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Conserved domains on  [gi|506352014|ref|WP_015871733|]
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3-deoxy-manno-octulosonate cytidylyltransferase [Edwardsiella ictaluri]

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
 1-248 3.38e-157

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


:

Pssm-ID: 235473  Cd Length: 245  Bit Score: 436.08  E-value: 3.38e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  81 EVVELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 161 PWDRERFAvsqSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVALQAPGTGVDTPEDL 240
Cdd:PRK05450 161 PYGRDAFA---DSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237


                 ....*...
gi 506352014 241 DCVRAILA 248
Cdd:PRK05450 238 ERVRALLA 245
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-248 3.38e-157

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 436.08  E-value: 3.38e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  81 EVVELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 161 PWDRERFAvsqSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVALQAPGTGVDTPEDL 240
Cdd:PRK05450 161 PYGRDAFA---DSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237


                 ....*...
gi 506352014 241 DCVRAILA 248
Cdd:PRK05450 238 ERVRALLA 245
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-246 2.24e-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: 423.70  E-value: 2.24e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQAS-GAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  80 AEVVELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLA-RCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAeDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 159 AIPWDRERFAvsqsqIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVAlQAPGTGVDTPE 238
Cdd:COG1212  161 PIPYPRDAFA-----EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDTPE 234


                 ....*...
gi 506352014 239 DLDCVRAI 246
Cdd:COG1212  235 DLERVRAL 242
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 6-241 1.75e-136

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


Pssm-ID: 129558  Cd Length: 238  Bit Score: 383.50  E-value: 1.75e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014    6 IIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEVVEL 85
Cdd:TIGR00466   3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   86 CGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAIPWDRE 165
Cdd:TIGR00466  83 LALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFDRD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506352014  166 RFAVSQSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVALQAPGTGVDTPEDLD 241
Cdd:TIGR00466 163 FFAKRQTPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 2-246 1.21e-126

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: 358.71  E-value: 1.21e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   2 SFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQA-QASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAkKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  81 EVVELCGfADDDIIVNVQGDEPLIPPQIIRQVAENLARC-DAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAA 159
Cdd:cd02517   81 EVAEKLD-ADDDIVVNVQGDEPLIPPEMIDQVVAALKDDpGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 160 IPWDRErfavsqSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVdVALQAPGTGVDTPED 239
Cdd:cd02517  160 IPYPRD------SSEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKV-VETDHESIGVDTPED 232


                 ....*..
gi 506352014 240 LDCVRAI 246
Cdd:cd02517  233 LERVEAL 239
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-221 4.28e-89

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: 262.66  E-value: 4.28e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014    4 IAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGA-ERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   83 VELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDA-GMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEpYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506352014  162 WDRERFAvsqsQIGQTFLRHIGIYAYRAG-FIRRYVNWAPSQLEQIEMLEQLRVLWYGEKI 221
Cdd:pfam02348 161 YIREHPA----ELYYVYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-248 3.38e-157

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 436.08  E-value: 3.38e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  81 EVVELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 161 PWDRERFAvsqSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVALQAPGTGVDTPEDL 240
Cdd:PRK05450 161 PYGRDAFA---DSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237


                 ....*...
gi 506352014 241 DCVRAILA 248
Cdd:PRK05450 238 ERVRALLA 245
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-246 2.24e-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: 423.70  E-value: 2.24e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQAS-GAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  80 AEVVELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLA-RCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAeDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 159 AIPWDRERFAvsqsqIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVAlQAPGTGVDTPE 238
Cdd:COG1212  161 PIPYPRDAFA-----EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDTPE 234


                 ....*...
gi 506352014 239 DLDCVRAI 246
Cdd:COG1212  235 DLERVRAL 242
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 6-241 1.75e-136

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


Pssm-ID: 129558  Cd Length: 238  Bit Score: 383.50  E-value: 1.75e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014    6 IIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEVVEL 85
Cdd:TIGR00466   3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   86 CGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAIPWDRE 165
Cdd:TIGR00466  83 LALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFDRD 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506352014  166 RFAVSQSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVDVALQAPGTGVDTPEDLD 241
Cdd:TIGR00466 163 FFAKRQTPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 2-246 1.21e-126

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: 358.71  E-value: 1.21e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   2 SFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQA-QASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAkKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  81 EVVELCGfADDDIIVNVQGDEPLIPPQIIRQVAENLARC-DAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAA 159
Cdd:cd02517   81 EVAEKLD-ADDDIVVNVQGDEPLIPPEMIDQVVAALKDDpGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 160 IPWDRErfavsqSQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVdVALQAPGTGVDTPED 239
Cdd:cd02517  160 IPYPRD------SSEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKV-VETDHESIGVDTPED 232


                 ....*..
gi 506352014 240 LDCVRAI 246
Cdd:cd02517  233 LERVEAL 239
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-247 2.24e-99

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 289.56  E-value: 2.24e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQ-AQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERL 79
Cdd:PRK13368   1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERaAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  80 AEVVELcgfADDDIIVNVQGDEPLIPPQIIRQVAEN-LARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRA 158
Cdd:PRK13368  81 AEVMLK---IEADIYINVQGDEPMIRPRDIDTLIQPmLDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 159 AIPWDRE-RFAVSqsqigqtfLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVdVALQAPGTGVDTP 237
Cdd:PRK13368 158 PIPSRRDgESARY--------LKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRM-VEVAATSIGVDTP 228

                        250
                 ....*....|
gi 506352014 238 EDLDCVRAIL 247
Cdd:PRK13368 229 EDLERVRAIM 238
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-221 4.28e-89

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: 262.66  E-value: 4.28e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014    4 IAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGA-ERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   83 VELCGFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDA-GMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEpYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506352014  162 WDRERFAvsqsQIGQTFLRHIGIYAYRAG-FIRRYVNWAPSQLEQIEMLEQLRVLWYGEKI 221
Cdd:pfam02348 161 YIREHPA----ELYYVYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
PLN02917 PLN02917
CMP-KDO synthetase
 4-250 2.34e-54

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 176.95  E-value: 2.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   4 IAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQ-ASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEV 82
Cdd:PLN02917  49 VGIIPARFASSRFEGKPLVHILGKPMIQRTWERAKlATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  83 VELCGfADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAEAFNPNAVKVVRDSQGYALYFSRAAIPW 162
Cdd:PLN02917 129 LKKLE-KKYDIVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGLIPY 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 163 DRERFAVSQSqigqTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMLEQLRVLWYGEKIHVdVALQAPGTGVDTPEDLDC 242
Cdd:PLN02917 208 NKSGKVNPQF----PYLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKV-IKVDHEAHGVDTPEDVEK 282


                 ....*...
gi 506352014 243 VRAILASQ 250
Cdd:PLN02917 283 IEALMRER 290
SpsF COG1861
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ...
 1-248 3.11e-19

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


Pssm-ID: 441466  Cd Length: 245  Bit Score: 83.71  E-value: 3.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQAS-GAERVIVAT-----DHPDVQHAvLQAGGEVCmtRADHNS 74
Cdd:COG1861    2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSkLIDEVVVATttdpaDDPLVDLA-KELGVPVF--RGSEDD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  75 GTERLAEVVElcgFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVP--IHD--AAEAFNPNAVKvvrdsqg 150
Cdd:COG1861   79 VLSRYYQAAE---AYGADVVVRITGDCPLIDPALIDELIAAFLESGADYVSNSLPrtYPRglDVEVFSFAALE------- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 151 YAlyFSRAAIPWDRErfavsqsqigqtflrHIGIYAYRAGFIRRYVNWAPSqleqiEMLEQLRVlwygekihvdvalqap 230
Cdd:COG1861  149 RA--WEEAKLPSERE---------------HVTPYIYEHPDRFRIGNVEPP-----EDLSDLRL---------------- 190

                        250
                 ....*....|....*...
gi 506352014 231 gTgVDTPEDLDCVRAILA 248
Cdd:COG1861  191 -T-VDTPEDLELIRAIYE 206
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 2-247 2.93e-17

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: 77.96  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   2 SFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGA-ERVIVATDHPDVQHAVLQAGGEVCMTR----ADHNSGT 76
Cdd:cd02513    1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLfDRVVVSTDDEEIAEVARKYGAEVPFLRpaelATDTASS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  77 ER-LAEVVELCG--FADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHdaaeaFNPNAVKVVRDSQGYAL 153
Cdd:cd02513   81 IDvILHALDQLEelGRDFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFH-----RFPWRALGLDDNGLEPV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014 154 YFSraaiPWDRERfavSQsQIGQTFLRHIGIYAYRAGFIRRYVNWAPSQLEQIEMleqlrvlwyGEKIHVDvalqapgtg 233
Cdd:cd02513  156 NYP----EDKRTR---RQ-DLPPAYHENGAIYIAKREALLESNSFFGGKTGPYEM---------PRERSID--------- 209

                        250
                 ....*....|....
gi 506352014 234 VDTPEDLDCVRAIL 247
Cdd:cd02513  210 IDTEEDFELAEALL 223
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-149 4.91e-15

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 71.73  E-value: 4.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQAQASGA-ERVIVATDHPDVQHAVLQAGGEVCMtRADHNSG-TER 78
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLfDRVVVSTDDEEIAEVAREYGAEVFL-RPAELAGdTAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  79 LAEVV-------ELCGFaDDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIH------------DAAEAFNP 139
Cdd:COG1083   80 TIDVIlhalewlEEQGE-EFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHhppywalkldedGRLEPLNP 158

                        170
                 ....*....|
gi 506352014 140 NAVKVVRdSQ 149
Cdd:COG1083  159 DPHNRPR-RQ 167
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 4-143 8.82e-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: 71.06  E-value: 8.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   4 IAIIPSRYASTRLPGKPLADIAGKPMVVHVMAQA-QASGAERVIVAT-----DHPDVQHAvLQAGgeVCMTRADHNSGTE 77
Cdd:cd02518    1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLkRSKLIDEIVIATstneeDDPLEALA-KKLG--VKVFRGSEEDVLG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  78 RLAEVVElcgFADDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAV----PIHDAAEAFNPNAVK 143
Cdd:cd02518   78 RYYQAAE---EYNADVVVRITGDCPLIDPEIIDAVIRLFLKSGADYTSNTLprtyPDGLDVEVFTRDALE 144
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-127 3.71e-12

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 65.27  E-value: 3.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTR----LPgKPLADIAGKPMVVHVMAQAQASGAERVIVAT--DHPDVQHAVLQAGGEVCMTRADHNS 74
Cdd:PRK14353   4 RTCLAIILAAGEGTRmkssLP-KVLHPVAGRPMLAHVLAAAASLGPSRVAVVVgpGAEAVAAAAAKIAPDAEIFVQKERL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 506352014  75 GTER--LAEVVELCGFADDDIIVNvqGDEPLIPPQIIRQVAENLARcDAGMATLA 127
Cdd:PRK14353  83 GTAHavLAAREALAGGYGDVLVLY--GDTPLITAETLARLRERLAD-GADVVVLG 134
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 14-130 1.04e-11

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: 61.83  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  14 TRL--PGKPLADIAGKPMVVHVMAQAQASGAERVIVAT--DHPDVQHAVLQAGGEVCMTradhnSGT---ERLAEVVELC 86
Cdd:COG2266    7 TRLggGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVspNTPKTREYLKERGVEVIET-----PGEgyvEDLNEALESI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 506352014  87 gfadDDIIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPI 130
Cdd:COG2266   82 ----SGPVLVVPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPA 121
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 14-150 8.90e-09

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: 54.06  E-value: 8.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  14 TR----LPgKPLADIAGKPMVVHVMAQAQASGAERVIV-----------ATDHPDVQ-----------HAVLQAggevcm 67
Cdd:cd02540   10 TRmksdLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVvvghgaeqvkkALANPNVEfvlqeeqlgtgHAVKQA------ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  68 tradhnsgterlaevVELCGFADDDIIVnVQGDEPLIPPQIIRQVAENLARCDAGMATLavpihdAAEAFNPNAV-KVVR 146
Cdd:cd02540   83 ---------------LPALKDFEGDVLV-LYGDVPLITPETLQRLLEAHREAGADVTVL------TAELEDPTGYgRIIR 140


                 ....
gi 506352014 147 DSQG 150
Cdd:cd02540  141 DGNG 144
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 15-150 5.70e-08

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: 52.72  E-value: 5.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  15 RLPgKPLADIAGKPMVVHVMAQAQASGAERVIV-----------ATDHPDVQ-----------HAVLQAggevcmtradh 72
Cdd:COG1207   19 KLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVvvghgaeqvraALADLDVEfvlqeeqlgtgHAVQQA----------- 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506352014  73 nsgterlaevVELCGFADDDIIVnVQGDEPLIPPQIIRQVAENLARCDAGMATLavpihdAAEAFNPNAV-KVVRDSQG 150
Cdd:COG1207   87 ----------LPALPGDDGTVLV-LYGDVPLIRAETLKALLAAHRAAGAAATVL------TAELDDPTGYgRIVRDEDG 148
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
12-132 3.19e-07

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.39  E-value: 3.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  12 ASTRLPG-KPLADIAGKPMVVHVMAQAQASGAERVIVAT--DHPDVQHAVLQAGGEVCmtradHNSGTER-----LAEVV 83
Cdd:COG2068   13 ASSRMGRpKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgaDAEEVAAALAGLGVRVV-----VNPDWEEgmsssLRAGL 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 506352014  84 ELCGFADDDIIVNVqGDEPLIPPQIIRQVaenLARCDAGMATLAVPIHD 132
Cdd:COG2068   88 AALPADADAVLVLL-GDQPLVTAETLRRL---LAAFRESPASIVAPTYD 132
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 16-150 1.13e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 49.21  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  16 LPgKPLADIAGKPMVVHVMAQAQASGAERVIVATDHPDVQHAVLQAGGEVCMTRADHNSGT-ERLAEVVELCGFADDDII 94
Cdd:PRK14358  25 LP-KVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAFARQEQQLGTgDAFLSGASALTEGDADIL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 506352014  95 VnVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPIHDAAeafnpNAVKVVRDSQG 150
Cdd:PRK14358 104 V-LYGDTPLLRPDTLRALVADHRAQGSAMTILTGELPDAT-----GYGRIVRGADG 153
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 12-124 2.64e-06

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: 46.40  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  12 ASTRLPG-KPLADIAGKPMVVHVMAQAQASGAERVIVAT-DHPDVQHAVLQAGGEVCMTRADHNSG-TERLAEVVELCGF 88
Cdd:cd04182   10 RSSRMGGnKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgAEADAVRAALAGLPVVVVINPDWEEGmSSSLAAGLEALPA 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 506352014  89 ADDDIIVNVqGDEPLIPPQIIRQVAENLARCDAGMA 124
Cdd:cd04182   90 DADAVLILL-ADQPLVTAETLRALIDAFREDGAGIV 124
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 12-132 4.01e-06

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: 45.65  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   12 ASTRLPG-KPLADIAGKPMVVHVMAQAQASGaERVIVATDHPDVQHAVLQAGGEVCMTRADHN---SGterLAEVVELCG 87
Cdd:pfam12804   8 RSSRMGGdKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLGVPVVPDPDPGQgplAG---LLAALRAAP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 506352014   88 FADDDIIVNVqgDEPLIPPQIIRQVAENLARCDAGmatLAVPIHD 132
Cdd:pfam12804  84 GADAVLVLAC--DMPFLTPELLRRLLAAAEESGAD---IVVPVYD 123
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 16-128 2.25e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.02  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  16 LPgKPLADIAGKPMVVHVMAQAQASGAERVivatdhpdvqHAVLQAGGEVCMTR-ADHNSG----TERL----AEVVELC 86
Cdd:PRK09451  23 LP-KVLHTLAGKPMVQHVIDAANELGAQHV----------HLVYGHGGDLLKQTlADEPLNwvlqAEQLgtghAMQQAAP 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 506352014  87 GFADDDIIVNVQGDEPLIPPQIIRQVAEnlARCDAGMATLAV 128
Cdd:PRK09451  92 FFADDEDILMLYGDVPLISVETLQRLRD--AKPQGGIGLLTV 131
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 19-132 1.33e-04

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: 42.04  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  19 KPLADIAGKPMVVHVMAQAQASGA-ERVIVAT---DHPDVQHAVLQ----------AGGEvcmTRADhnsgTERLA-EVV 83
Cdd:COG1211   17 KQFLPLGGKPVLEHTLEAFLAHPRiDEIVVVVppdDIEYFEELLAKygidkpvrvvAGGA---TRQD----SVRNGlEAL 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 506352014  84 ElcgfADDDIIVnVQ-GDEPLIPPQIIRQVAENLARCDAgmATLAVPIHD 132
Cdd:COG1211   90 P----DDDDWVL-VHdAARPLVSPELIDRVIEAAREYGA--AIPALPVTD 132
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 19-51 1.63e-04

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: 41.68  E-value: 1.63e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 506352014  19 KPLADIAGKPMVVHVMAQAQASGAERVIVATDH 51
Cdd:COG1208   22 KPLLPVGGKPLLEHILERLAAAGITEIVINVGY 54
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-150 3.23e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.36  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   1 MSFIAIIPSRYASTR----LPgKPLADIAGKPMVVHVMAQAQASGAERVIVATDH--PDVQ------------------- 55
Cdd:PRK14354   1 MNRYAIILAAGKGTRmkskLP-KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHgaEEVKevlgdrsefalqeeqlgtg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  56 HAVLQAGgevcmtradhnsgterlaevvELCGFADDDIIVnVQGDEPLIPPQIIRQVAENlaRCDAG-MATLAvpihdAA 134
Cdd:PRK14354  80 HAVMQAE---------------------EFLADKEGTTLV-ICGDTPLITAETLKNLIDF--HEEHKaAATIL-----TA 130

                        170
                 ....*....|....*..
gi 506352014 135 EAFNPNAV-KVVRDSQG 150
Cdd:PRK14354 131 IAENPTGYgRIIRNENG 147
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 19-61 1.16e-03

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 39.09  E-value: 1.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 506352014  19 KPLADIAGKPMVVHVMAQAQASGAERVIVATDH-PDVQHAVLQA 61
Cdd:cd06422   22 KPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHlADQIEAHLGD 65
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-196 1.77e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014   5 AIIPSRYASTRLPG---KPLADIAGKPMVVHVMAQAQASGAERVIVATDH-PDVQHAVLQAGGEVCMTRADHNSGTER-- 78
Cdd:PRK14355   6 AIILAAGKGTRMKSdlvKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHqAEKVREHFAGDGDVSFALQEEQLGTGHav 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  79 LAEVVELCGFADDDIIVNvqGDEPLIPPQIIRQVAENLARCDAGMATLavpihdAAEAFNPNAV-KVVRDSQGYALYF-- 155
Cdd:PRK14355  86 ACAAPALDGFSGTVLILC--GDVPLLRAETLQGMLAAHRATGAAVTVL------TARLENPFGYgRIVRDADGRVLRIve 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 506352014 156 SRAAIPWDRERFAVSQsqigqtflrhiGIYAYRAGFIRRYV 196
Cdd:PRK14355 158 EKDATPEERSIREVNS-----------GIYCVEAAFLFDAI 187
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 19-114 1.91e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 39.15  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  19 KPLADIAGKPMVVHVMAQAQASGAER--VIVATDHPDVQHAVLQAGGEVCMTRADHNSGTERLAEVV--ELCGFADDDII 94
Cdd:PRK14352  24 KVLHTLAGRSMLGHVLHAAAGLAPQHlvVVVGHDRERVAPAVAELAPEVDIAVQDEQPGTGHAVQCAleALPADFDGTVV 103

                         90       100
                 ....*....|....*....|
gi 506352014  95 VnVQGDEPLIPPQIIRQVAE 114
Cdd:PRK14352 104 V-TAGDVPLLDGETLADLVA 122
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 19-153 3.21e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.55  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506352014  19 KPLADIAGKPMVVHVMAQAQA-----------SGAERVIVATDHPD----VQ-------HAVLQAGGEVCMTRADHnsgt 76
Cdd:PRK14356  25 KVLQTLLGEPMLRFVYRALRPlfgdnvwtvvgHRADMVRAAFPDEDarfvLQeqqlgtgHALQCAWPSLTAAGLDR---- 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506352014  77 erlaevvelcgfadddiIVNVQGDEPLIPPQIIRQVAENLARCDAGMATLAVPihdaaeafNPNAV-KVVR-DSQGYAL 153
Cdd:PRK14356 101 -----------------VLVVNGDTPLVTTDTIDDFLKEAAGADLAFMTLTLP--------DPGAYgRVVRrNGHVAAI 154
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-51 4.22e-03

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: 37.56  E-value: 4.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 506352014   5 AIIPSRYASTRL-------PgKPLADIAGKPMVVHVMAQAQASGAERVIVATDH 51
Cdd:cd04181    1 AVILAAGKGTRLrpltdtrP-KPLLPIAGKPILEYIIERLARAGIDEIILVVGY 53
 
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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