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Conserved domains on  [gi|499385827|ref|WP_011073294|]
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2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Shewanella oneidensis]

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;
23-249 1.03e-120

D-ribitol-5-phosphate cytidylyltransferase;


:

Pssm-ID: 234670  Cd Length: 227  Bit Score: 342.88  E-value: 1.03e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  23 SSNVVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPED-ADFYALPQAKHPKLKTVIGGS 101
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 102 ERANSVLAALDKAPDNSWALVHDAARPCLMASDIDKLLTSRVQFpQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHAL 181
Cdd:PRK00155  81 ERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAAQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499385827 182 TPQLFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFLMRAKA 249
Cdd:PRK00155 160 TPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
23-249 1.03e-120

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 342.88  E-value: 1.03e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  23 SSNVVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPED-ADFYALPQAKHPKLKTVIGGS 101
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 102 ERANSVLAALDKAPDNSWALVHDAARPCLMASDIDKLLTSRVQFpQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHAL 181
Cdd:PRK00155  81 ERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAAQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499385827 182 TPQLFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFLMRAKA 249
Cdd:PRK00155 160 TPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 29-249 6.35e-100

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: 290.11  E-value: 6.35e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  29 IVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAK---HPKLKTVIGGSERAN 105
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKygiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 106 SVLAALDKAP-DNSWALVHDAARPCLMASDIDKLLtSRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHALTPQ 184
Cdd:COG1211   81 SVRNGLEALPdDDDWVLVHDAARPLVSPELIDRVI-EAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499385827 185 LFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFLMRAKA 249
Cdd:COG1211  160 GFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 27-244 2.72e-89

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: 262.99  E-value: 2.72e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827   27 VAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAKHPKLKTVIGGSERANS 106
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  107 VLAALDKAPDNSWALVHDAARPCLMASDIDKLLtSRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHALTPQLF 186
Cdd:TIGR00453  81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLL-EALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTPQAF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499385827  187 PTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFL 244
Cdd:TIGR00453 160 RTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 26-240 4.26e-87

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: 257.45  E-value: 4.26e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  26 VVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAK--HPKLKTVIGGSER 103
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYglSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 104 ANSVLAALD--KAPDNSWALVHDAARPCLMASDIDKLLTsRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHAL 181
Cdd:cd02516   81 QDSVLNGLKalPDADPDIVLIHDAARPFVSPELIDRLID-ALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499385827 182 TPQLFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELA 240
Cdd:cd02516  160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 28-246 2.05e-81

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: 243.13  E-value: 2.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827   28 AIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDAD-FYALPQakHPKLKTVIGGSERANS 106
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPeFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  107 VLAALDK-APDNSWALVHDAARPCLMASDIDKLLTSRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHALTPQL 185
Cdd:pfam01128  79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTPQG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499385827  186 FPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFLMR 246
Cdd:pfam01128 159 FRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
 
Name Accession Description Interval E-value
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
23-249 1.03e-120

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 342.88  E-value: 1.03e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  23 SSNVVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPED-ADFYALPQAKHPKLKTVIGGS 101
Cdd:PRK00155   1 MMMVYAIIPAAGKGSRMGADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVVPPDDrPDFAELLLAKDPKVTVVAGGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 102 ERANSVLAALDKAPDNSWALVHDAARPCLMASDIDKLLTSRVQFpQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHAL 181
Cdd:PRK00155  81 ERQDSVLNGLQALPDDDWVLVHDAARPFLTPDDIDRLIEAAEET-GAAILAVPVKDTIKRSDDGGGIVDTPDRSGLWAAQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499385827 182 TPQLFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFLMRAKA 249
Cdd:PRK00155 160 TPQGFRIELLREALARALAEGKTITDDASAVERLGKPVRLVEGRYDNIKITTPEDLALAEAILKRRIA 227
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 29-249 6.35e-100

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: 290.11  E-value: 6.35e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  29 IVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAK---HPKLKTVIGGSERAN 105
Cdd:COG1211    1 IIPAAGSGSRMGAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKygiDKPVRVVAGGATRQD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 106 SVLAALDKAP-DNSWALVHDAARPCLMASDIDKLLtSRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHALTPQ 184
Cdd:COG1211   81 SVRNGLEALPdDDDWVLVHDAARPLVSPELIDRVI-EAAREYGAAIPALPVTDTIKRVDDDGRVTETVDRSGLWAAQTPQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499385827 185 LFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFLMRAKA 249
Cdd:COG1211  160 GFRLDLLLEAHEAAAADGLEFTDDASLVERLGLPVRLVEGSEDNIKITTPEDLALAEALLRSRER 224
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 27-244 2.72e-89

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: 262.99  E-value: 2.72e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827   27 VAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAKHPKLKTVIGGSERANS 106
Cdd:TIGR00453   1 SAVIPAAGRGTRFGSGVPKQYLELGGRPLLEHALDAFLAHPAIDEVVVVVSPDDTEFFQKYLVARAVPKIVAGGDTRQDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  107 VLAALDKAPDNSWALVHDAARPCLMASDIDKLLtSRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHALTPQLF 186
Cdd:TIGR00453  81 VRNGLKALKDAEFVLVHDAARPFVPKELLDRLL-EALRKAGAAILALPVADTLKRVEADGFVVETVDREGLWAAQTPQAF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 499385827  187 PTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFL 244
Cdd:TIGR00453 160 RTELLKKALARAKLEGFEITDDASAVEKLGGKVQLVEGDALNFKITTPEDLALAEALL 217
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 26-240 4.26e-87

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: 257.45  E-value: 4.26e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  26 VVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAK--HPKLKTVIGGSER 103
Cdd:cd02516    1 VAAIILAAGSGSRMGADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYglSKVVKIVEGGATR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 104 ANSVLAALD--KAPDNSWALVHDAARPCLMASDIDKLLTsRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHAL 181
Cdd:cd02516   81 QDSVLNGLKalPDADPDIVLIHDAARPFVSPELIDRLID-ALKEYGAAIPAVPVTDTIKRVDDDGVVVETLDREKLWAAQ 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499385827 182 TPQLFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELA 240
Cdd:cd02516  160 TPQAFRLDLLLKAHRQASEEGEEFTDDASLVEAAGGKVALVEGSEDNIKITTPEDLALA 218
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 28-246 2.05e-81

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: 243.13  E-value: 2.05e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827   28 AIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDAD-FYALPQakHPKLKTVIGGSERANS 106
Cdd:pfam01128   1 AVIPAAGSGKRMGAGVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVVAVSPDDTPeFRQLLG--DPSIQLVAGGDTRQDS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  107 VLAALDK-APDNSWALVHDAARPCLMASDIDKLLTSRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHALTPQL 185
Cdd:pfam01128  79 VLNGLKAlAGTAKFVLVHDGARPCLPHADLARLLAALETGTQGAILALPVTDTIKRVEADGVVAGTPDRSGLWAAQTPQG 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499385827  186 FPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFLMR 246
Cdd:pfam01128 159 FRVDLLLAAHQRGDQPGAEITDDASLVEHAGGSVQVVPGRPDNLKITTPEDLALAEAILTR 219
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 24-244 1.89e-55

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: 181.97  E-value: 1.89e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  24 SNVVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAKHPKLKTVIGGSER 103
Cdd:PRK09382   4 SDISLVIVAAGRSTRFSAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPDDIAYMKKALPEIKFVTLVTGGATR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 104 ANSVLAALdKAPDNSWALVHDAARPCLMASDIDKLLTSRVQFPqGAILAMPVRDTMKRAnslgeiNSTVCRDNLWHALTP 183
Cdd:PRK09382  84 QESVRNAL-EALDSEYVLIHDAARPFVPKELIDRLIEALDKAD-CVLPALPVADTLKRA------NETVDREGLKLIQTP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499385827 184 QLFPTSLlrlhLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFL 244
Cdd:PRK09382 156 QLSRTKT----LKAAADGRGDFTDDSSAAEAAGGKVALVEGSEDLHKLTYKEDLKMADLLL 212
PLN02728 PLN02728
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
 24-244 5.28e-40

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


Pssm-ID: 215387  Cd Length: 252  Bit Score: 138.33  E-value: 5.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  24 SNVVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPQAKHPK-LKTVIGGSE 102
Cdd:PLN02728  23 KSVSVILLAGGVGKRMGANMPKQYLPLLGQPIALYSLYTFARMPEVKEIVVVCDPSYRDVFEEAVENIDVpLKFALPGKE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 103 RANSVLAALDKAPDNS-WALVHDAARPCLMASDIDKLLtSRVQFPQGAILAMPVRDTMKRANSLGEINSTVCRDNLWHAL 181
Cdd:PLN02728 103 RQDSVFNGLQEVDANSeLVCIHDSARPLVTSADIEKVL-KDAAVHGAAVLGVPVKATIKEANSDSFVVKTLDRKRLWEMQ 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499385827 182 TPQLFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFL 244
Cdd:PLN02728 182 TPQVIKPELLRRGFELVEREGLEVTDDVSIVEALKHPVFITEGSYTNIKVTTPDDMLVAERIL 244
PRK13385 PRK13385
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Provisional
 25-244 4.58e-36

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


Pssm-ID: 184017  Cd Length: 230  Bit Score: 127.68  E-value: 4.58e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  25 NVVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVAL------HPEDAdFYALPQAKHpKLKTVI 98
Cdd:PRK13385   2 NYELIFLAAGQGKRMNAPLNKMWLDLVGEPIFIHALRPFLADNRCSKIIIVTqaqerkHVQDL-MKQLNVADQ-RVEVVK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  99 GGSERANSVLAALDKAPDNSWALVHDAARPCLMASDIDKLLTSRVQFpQGAILAMPVRDTMKRANSlGEINSTVCRDNLW 178
Cdd:PRK13385  80 GGTERQESVAAGLDRIGNEDVILVHDGARPFLTQDIIDRLLEGVAKY-GAAICAVEVKDTVKRVKD-KQVIETVDRNELW 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499385827 179 HALTPQLFPTSLLRLHLQGALNAGAVVTDEASAMEWAGISPGLVAGRADNIKVTHPDDLELAELFL 244
Cdd:PRK13385 158 QGQTPQAFELKILQKAHRLASEQQFLGTDEASLVERSPHPVKLVQGSYYNIKLTTPEDMPLAKAIL 223
matur_MocA_YgfJ TIGR03310
molybdenum cofactor cytidylyltransferase; Members of this protein include MocA, which ...
 28-151 4.10e-11

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: 60.05  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827   28 AIVPAAGIGSRMgaGKPKQYLPLLGQSILAHTLDKLLSHpLISQVIVALHPEdADFYALPQAKHPKLKTVI------GGS 101
Cdd:TIGR03310   2 AIILAAGLSSRM--GQNKLLLPYKGKTILEHVVDNALRL-FFDEVILVLGHE-ADELVALLANHSNITLVHnpqyaeGQS 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 499385827  102 EranSVLAALDKAPDNSWALVHDAARPCLMASDIDKLLTSRVQFPQGAIL 151
Cdd:TIGR03310  78 S---SIKLGLELPVQSDGYLFLLGDQPFVTPDIIQLLLEAFALKNDEIVV 124
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
23-153 7.06e-11

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 59.79  E-value: 7.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  23 SSNVVAIVPAAGIGSRMGAgkPKQYLPLLGQSILAHTLDKLLSHPLiSQVIVALHPEDADfyALPQAKHPKLKTVIggSE 102
Cdd:COG2068    1 MSKVAAIILAAGASSRMGR--PKLLLPLGGKPLLERAVEAALAAGL-DPVVVVLGADAEE--VAAALAGLGVRVVV--NP 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499385827 103 RAN-----SVLAALDKAPDNSWA-LVHDAARPCLMASDIDKLLTSRVQFPQGAILAM 153
Cdd:COG2068   74 DWEegmssSLRAGLAALPADADAvLVLLGDQPLVTAETLRRLLAAFRESPASIVAPT 130
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 26-153 3.13e-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: 54.87  E-value: 3.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  26 VVAIVPAAGIGSRMGAgkPKQYLPLLGQSILAHTLDKLLSHPLiSQVIVALHPEDadfyALPQAKHPKLKTVIGGSERAN 105
Cdd:cd04182    1 IAAIILAAGRSSRMGG--NKLLLPLDGKPLLRHALDAALAAGL-SRVIVVLGAEA----DAVRAALAGLPVVVVINPDWE 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499385827 106 -----SVLAALDKAPDNSwalvhDAA------RPCLMASDIDKLLTSRVQFPQGAILAM 153
Cdd:cd04182   74 egmssSLAAGLEALPADA-----DAVlilladQPLVTAETLRALIDAFREDGAGIVAPV 127
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 28-152 3.94e-08

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: 51.43  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827   28 AIVPAAGIGSRMGagKPKQYLPLLGQSILAHTLDKLLSHPliSQVIVALHPEDadfyALPQAKHPKLKTVIGGSERAN-- 105
Cdd:pfam12804   1 AVILAGGRSSRMG--GDKALLPLGGKPLLERVLERLRPAG--DEVVVVANDEE----VLAALAGLGVPVVPDPDPGQGpl 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499385827  106 -SVLAALDKAPDNSWALVHDAARPCLMASDIDKLLTSRVQFPQGAILA 152
Cdd:pfam12804  73 aGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIVVP 120
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
28-97 3.73e-07

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 49.47  E-value: 3.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499385827  28 AIVPAAGIGSRMG---AGKPKQYLPLLGQSILAHTLDKLLSHPlISQVIVALHPEDADFYALPQAKHPKLKTV 97
Cdd:COG1213    2 AVILAAGRGSRLGpltDDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVVVTGYKAELIEEALARPGPDVTFV 73
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 28-158 1.24e-06

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: 47.96  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  28 AIVPAAGIGSRMG---AGKPKQYLPLLGQSILAHTLDKLLSHPlISQVIVALHPEDA---DFYALPQAKHPKLKTVIGGS 101
Cdd:cd04181    1 AVILAAGKGTRLRpltDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYLGEqieEYFGDGSKFGVNIEYVVQEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827 102 ER--ANSVLAALDKAPDNSWALVH-DAarpcLMASDIDKLLtsRVQFPQGAILAMPVRDT 158
Cdd:cd04181   80 PLgtAGAVRNAEDFLGDDDFLVVNgDV----LTDLDLSELL--RFHREKGADATIAVKEV 133
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 28-98 2.89e-06

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: 46.84  E-value: 2.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499385827  28 AIVPAAGIGSRMGA---GKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDADFYALPqaKHPKLKTVI 98
Cdd:cd02523    1 AIILAAGRGSRLRPlteDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLK--KYPNIKFVY 72
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 28-77 1.21e-05

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: 45.14  E-value: 1.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499385827  28 AIVPAAGIGSRMG---AGKPKQYLPLLGQSILAHTLDKLLSHPlISQVIVALH 77
Cdd:COG1208    2 AVILAGGLGTRLRpltDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVG 53
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 26-75 4.13e-04

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: 40.64  E-value: 4.13e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499385827  26 VVAIVPAAGIGSRM----GAGKPKQYLPLLG-QSILAHTLDKLLSHPLISQVIVA 75
Cdd:cd02509    1 IYPVILAGGSGTRLwplsRESYPKQFLKLFGdKSLLQQTLDRLKGLVPPDRILVV 55
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 28-83 5.75e-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: 40.24  E-value: 5.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499385827  28 AIVPAAGIGSRMG---AGKPKQYLPLLGQSILAHTLDKLLSHPlISQVIVALHPEDADF 83
Cdd:cd04189    3 GLILAGGKGTRLRpltYTRPKQLIPVAGKPIIQYAIEDLREAG-IEDIGIVVGPTGEEI 60
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 25-74 6.39e-04

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 39.76  E-value: 6.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499385827  25 NVVAIVPAAGiGSRmgaGKP-KQYLPLLGQSILAHTLDKLLSHPLISQVIV 74
Cdd:COG1083    2 KILAIIPARG-GSK---GIPgKNIRPLAGKPLIAYSIEAALKSGLFDRVVV 48
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-91 9.14e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.09  E-value: 9.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499385827  28 AIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLlsHPLISQVI--VALHPEDADFYALPQAKH 91
Cdd:PRK14356   8 ALILAAGKGTRMHSDKPKVLQTLLGEPMLRFVYRAL--RPLFGDNVwtVVGHRADMVRAAFPDEDA 71
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 28-87 1.27e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 38.71  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  28 AIVPAAGIGSRMGAgkPKQYLPLLGQSILAHTLDKLLshPLISQVIVALHPEDADFYALP 87
Cdd:cd02503    3 GVILAGGKSRRMGG--DKALLELGGKPLLEHVLERLK--PLVDEVVISANRDQERYALLG 58
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 23-157 1.45e-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: 38.63  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  23 SSNVVAIVPAAGIGSRMGAGKPKqyLPLLGQSILAHTLDKLlsHPLISQV-IVALHPEDADFYALPQAK-HPKLKTVIGG 100
Cdd:COG0746    2 TMPITGVILAGGRSRRMGQDKAL--LPLGGRPLLERVLERL--RPQVDEVvIVANRPERYAALGVPVVPdDPPGAGPLAG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499385827 101 seransVLAALDKAPDNSWALVhdaarPC----LMASDIDKLLTsrvQFPQGAILAMPVRD 157
Cdd:COG0746   78 ------ILAALEAAPAEWVLVL-----ACdmpfLPPDLVRRLLE---ALEEGADAVVPRSG 124
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 28-81 1.79e-03

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: 38.65  E-value: 1.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499385827  28 AIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDKLLSHPLISQVIVALHPEDA 81
Cdd:cd02540    1 AVILAAGKGTRMKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQ 54
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 28-77 2.47e-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: 37.94  E-value: 2.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 499385827  28 AIVPAAGIGSRMG---AGKPKQYLPLLGQSILAHTLDKLLSHPlISQVIVALH 77
Cdd:cd06422    2 AMILAAGLGTRMRpltDTRPKPLVPVAGKPLIDHALDRLAAAG-IRRIVVNTH 53
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 29-113 5.19e-03

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: 37.23  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  29 IVPAAGIGSR---MGAGKPKQYLPLLGQSILAHTLDKlLSHPLISQVIVALHPEDADFYALPQAK---HPKLKTVI---- 98
Cdd:cd04183    2 IIPMAGLGSRfkkAGYTYPKPLIEVDGKPMIEWVIES-LAKIFDSRFIFICRDEHNTKFHLDESLkllAPNATVVEldge 80

                         90
                 ....*....|....*.
gi 499385827  99 -GGSerANSVLAALDK 113
Cdd:cd04183   81 tLGA--ACTVLLAADL 94
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 24-61 5.68e-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: 37.70  E-value: 5.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499385827  24 SNVVAIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLD 61
Cdd:COG1207    1 SPLAVVILAAGKGTRMKSKLPKVLHPLAGKPMLEHVLD 38
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 25-74 5.68e-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: 37.13  E-value: 5.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499385827  25 NVVAIVPAAGiGSRmgaGKP-KQYLPLLGQSILAHTLDKLLSHPLISQVIV 74
Cdd:cd02513    1 KILAIIPARG-GSK---GIPgKNIRPLGGKPLIAWTIEAALESKLFDRVVV 47
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-112 6.50e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.53  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499385827  28 AIVPAAGIGSRMGAGKPKQYLPLLGQSILAHTLDkLLSHPLISQVIVALHPEDADFYALPQAKHPKLKTVIgGSER---A 104
Cdd:PRK14353   8 AIILAAGEGTRMKSSLPKVLHPVAGRPMLAHVLA-AAASLGPSRVAVVVGPGAEAVAAAAAKIAPDAEIFV-QKERlgtA 85


                 ....*...
gi 499385827 105 NSVLAALD 112
Cdd:PRK14353  86 HAVLAARE 93
 
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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