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Conserved domains on  [gi|515624436|ref|WP_017057036|]
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MULTISPECIES: 3-deoxy-manno-octulosonate cytidylyltransferase [Vibrio]

Protein Classification

3-deoxy-manno-octulosonate cytidylyltransferase family protein( domain architecture ID 10012410)

3-deoxy-manno-octulosonate cytidylyltransferase family protein similar to 3-deoxy-manno-octulosonate cytidylyltransferase that catalyzes the activation of 3-deoxy-D-manno-octulosonate (or 2-keto-3-deoxy-manno-octonic acid; KDO) by forming CMP-KDO, and 8-amino-3,8-dideoxy-manno-octulosonate cytidylyltransferase that activates KDO8N (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in the Shewanella genus

CATH:  3.90.550.10
EC:  2.7.7.-
Gene Ontology:  GO:0009103|GO:0008690
PubMed:  9445404|12691742
SCOP:  4002789

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
1-247 1.04e-156

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


:

Pssm-ID: 235473  Cd Length: 245  Bit Score: 434.54  E-value: 1.04e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  81 EVIEVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 161 PWDRDAYANngtAAESPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVDVAMEAPSAGVDTLEDL 240
Cdd:PRK05450 161 PYGRDAFAD---SAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237

                 ....*..
gi 515624436 241 EAVRAII 247
Cdd:PRK05450 238 ERVRALL 244
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
1-247 1.04e-156

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 434.54  E-value: 1.04e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  81 EVIEVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 161 PWDRDAYANngtAAESPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVDVAMEAPSAGVDTLEDL 240
Cdd:PRK05450 161 PYGRDAFAD---SAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237

                 ....*..
gi 515624436 241 EAVRAII 247
Cdd:PRK05450 238 ERVRALL 244
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
1-246 8.63e-152

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 422.16  E-value: 8.63e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKA-GADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  80 AEVIEVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLA-NSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAeDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 159 TIPWDRDAYANNGtaaesPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVDVAmEAPSAGVDTLE 238
Cdd:COG1212  161 PIPYPRDAFAEDG-----PYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDTPE 234

                 ....*...
gi 515624436 239 DLEAVRAI 246
Cdd:COG1212  235 DLERVRAL 242
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
2-246 1.28e-133

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 376.04  E-value: 1.28e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   2 SYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKA-GADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  81 EVIEVMNIPDDhIIVNVQGDEPLIPPAIINQVANNLANS-TAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRAT 159
Cdd:cd02517   81 EVAEKLDADDD-IVVNVQGDEPLIPPEMIDQVVAALKDDpGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 160 IPWDRDAYANngtaaeSPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVdVAMEAPSAGVDTLED 239
Cdd:cd02517  160 IPYPRDSSED------FPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKV-VETDHESIGVDTPED 232

                 ....*..
gi 515624436 240 LEAVRAI 246
Cdd:cd02517  233 LERVEAL 239
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
4-241 4.48e-123

3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129558  Cd Length: 238  Bit Score: 349.60  E-value: 4.48e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436    4 TVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLAEVI 83
Cdd:TIGR00466   1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   84 EVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATIPWD 163
Cdd:TIGR00466  81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624436  164 RDAYANNGTAAESPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVDVAMEAPSAGVDTLEDLE 241
Cdd:TIGR00466 161 RDFFAKRQTPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
4-221 2.44e-80

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: 240.32  E-value: 2.44e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436    4 TVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGA-DNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   83 IEVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLANSTAP-MATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPyMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624436  162 WDRDAYANNGTaaesPLLRHIGIYAYRAG-FINTYINWEPSTLERIECLEQLRVLWYGEKI 221
Cdd:pfam02348 161 YIREHPAELYY----VYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
1-247 1.04e-156

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 434.54  E-value: 1.04e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  81 EVIEVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 161 PWDRDAYANngtAAESPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVDVAMEAPSAGVDTLEDL 240
Cdd:PRK05450 161 PYGRDAFAD---SAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237

                 ....*..
gi 515624436 241 EAVRAII 247
Cdd:PRK05450 238 ERVRALL 244
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
1-246 8.63e-152

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 422.16  E-value: 8.63e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKA-GADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  80 AEVIEVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLA-NSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAeDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 159 TIPWDRDAYANNGtaaesPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVDVAmEAPSAGVDTLE 238
Cdd:COG1212  161 PIPYPRDAFAEDG-----PYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDTPE 234

                 ....*...
gi 515624436 239 DLEAVRAI 246
Cdd:COG1212  235 DLERVRAL 242
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
2-246 1.28e-133

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 376.04  E-value: 1.28e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   2 SYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKA-GADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  81 EVIEVMNIPDDhIIVNVQGDEPLIPPAIINQVANNLANS-TAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRAT 159
Cdd:cd02517   81 EVAEKLDADDD-IVVNVQGDEPLIPPEMIDQVVAALKDDpGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 160 IPWDRDAYANngtaaeSPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVdVAMEAPSAGVDTLED 239
Cdd:cd02517  160 IPYPRDSSED------FPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKV-VETDHESIGVDTPED 232

                 ....*..
gi 515624436 240 LEAVRAI 246
Cdd:cd02517  233 LERVEAL 239
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
4-241 4.48e-123

3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 129558  Cd Length: 238  Bit Score: 349.60  E-value: 4.48e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436    4 TVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLAEVI 83
Cdd:TIGR00466   1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   84 EVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATIPWD 163
Cdd:TIGR00466  81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515624436  164 RDAYANNGTAAESPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVDVAMEAPSAGVDTLEDLE 241
Cdd:TIGR00466 161 RDFFAKRQTPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
1-246 1.08e-103

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 300.34  E-value: 1.08e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQ-SMKAGADNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERL 79
Cdd:PRK13368   1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERaAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  80 AEVIEVMnipDDHIIVNVQGDEPLIPPAIINQVANN-LANSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRA 158
Cdd:PRK13368  81 AEVMLKI---EADIYINVQGDEPMIRPRDIDTLIQPmLDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 159 TIPWDRDAYANNGtaaesplLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVdVAMEAPSAGVDTLE 238
Cdd:PRK13368 158 PIPSRRDGESARY-------LKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRM-VEVAATSIGVDTPE 229

                 ....*...
gi 515624436 239 DLEAVRAI 246
Cdd:PRK13368 230 DLERVRAI 237
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
4-221 2.44e-80

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: 240.32  E-value: 2.44e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436    4 TVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGA-DNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   83 IEVMNIPDDHIIVNVQGDEPLIPPAIINQVANNLANSTAP-MATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPyMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624436  162 WDRDAYANNGTaaesPLLRHIGIYAYRAG-FINTYINWEPSTLERIECLEQLRVLWYGEKI 221
Cdd:pfam02348 161 YIREHPAELYY----VYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
PLN02917 PLN02917
CMP-KDO synthetase
6-247 4.43e-63

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 198.91  E-value: 4.43e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   6 VIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGA-DNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERLAEVIE 84
Cdd:PLN02917  51 IIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTlDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  85 VMNIPDDhIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHADEVFNPNAVKVVTDKDGYALYFSRATIPWDR 164
Cdd:PLN02917 131 KLEKKYD-IVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGLIPYNK 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 165 DAYANngtaAESPLLRHIGIYAYRAGFINTYINWEPSTLERIECLEQLRVLWYGEKIHVdVAMEAPSAGVDTLEDLEAVR 244
Cdd:PLN02917 210 SGKVN----PQFPYLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKV-IKVDHEAHGVDTPEDVEKIE 284

                 ...
gi 515624436 245 AII 247
Cdd:PLN02917 285 ALM 287
SpsF COG1861
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ...
1-247 1.56e-19

Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441466  Cd Length: 245  Bit Score: 84.48  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKA-GADNVIIAT----DDARVEKAVKAFGATVCMTSPNhDSg 75
Cdd:COG1861    2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSkLIDEVVVATttdpADDPLVDLAKELGVPVFRGSED-DV- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  76 TERLAEVIEVMNiPDdhIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHAD----EVfnpnavkvvtdkdgy 151
Cdd:COG1861   80 LSRYYQAAEAYG-AD--VVVRITGDCPLIDPALIDELIAAFLESGADYVSNSLPRTYPRgldvEV--------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 152 alyFSRATIpwdRDAYANngtaAESPLLR-HIGIYAYRAG--FINTYINWEPStleriecLEQLRVLwygekihvdvame 228
Cdd:COG1861  142 ---FSFAAL---ERAWEE----AKLPSEReHVTPYIYEHPdrFRIGNVEPPED-------LSDLRLT------------- 191
                        250
                 ....*....|....*....
gi 515624436 229 apsagVDTLEDLEAVRAII 247
Cdd:COG1861  192 -----VDTPEDLELIRAIY 205
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
4-143 4.95e-15

SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.


Pssm-ID: 133011  Cd Length: 233  Bit Score: 71.83  E-value: 4.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   4 TVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKA-GADNVIIAT----DDARVEKAVKAFGATVCMTSPNhDSgTER 78
Cdd:cd02518    1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSkLIDEIVIATstneEDDPLEALAKKLGVKVFRGSEE-DV-LGR 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515624436  79 LAEVIEvMNIPDdhIIVNVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHAD----EVFNPNAVK 143
Cdd:cd02518   79 YYQAAE-EYNAD--VVVRITGDCPLIDPEIIDAVIRLFLKSGADYTSNTLPRTYPDgldvEVFTRDALE 144
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
1-124 4.46e-14

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 69.03  E-value: 4.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGA-DNVIIATDDARVEKAVKAFGATVCMTSPNHDSGTERL 79
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLfDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTAST 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515624436  80 AEVI-------EVMNIPDDHIIVnVQGDEPLIPPAIINQVANNLANSTAPMA 124
Cdd:COG1083   81 IDVIlhalewlEEQGEEFDYVVL-LQPTSPLRTAEDIDEAIELLLESGADSV 131
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
2-121 1.69e-13

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: 67.56  E-value: 1.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   2 SYTVVIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGA-DNVIIATDDARVEKAVKAFGATVC-MTSPNHDSGTERL 79
Cdd:cd02513    1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLfDRVVVSTDDEEIAEVARKYGAEVPfLRPAELATDTASS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515624436  80 AEVI-EVMN-IPDDH----IIVNVQGDEPLIPPAIINQVANNLANSTA 121
Cdd:cd02513   81 IDVIlHALDqLEELGrdfdIVVLLQPTSPLRSAEDIDEAIELLLSEGA 128
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-124 2.73e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 57.86  E-value: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSRLPG-KPLADIGGKPMIQWVYEQSMKAGADNVIIAT--DDARVEKAVKAFGATVCmTSPNHDSG-T 76
Cdd:COG2068    2 SKVAAIILAAGASSRMGRpKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgaDAEEVAAALAGLGVRVV-VNPDWEEGmS 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515624436  77 ERLAEVIEVMNIPDDHIIVNVqGDEPLIPPAIINQVANNLANSTAPMA 124
Cdd:COG2068   81 SSLRAGLAALPADADAVLVLL-GDQPLVTAETLRRLLAAFRESPASIV 127
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
14-130 1.77e-09

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: 55.66  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  14 SRL--PGKPLADIGGKPMIQWVYEQSMKAGADNVIIATDDA--RVEKAVKAFGATVCMTspnhdSGTERLAEVIEVMNIP 89
Cdd:COG2266    7 TRLggGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNtpKTREYLKERGVEVIET-----PGEGYVEDLNEALESI 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 515624436  90 DDHIIVnVQGDEPLIPPAIINQVANNLANSTAPMATLGVEI 130
Cdd:COG2266   82 SGPVLV-VPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPA 121
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
6-124 4.64e-09

pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci.


Pssm-ID: 274660  Cd Length: 222  Bit Score: 55.03  E-value: 4.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436    6 VIPARYQSSRLPGKPLADIGGKPMIQWVYEQSMKAGA-DNVIIATDDARVEKAVKAFGATVCMTSP-----NHDSGTERL 79
Cdd:TIGR03584   3 IIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLfDKVVVSTDDEEIAEVAKSYGASVPFLRPkeladDFTGTAPVV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 515624436   80 AEVIEVM--NIPDDHIIVnVQGDEPLIPPAIINQVANNLANSTAPMA 124
Cdd:TIGR03584  83 KHAIEELklQKQYDHACC-IYATAPFLQAKILKEAFELLKQPNAHFV 128
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
12-139 4.66e-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: 51.04  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   12 QSSRLPG-KPLADIGGKPMIQWVYEQsMKAGADNVIIATDDARVEKAVKAFGATVCmtsPNHDSGTERLAEVIEVM-NIP 89
Cdd:pfam12804   8 RSSRMGGdKALLPLGGKPLLERVLER-LRPAGDEVVVVANDEEVLAALAGLGVPVV---PDPDPGQGPLAGLLAALrAAP 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 515624436   90 D-DHIIVnVQGDEPLIPPAIINQVANNLANSTAPMATLgveiTHADEVFNP 139
Cdd:pfam12804  84 GaDAVLV-LACDMPFLTPELLRRLLAAAEESGADIVVP----VYDGGRGHP 129
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
14-150 2.07e-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: 50.21  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  14 SRLPgKPLADIGGKPMIQWVYEQSMKAGADNVIIAT--DDARVEKAVKAFGATVCMTSPNhdSGTER-LAEVIEVMNIPD 90
Cdd:cd02540   14 SDLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVghGAEQVKKALANPNVEFVLQEEQ--LGTGHaVKQALPALKDFE 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515624436  91 DHIIVnVQGDEPLIPPAIINQVANNLANSTAPMATLGVEIThadevfNPNAV-KVVTDKDG 150
Cdd:cd02540   91 GDVLV-LYGDVPLITPETLQRLLEAHREAGADVTVLTAELE------DPTGYgRIIRDGNG 144
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
4-124 3.86e-07

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 48.71  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   4 TVVIPARYQSSRLPG-KPLADIGGKPMIQWVYEQSMKAGADNVIIAT--DDARVEKAVKAFGATVCmTSPNHDSG-TERL 79
Cdd:cd04182    2 AAIILAAGRSSRMGGnKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgaEADAVRAALAGLPVVVV-INPDWEEGmSSSL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515624436  80 AEVIEVMNIPDDHIIVNVqGDEPLIPPAIINQVANNLANSTAPMA 124
Cdd:cd04182   81 AAGLEALPADADAVLILL-ADQPLVTAETLRALIDAFREDGAGIV 124
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-248 1.26e-06

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 47.93  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   5 VVIPARYQSSRL-------PgKPLADIGGKPMIQWVYEQSMKAGADNVIIAT---DDArVEKAVKAFGATV-CMTSPNHD 73
Cdd:COG1213    2 AVILAAGRGSRLgpltddiP-KCLVEIGGKTLLERQLEALAAAGIKDIVVVTgykAEL-IEEALARPGPDVtFVYNPDYD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  74 SgTERLAEVIEVMN-IPDDHIIVNvqGDepLI-PPAIINQVannLANSTAPMATLGVEITHADEvfnpNAVKVVTDKDGY 151
Cdd:COG1213   80 E-TNNIYSLWLAREaLDEDFLLLN--GD--VVfDPAILKRL---LASDGDIVLLVDRKWEKPLD----EEVKVRVDEDGR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436 152 ALYFSRaTIPwdrdayaNNGTAAESpllrhIGIYAYRAGFINTYINWepstLERIECLEQLRvLWY----------GEKI 221
Cdd:COG1213  148 IVEIGK-KLP-------PEEADGEY-----IGIFKFSAEGAAALREA----LEALIDEGGPN-LYYedalqelideGGPV 209
                        250       260       270
                 ....*....|....*....|....*....|..
gi 515624436 222 H-VDV----AMEapsagVDTLEDLEAVRAIIG 248
Cdd:COG1213  210 KaVDIgglpWVE-----IDTPEDLERAEELFA 236
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
12-122 9.40e-05

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: 41.79  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  12 QSSRLPG-KPLADIGGKPMIQWVYEQSMKAGADNVIIATDDarvEKAVKAFGATVCMTSPNhDSGTerLAEVIEVMN-IP 89
Cdd:cd02503   10 KSRRMGGdKALLELGGKPLLEHVLERLKPLVDEVVISANRD---QERYALLGVPVIPDEPP-GKGP--LAGILAALRaAP 83
                         90       100       110
                 ....*....|....*....|....*....|...
gi 515624436  90 DDHIIVnVQGDEPLIPPAIINQVANNLANSTAP 122
Cdd:cd02503   84 ADWVLV-LACDMPFLPPELLERLLAAAEEGADA 115
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
5-133 1.10e-04

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.04  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   5 VVIPARYQSSR----LPgKPLADIGGKPMIQWVYEQSMKAGADNVIIATDDA--RVEKAVKAFGATVCMTSPNHDSGTER 78
Cdd:PRK14358  10 VVILAAGQGTRmksaLP-KVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGaeQVEAALQGSGVAFARQEQQLGTGDAF 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515624436  79 LAEViEVMNIPDDHIIVnVQGDEPLIPPAIINQVANNLANSTAPMATLGVEITHA 133
Cdd:PRK14358  89 LSGA-SALTEGDADILV-LYGDTPLLRPDTLRALVADHRAQGSAMTILTGELPDA 141
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
14-130 3.21e-04

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: 41.55  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436  14 SRLPgKPLADIGGKPMIQWVYEQSMKAGADNVIIAT--DDARVEKAVKAFGATVCMTSPNHdsGTER-LAEVIEVMNIPD 90
Cdd:COG1207   18 SKLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVghGAEQVRAALADLDVEFVLQEEQL--GTGHaVQQALPALPGDD 94
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515624436  91 DHIIVnVQGDEPLIPPAIINQVANNLANSTAPMATLGVEI 130
Cdd:COG1207   95 GTVLV-LYGDVPLIRAETLKALLAAHRAAGAAATVLTAEL 133
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
5-49 8.54e-04

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 39.49  E-value: 8.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515624436   5 VVIPARYQSSRL-------PgKPLADIGGKPMIQWVYEQSMKAGADNVIIAT 49
Cdd:cd04181    1 AVILAAGKGTRLrpltdtrP-KPLLPIAGKPILEYIIERLARAGIDEIILVV 51
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
12-65 1.23e-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: 1.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515624436  12 QSSRLPG-KPLADIGGKPMIQWVYEQsMKAGADNVIIAtddARVEKAVKAFGATV 65
Cdd:COG0746   14 RSRRMGQdKALLPLGGRPLLERVLER-LRPQVDEVVIV---ANRPERYAALGVPV 64
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
4-125 1.27e-03

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 38.63  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   4 TVVIPARYQSSRLPG--KPLADIGGKPMIQWVYEQSMKAGADNVIIATDDArveKAVKAFGATVCMTSPNHDSGTerLAE 81
Cdd:PRK00317   5 TGVILAGGRSRRMGGvdKGLQELNGKPLIQHVIERLAPQVDEIVINANRNL---ARYAAFGLPVIPDSLADFPGP--LAG 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515624436  82 VIEVMNIPD-DHIIVnVQGDEPLIPPAIINQVANNLANSTAPMAT 125
Cdd:PRK00317  80 ILAGLKQARtEWVLV-VPCDTPFIPPDLVARLAQAAGKDDADVAW 123
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
19-49 5.79e-03

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: 37.05  E-value: 5.79e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 515624436  19 KPLADIGGKPMIQWVYEQSMKAGADNVIIAT 49
Cdd:COG1208   22 KPLLPVGGKPLLEHILERLAAAGITEIVINV 52
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-129 6.62e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.15  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624436   1 MSYTVVIPARYQSSR----LPgKPLADIGGKPMIQWVYEQSMKAGADNVIIAT--DDARVEKAVKAFG--ATVCMTSPNH 72
Cdd:PRK14353   4 RTCLAIILAAGEGTRmkssLP-KVLHPVAGRPMLAHVLAAAASLGPSRVAVVVgpGAEAVAAAAAKIApdAEIFVQKERL 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515624436  73 DSGTERLAEVIEVMNIPDDHIIVNvqGDEPLIPPAIINQVANNLANSTApMATLGVE 129
Cdd:PRK14353  83 GTAHAVLAAREALAGGYGDVLVLY--GDTPLITAETLARLRERLADGAD-VVVLGFR 136
 
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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