125095  81 TR--QESVYNAIRALDGectEDDILVI 105
Cdd:cd04183    81 TLgaACTVLLAADLIDN---DDPLLIF 104
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-51 4.36e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.83  E-value: 4.36e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDvNPEIDKIMVV 51
Cdd:PRK14354    5 AIILAAGKGTRMKSKLPKVLHKVCGKPMVEHVVDSVK-KAGIDKIVTV 51
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-77 6.17e-07

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 48.70  E-value: 6.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527125095   4 AIILAGGSGTRMG---SDIPKQFIDIYGKPMIIHTLESFDVNpEIDKIMVVCKSEwQEDLKIWIRKFGLNkVRGIVN 77
Cdd:COG1213     2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYK-AELIEEALARPGPD-VTFVYN 75
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-73 6.55e-07

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 48.42  E-value: 6.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527125095   4 AIILAGGSGTRMG---SDIPKQFIDIYGKPMIIHTLESFDVNPeIDKIMVVCKSEWQEDLKIWIRKFGLNKVR 73
Cdd:cd04198     3 AVILAGGGGSRLYpltDNIPKALLPVANKPMIWYPLDWLEKAG-FEDVIVVVPEEEQAEISTYLRSFPLNLKQ 74
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-52 1.43e-06

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: 47.63  E-value: 1.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2527125095   3 IAIILAGGSGTRM---GSDIPKQFIDIYGK-PMIIHTLESFdVNPEIDKIMVVC 52
Cdd:pfam00483   1 KAIILAGGSGTRLwplTRTLAKPLVPVGGKyPLIDYPLSRL-ANAGIREIIVIL 53
glmU TIGR01173
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This ...
 3-51 1.47e-06

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; This protein is a bifunctional enzyme, GlmU, which catalyzes last two reactions in the four-step pathway of UDP-N-acetylglucosamine biosynthesis from fructose-6-phosphate. Its reaction product is required from peptidoglycan biosynthesis, LPS biosynthesis in species with LPS, and certain other processes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]


Pssm-ID: 273482 [Multi-domain]  Cd Length: 451  Bit Score: 48.43  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2527125095   3 IAIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLES-FDVNPEidKIMVV 51
Cdd:TIGR01173   2 SVVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVIDAaRALGPQ--KIHVV 49
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-51 2.09e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 47.93  E-value: 2.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFDVNpEIDKIMVV 51
Cdd:PRK14353    8 AIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLAAAASL-GPSRVAVV 54
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 3-55 2.79e-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: 47.19  E-value: 2.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2527125095   3 IAIILAGGSGTRM----GSDIPKQFIDIYG-KPMIIHTLESFDVNPEIDKIMVVCKSE 55
Cdd:cd02509     2 YPVILAGGSGTRLwplsRESYPKQFLKLFGdKSLLQQTLDRLKGLVPPDRILVVTNEE 59
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-49 2.98e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 47.29  E-value: 2.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2527125095   1 MNIAI-ILAGGSGTRMGSDIPKQFIDIYGKPMIIHTL-ESFDVNPEIDKIM 49
Cdd:PRK14359    1 MKLSIiILAAGKGTRMKSSLPKVLHTICGKPMLFYILkEAFAISDDVHVVL 51
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
4-65 3.36e-06

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 46.18  E-value: 3.36e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDipKQFIDIYGKPMIIHTLE--------SFDVNPEIDKIMVVCKSEWQedlkiWIR 65
Cdd:PRK02726   10 ALILAGGKSSRMGQD--KALLPWQGVPLLQRVARiaaacadeVYIITPWPERYQSLLPPGCH-----WLR 72
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-40 4.50e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 47.03  E-value: 4.50e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESFD 40
Cdd:PRK14356    8 ALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRALR 44
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 3-136 5.82e-06

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 45.79  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   3 IAIILAGGSGTRMgsdIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEWQEDLkiwIRKFGLNKV--RGIVNGGD 80
Cdd:pfam02348   1 AAIIPARLGSKRL---PGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADV---AKEFGAGVVmtSGSLSSGT 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2527125095  81 TRqesVYNAIRALDGEctEDDILVIHDSARPLISQRIINENISGAKEHGAVDTVIP 136
Cdd:pfam02348  75 DR---FYEVVKAFLND--HDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTL 125
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-51 8.51e-06

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: 46.17  E-value: 8.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLES-FDVNPeiDKIMVV 51
Cdd:COG1207     5 VVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLDAaRALGP--DRIVVV 51
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-38 1.13e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.79  E-value: 1.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLES 38
Cdd:PRK09451    8 VVILAAGKGTRMYSDLPKVLHTLAGKPMVQHVIDA 42
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 4-70 1.14e-05

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 44.87  E-value: 1.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527125095   4 AIILAGGSGTRMGS---DIPKQFIDIYGKPMIIHTLESFdVNPEIDKIMVVCkSEWQEDLKIWI---RKFGLN 70
Cdd:cd04189     3 GLILAGGKGTRLRPltyTRPKQLIPVAGKPIIQYAIEDL-REAGIEDIGIVV-GPTGEEIKEALgdgSRFGVR 73
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 4-49 1.98e-05

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 44.74  E-value: 1.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2527125095   4 AIILAGGSGTRMGSdIPKQFIDIYGKPMIIHTLESFdvNPEIDKIM 49
Cdd:PRK14489    8 GVILAGGLSRRMNG-RDKALILLGGKPLIERVVDRL--RPQFARIH 50
molyb_mobA TIGR02665
molybdenum cofactor guanylyltransferase, proteobacterial; In many molybdopterin-containing ...
 4-52 2.07e-05

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: 43.81  E-value: 2.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2527125095   4 AIILAGGSGTRMGSDiPKQFIDIYGKPMIIHTLESfdVNPEIDKIMVVC 52
Cdd:TIGR02665   3 GVILAGGRARRMGGR-DKGLVELGGKPLIEHVLAR--LRPQVSDLAISA 48
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-37 2.09e-05

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 44.08  E-value: 2.09e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2527125095   4 AIILAGGSGTRMGS---DIPKQFIDIYGKPMIIHTLE 37
Cdd:cd06915     1 AVILAGGLGTRLRSvvkDLPKPLAPVAGRPFLEYLLE 37
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-61 2.39e-05

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: 44.15  E-value: 2.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527125095   4 AIILAGGSGTRMGS---DIPKQFIDIYGKPMIIHTLESFDVNpEIDKIMVVC--KSEWQEDLK 61
Cdd:cd02523     1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVTgyKKEQIEELL 62
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 4-71 2.54e-05

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 43.78  E-value: 2.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2527125095   4 AIILAGGSGTRMG---SDIPKQFIDIYGKPMIIHTLESFDVNpEIDKIMVVCKSEWQEDLKIWIRKFGLNK 71
Cdd:cd02507     3 AVVLADGFGSRFLpltSDIPKALLPVANVPLIDYTLEWLEKA-GVEEVFVVCCEHSQAIIEHLLKSKWSSL 72
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 7-70 2.78e-05

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: 43.34  E-value: 2.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2527125095   7 LAGGSGTRMGsDIPKQFIDIYGKPMIIHTLESFdVNPEIDKImVVCKSEWQEDLKIWIRKFGLN 70
Cdd:COG2266     1 MAGGKGTRLG-GGEKPLLEICGKPMIDRVIDAL-EESCIDKI-YVAVSPNTPKTREYLKERGVE 61
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 4-51 4.83e-05

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short 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 homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. 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.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 43.33  E-value: 4.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2527125095   4 AIILAGGSGTRMGS---DIPKQFIDIYGKPMIIHTLESFdVNPEIDKIMVV 51
Cdd:cd02538     3 GIILAGGSGTRLYPltkVVSKQLLPVYDKPMIYYPLSTL-MLAGIREILII 52
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-37 5.02e-05

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: 42.94  E-value: 5.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2527125095   4 AIILAGGSGTRMGS---DIPKQFIDIYGKPMIIHTLE 37
Cdd:cd06422     2 AMILAAGLGTRMRPltdTRPKPLVPVAGKPLIDHALD 38
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-51 1.17e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 42.62  E-value: 1.17e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMIIHTLESF-DVNPEidKIMVV 51
Cdd:PRK14352    7 VIVLAAGAGTRMRSDTPKVLHTLAGRSMLGHVLHAAaGLAPQ--HLVVV 53
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-32 1.36e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.42  E-value: 1.36e-04
                          10        20
                  ....*....|....*....|....*....
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMI 32
Cdd:PRK14355    6 AIILAAGKGTRMKSDLVKVMHPLAGRPMV 34
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 4-34 1.82e-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: 41.40  E-value: 1.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2527125095   4 AIILAGGSGTRMG---SDIPKQFIDIYGKPMIIH 34
Cdd:cd02524     1 VVILAGGLGTRLSeetELKPKPMVEIGGRPILWH 34
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-210 2.60e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 41.67  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   4 AIILAGGSGTRMGSDIPKQFIDIYGKPMI---IHTLESFdvnpeIDKIMVV-------CKSEWQEDLKIWIRKFGLNKVR 73
Cdd:PRK14357    3 ALVLAAGKGTRMKSKIPKVLHKISGKPMInwvIDTAKKV-----AQKVGVVlgheaelVKKLLPEWVKIFLQEEQLGTAH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095  74 GIVNGGDTRQEsvynairaldgectEDDILVIHDSArPLISQRIINENIsgaKEHgavdtvipsadtiVKSINNETIDTI 153
Cdd:PRK14357   78 AVMCARDFIEP--------------GDDLLILYGDV-PLISENTLKRLI---EEH-------------NRKGADVTILVA 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2527125095 154 PKRSELYLGQTPQ-SFKYKLIKEAhevsierqtqDATDDCQLVLALNKDVYLVNGDKL 210
Cdd:PRK14357  127 DLEDPTGYGRIIRdGGKYRIVEDK----------DAPEEEKKIKEINTGIYVFSGDFL 174
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
 5-26 6.66e-04

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 40.11  E-value: 6.66e-04
                          10        20
                  ....*....|....*....|..
gi 2527125095   5 IILAGGSGTRMGSDIPKQFIDI 26
Cdd:PTZ00339  110 LILAGGLGTRLGSDKPKGLLEC 131
UDPGlcNAc_PPase cd04193
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ...
 5-26 9.69e-04

UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.


Pssm-ID: 133036  Cd Length: 323  Bit Score: 39.51  E-value: 9.69e-04
                          10        20
                  ....*....|....*....|..
gi 2527125095   5 IILAGGSGTRMGSDIPKQFIDI 26
Cdd:cd04193    19 LLLAGGQGTRLGFDGPKGMFPV 40
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 4-67 1.36e-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: 38.73  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527125095   4 AIILAGGSGTRMGS---DIPKQFIDIYGKPMIIHTLESFdVNPEIDKImVVCKSEWQEDLKIWIRKF 67
Cdd:cd06425     3 ALILVGGYGTRLRPltlTVPKPLVEFCNKPMIEHQIEAL-AKAGVKEI-ILAVNYRPEDMVPFLKEY 67
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 1-136 1.99e-03

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


Pssm-ID: 133006  Cd Length: 223  Bit Score: 38.29  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527125095   1 MNIAIILA-GGSGtrmgsDIP-KQFIDIYGKPMIIHTLESFDVNPEIDKIMVVCKSEwqEDLKIwIRKFGLNKV--RGIV 76
Cdd:cd02513     1 KILAIIPArGGSK-----GIPgKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDE--EIAEV-ARKYGAEVPflRPAE 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2527125095  77 NGGDTRQ--ESVYNAIRALDGECTEDDILVIHDSARPLISQRIINENISGAKEHGAvDTVIP 136
Cdd:cd02513    73 LATDTASsiDVILHALDQLEELGRDFDIVVLLQPTSPLRSAEDIDEAIELLLSEGA-DSVFS 133
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-39 2.12e-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: 38.26  E-value: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2527125095   4 AIILAGGSGTRMG---SDIPKQFIDIYGKPMIIHTLESF 39
Cdd:cd06426     1 VVIMAGGKGTRLRpltENTPKPMLKVGGKPILETIIDRF 39
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-65 4.37e-03

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. 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 that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH 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 including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 37.23  E-value: 4.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2527125095   4 AIILAGG--SGTRM---GSDIPKQFIDIYGKPMIIHTLESFDVNPEIDKIMVVC----------KSEWQEDLKIWIR 65
Cdd:cd06428     1 AVILVGGpqKGTRFrplSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGfypesvfsdfISDAQQEFNVPIR 77
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 4-39 5.83e-03

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 36.96  E-value: 5.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2527125095   4 AIILAGGSGTRM---GSDIPKQFIDIYGKPMIIHTLESF 39
Cdd:PRK15480    6 GIILAGGSGTRLypvTMAVSKQLLPIYDKPMIYYPLSTL 44
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
4-21 8.41e-03

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 36.79  E-value: 8.41e-03
                          10
                  ....*....|....*...
gi 2527125095   4 AIILAGGSGTRMGSDIPK 21
Cdd:COG4284    98 VILLAGGQGTRLGFDGPK 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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