NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|556426074|ref|WP_023311001|]
View 

MULTISPECIES: 3-deoxy-manno-octulosonate cytidylyltransferase [Enterobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-248 3.08e-161

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


:

Pssm-ID: 235473  Cd Length: 245  Bit Score: 446.10  E-value: 3.08e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  81 EVVEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 161 PWDRDRFAlskETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVASEVPGTGVDTPEDL 240
Cdd:PRK05450 161 PYGRDAFA---DSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237


                 ....*...
gi 556426074 241 ERVRAELR 248
Cdd:PRK05450 238 ERVRALLA 245
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-248 3.08e-161

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 446.10  E-value: 3.08e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  81 EVVEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 161 PWDRDRFAlskETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVASEVPGTGVDTPEDL 240
Cdd:PRK05450 161 PYGRDAFA---DSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237


                 ....*...
gi 556426074 241 ERVRAELR 248
Cdd:PRK05450 238 ERVRALLA 245
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-245 4.77e-157

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: 435.26  E-value: 4.77e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARES-GADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  80 AEVVEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQR-QVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDpEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 159 TIPWDRDRFAlsketIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVAsEVPGTGVDTPE 238
Cdd:COG1212  161 PIPYPRDAFA-----EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDTPE 234


                 ....*..
gi 556426074 239 DLERVRA 245
Cdd:COG1212  235 DLERVRA 241
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 4-241 4.07e-154

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


Pssm-ID: 129558  Cd Length: 238  Bit Score: 428.18  E-value: 4.07e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074    4 VVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLAEVV 83
Cdd:TIGR00466   1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   84 EKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATIPWD 163
Cdd:TIGR00466  81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426074  164 RDRFALSKETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVASEVPGTGVDTPEDLE 241
Cdd:TIGR00466 161 RDFFAKRQTPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 2-245 6.35e-132

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: 371.81  E-value: 6.35e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   2 SFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARES-GADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  81 EVVEKCGFSDDtVIVNVQGDEPMIPAVIIRQVAENLAQ-RQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRAT 159
Cdd:cd02517   81 EVAEKLDADDD-IVVNVQGDEPLIPPEMIDQVVAALKDdPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 160 IPWDRDrfalskETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVASEVPgTGVDTPED 239
Cdd:cd02517  160 IPYPRD------SSEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHES-IGVDTPED 232


                 ....*.
gi 556426074 240 LERVRA 245
Cdd:cd02517  233 LERVEA 238
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-221 3.27e-94

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: 275.37  E-value: 3.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074    4 VVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGA-DRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   83 VEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQ-VGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGePYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426074  162 WDRDRFALsketIGDTFLRHIGIYGYRAG-FIRRYVTWAPSPLEHIEMLEQLRVLWYGEKI 221
Cdd:pfam02348 161 YIREHPAE----LYYVYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-248 3.08e-161

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 446.10  E-value: 3.08e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  81 EVVEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 161 PWDRDRFAlskETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVASEVPGTGVDTPEDL 240
Cdd:PRK05450 161 PYGRDAFA---DSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPEDL 237


                 ....*...
gi 556426074 241 ERVRAELR 248
Cdd:PRK05450 238 ERVRALLA 245
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-245 4.77e-157

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: 435.26  E-value: 4.77e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARES-GADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  80 AEVVEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQR-QVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDpEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 159 TIPWDRDRFAlsketIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVAsEVPGTGVDTPE 238
Cdd:COG1212  161 PIPYPRDAFA-----EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDTPE 234


                 ....*..
gi 556426074 239 DLERVRA 245
Cdd:COG1212  235 DLERVRA 241
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 4-241 4.07e-154

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


Pssm-ID: 129558  Cd Length: 238  Bit Score: 428.18  E-value: 4.07e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074    4 VVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLAEVV 83
Cdd:TIGR00466   1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   84 EKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATIPWD 163
Cdd:TIGR00466  81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556426074  164 RDRFALSKETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVASEVPGTGVDTPEDLE 241
Cdd:TIGR00466 161 RDFFAKRQTPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 2-245 6.35e-132

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: 371.81  E-value: 6.35e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   2 SFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARES-GADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  81 EVVEKCGFSDDtVIVNVQGDEPMIPAVIIRQVAENLAQ-RQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRAT 159
Cdd:cd02517   81 EVAEKLDADDD-IVVNVQGDEPLIPPEMIDQVVAALKDdPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 160 IPWDRDrfalskETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVAVASEVPgTGVDTPED 239
Cdd:cd02517  160 IPYPRD------SSEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHES-IGVDTPED 232


                 ....*.
gi 556426074 240 LERVRA 245
Cdd:cd02517  233 LERVEA 238
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-247 1.95e-100

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 292.25  E-value: 1.95e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARES-GADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERL 79
Cdd:PRK13368   1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAaGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  80 AEVVEKCgfsDDTVIVNVQGDEPMIPAVIIRQVAEN-LAQRQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRA 158
Cdd:PRK13368  81 AEVMLKI---EADIYINVQGDEPMIRPRDIDTLIQPmLDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 159 TIPWDRDrfalskeTIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHvAVASEVPGTGVDTPE 238
Cdd:PRK13368 158 PIPSRRD-------GESARYLKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIR-MVEVAATSIGVDTPE 229


                 ....*....
gi 556426074 239 DLERVRAEL 247
Cdd:PRK13368 230 DLERVRAIM 238
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-221 3.27e-94

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: 275.37  E-value: 3.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074    4 VVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGA-DRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   83 VEKCGFSDDTVIVNVQGDEPMIPAVIIRQVAENLAQRQ-VGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGePYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556426074  162 WDRDRFALsketIGDTFLRHIGIYGYRAG-FIRRYVTWAPSPLEHIEMLEQLRVLWYGEKI 221
Cdd:pfam02348 161 YIREHPAE----LYYVYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
PLN02917 PLN02917
CMP-KDO synthetase
 4-248 8.01e-59

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 188.12  E-value: 8.01e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   4 VVIIPARYASTRLPGKPLVDINGKPMIVHVLERAR-ESGADRVIVATDHPDVARAVEAAGGEVCMTRADHQSGTERLAEV 82
Cdd:PLN02917  49 VGIIPARFASSRFEGKPLVHILGKPMIQRTWERAKlATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  83 VEKCGFSDDtVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHHAEEAFNPNAVKVVMDAEGYALYFSRATIPW 162
Cdd:PLN02917 129 LKKLEKKYD-IVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGLIPY 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 163 DRdrfalsKETIGDTF--LRHIGIYGYRAGFIRRYVTWAPSPLEHIEMLEQLRVLWYGEKIHVaVASEVPGTGVDTPEDL 240
Cdd:PLN02917 208 NK------SGKVNPQFpyLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKV-IKVDHEAHGVDTPEDV 280


                 ....*...
gi 556426074 241 ERVRAELR 248
Cdd:PLN02917 281 EKIEALMR 288
SpsF COG1861
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ...
 1-245 1.15e-18

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


Pssm-ID: 441466  Cd Length: 245  Bit Score: 81.79  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARES-GADRVIVAT-DHPD---VARAVEAAGGEVCmtRADHQSG 75
Cdd:COG1861    2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSkLIDEVVVATtTDPAddpLVDLAKELGVPVF--RGSEDDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  76 TERLAEVVEKcgFSDDtVIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVP--IHHAeeafnpnavkvvMDAEGyal 153
Cdd:COG1861   80 LSRYYQAAEA--YGAD-VVVRITGDCPLIDPALIDELIAAFLESGADYVSNSLPrtYPRG------------LDVEV--- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 154 yFSRATIPWdrdrfaLSKETIgDTFLR-HIGIYGYRAG--FIRRYVTWAPSplehiemLEQLRVlwygekihvavasevp 230
Cdd:COG1861  142 -FSFAALER------AWEEAK-LPSEReHVTPYIYEHPdrFRIGNVEPPED-------LSDLRL---------------- 190

                        250
                 ....*....|....*
gi 556426074 231 gTgVDTPEDLERVRA 245
Cdd:COG1861  191 -T-VDTPEDLELIRA 203
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 2-132 1.26e-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: 78.73  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   2 SFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGA-DRVIVATDHPDVARAVEAAGGEVCMTR----ADHQSGT 76
Cdd:cd02513    1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLfDRVVVSTDDEEIAEVARKYGAEVPFLRpaelATDTASS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  77 ERL----AEVVEKCGFSDDTViVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHH 132
Cdd:cd02513   81 IDVilhaLDQLEELGRDFDIV-VLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHR 139
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-132 1.22e-16

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 75.97  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGA-DRVIVATDHPDVARAVEAAGGEVCM----TRADHQSG 75
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLfDRVVVSTDDEEIAEVAREYGAEVFLrpaeLAGDTAST 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556426074  76 TERLAEVVEKCGFSDDT--VIVNVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPIHH 132
Cdd:COG1083   81 IDVILHALEWLEEQGEEfdYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHH 139
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 4-112 7.20e-16

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: 74.15  E-value: 7.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   4 VVIIPARYASTRLPGKPLVDINGKPMIVHVLERARES-GADRVIVAT--DHPDVARAVEAAGGEVCMTRADHQSGTERLA 80
Cdd:cd02518    1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSkLIDEIVIATstNEEDDPLEALAKKLGVKVFRGSEEDVLGRYY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 556426074  81 EVVEKcgFSDDtVIVNVQGDEPMIPAVIIRQV 112
Cdd:cd02518   81 QAAEE--YNAD-VVVRITGDCPLIDPEIIDAV 109
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 14-130 3.50e-12

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: 62.98  E-value: 3.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  14 TRL--PGKPLVDINGKPMIVHVLERARESGADRVIVAT--DHPDVARAVEAAGGEVCMTradhqSGT---ERLAEVVEKC 86
Cdd:COG2266    7 TRLggGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVspNTPKTREYLKERGVEVIET-----PGEgyvEDLNEALESI 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 556426074  87 gfsDDTVIVnVQGDEPMIPAVIIRQVAENLAQRQVGMATLAVPI 130
Cdd:COG2266   82 ---SGPVLV-VPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPA 121
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 4-133 5.08e-12

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: 63.51  E-value: 5.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074    4 VVIIPARYASTRLPGKPLVDINGKPMIVHVLERARESGA-DRVIVATDHPDVARAVEAAGGEVCMTRA-----DHQSGTE 77
Cdd:TIGR03584   1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLfDKVVVSTDDEEIAEVAKSYGASVPFLRPkeladDFTGTAP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556426074   78 RLAEVVE--KCGFSDDTVIVnVQGDEPMIPAVIIRQVAENLAQRQV----GMATLAVPIHHA 133
Cdd:TIGR03584  81 VVKHAIEelKLQKQYDHACC-IYATAPFLQAKILKEAFELLKQPNAhfvfSVTSFAFPIQRA 141
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-246 2.84e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 57.86  E-value: 2.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRLPG-KPLVDINGKPMIVHVLERARESGADRVIVAT--DHPDVARAVEAAGGEVCMTrADHQSG-T 76
Cdd:COG2068    2 SKVAAIILAAGASSRMGRpKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgaDAEEVAAALAGLGVRVVVN-PDWEEGmS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  77 ERLAEVVEKCGFSDDTVIVNVqGDEPMIPAVIIRQVAENLAQRQvgmATLAVPIHHaeeafnpnavkvvmDAEGYALYFS 156
Cdd:COG2068   81 SSLRAGLAALPADADAVLVLL-GDQPLVTAETLRRLLAAFRESP---ASIVAPTYD--------------GRRGHPVLFS 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 157 RATIPwdrdrfALSKETiGDTFLRHIgiygyragfIRRYvtwaPSPLEHIEMlEQLRVLWygekihvavasevpgtGVDT 236
Cdd:COG2068  143 RRLFP------ELLALT-GDQGARAL---------LRRH----PDRVRLVPV-DDPGVLL----------------DIDT 185

                        250
                 ....*....|
gi 556426074 237 PEDLERVRAE 246
Cdd:COG2068  186 PEDLARLLAR 195
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 12-134 2.23e-09

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 54.89  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   12 ASTRLPG-KPLVDINGKPMIVHVLERARESGaDRVIVATDHPDVARAVEAAGGEVCMTRADHQ---SGterLAEVVEKCG 87
Cdd:pfam12804   8 RSSRMGGdKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGLGVPVVPDPDPGQgplAG---LLAALRAAP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 556426074   88 FSDDTVIVNVqgDEPMIPAVIIRQVAENLAQRQvgmATLAVPIHHAE 134
Cdd:pfam12804  84 GADAVLVLAC--DMPFLTPELLRRLLAAAEESG---ADIVVPVYDGG 125
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-128 2.56e-09

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 56.79  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTR----LPgKPLVDINGKPMIVHVLERARESGADRVIVAT--DHPDVARAVEAAGGEVCMTRADHQS 74
Cdd:PRK14353   4 RTCLAIILAAGEGTRmkssLP-KVLHPVAGRPMLAHVLAAAASLGPSRVAVVVgpGAEAVAAAAAKIAPDAEIFVQKERL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556426074  75 GT--------ERLAevvekcGFSDDTVIVNvqGDEPMIPAVIIRQVAENLAQRqvgmATLAV 128
Cdd:PRK14353  83 GTahavlaarEALA------GGYGDVLVLY--GDTPLITAETLARLRERLADG----ADVVV 132
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-114 5.91e-09

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 54.10  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   3 FVVIIPARYASTRLPG-KPLVDINGKPMIVHVLERARESGADRVIVATDHPDVARAVEAAGGEVCMTRADH----QSGTE 77
Cdd:cd04182    1 IAAIILAAGRSSRMGGnKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDweegMSSSL 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 556426074  78 RLAevVEKCGFSDDTVIVNVqGDEPMIPAVIIRQVAE 114
Cdd:cd04182   81 AAG--LEALPADADAVLILL-ADQPLVTAETLRALID 114
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-128 1.72e-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: 50.59  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   5 VIIPARYASTR----LPgKPLVDINGKPMIVHVLERARESGADRVIVATDHPdvARAVEAAGGE--VCMTRADHQSGTER 78
Cdd:cd02540    1 AVILAAGKGTRmksdLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHG--AEQVKKALANpnVEFVLQEEQLGTGH 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 556426074  79 -LAEVVEKCGFSDDTVIVnVQGDEPMIPAVIIRQVAENLAQRQVGMATLAV 128
Cdd:cd02540   78 aVKQALPALKDFEGDVLV-LYGDVPLITPETLQRLLEAHREAGADVTVLTA 127
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
19-248 2.23e-07

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 50.24  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  19 KPLVDINGKPMIVHVLERARESGADRVIVATDH--PDVARAVEAAGGEV----------------CMTRADHqsgterla 80
Cdd:COG1213   22 KCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYkaELIEEALARPGPDVtfvynpdydetnniysLWLAREA-------- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  81 evvekcgFSDDTVIVNvqGD---EPMIPAVIIRQVAENlaqrqvgmaTLAVPIHHAEEAfnPNAVKVVMDAEGYALYFSR 157
Cdd:COG1213   94 -------LDEDFLLLN--GDvvfDPAILKRLLASDGDI---------VLLVDRKWEKPL--DEEVKVRVDEDGRIVEIGK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 158 aTIPwdrdrfalSKETIGDTflrhIGIYGYRAGFIRRYVTWapspLEHIEMLEQLRvLWY----------GEKIHVAVAS 227
Cdd:COG1213  154 -KLP--------PEEADGEY----IGIFKFSAEGAAALREA----LEALIDEGGPN-LYYedalqelideGGPVKAVDIG 215

                        250       260
                 ....*....|....*....|.
gi 556426074 228 EVPGTGVDTPEDLERVRAELR 248
Cdd:COG1213  216 GLPWVEIDTPEDLERAEELFA 236
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 19-248 4.58e-07

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


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 49.38  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  19 KPLVDINGKPMIVHVLERARESGADRVIVATDHPdvARAVEAA-------GGEVCMTRADHQSGT-ERLAEVVEKcgFSD 90
Cdd:COG1208   22 KPLLPVGGKPLLEHILERLAAAGITEIVINVGYL--AEQIEEYfgdgsrfGVRITYVDEGEPLGTgGALKRALPL--LGD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  91 DTVIVnVQGDepmipAVI---IRQVAENLAQRQvGMATLAVpihHAEEAFNPNAVkVVMDAEGYALYFsratipwdrdrf 167
Cdd:COG1208   98 EPFLV-LNGD-----ILTdldLAALLAFHREKG-ADATLAL---VPVPDPSRYGV-VELDGDGRVTRF------------ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074 168 aLSKETIGDTFLRHIGIYGYRAGFIRRYVTWAPSPLEHI--EMLEQLRVlwYGEKIHvavasevpG--TGVDTPEDLERV 243
Cdd:COG1208  155 -VEKPEEPPSNLINAGIYVLEPEIFDYIPEGEPFDLEDLlpRLIAEGRV--YGYVHD--------GywLDIGTPEDLLEA 223


                 ....*
gi 556426074 244 RAELR 248
Cdd:COG1208  224 NALLL 228
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 19-51 5.83e-06

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: 46.02  E-value: 5.83e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 556426074  19 KPLVDINGKPMIVHVLERARESGADRVIVATDH 51
Cdd:cd06422   22 KPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHH 54
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-51 1.14e-05

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: 44.88  E-value: 1.14e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556426074   5 VIIPARYASTRL-------PgKPLVDINGKPMIVHVLERARESGADRVIVATDH 51
Cdd:cd04181    1 AVILAAGKGTRLrpltdtrP-KPLLPIAGKPILEYIIERLARAGIDEIILVVGY 53
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 13-57 1.86e-05

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 44.02  E-value: 1.86e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 556426074  13 STRLPG--KPLVDINGKPMIVHVLERARESGADRVIVATDHPDVARA 57
Cdd:PRK00317  14 SRRMGGvdKGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYAA 60
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-128 1.87e-05

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: 45.02  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTR----LPgKPLVDINGKPMIVHVLERARESGADRVIVATDH--PDVARAVEAAGGEVCMTraDHQS 74
Cdd:COG1207    1 SPLAVVILAAGKGTRmkskLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHgaEQVRAALADLDVEFVLQ--EEQL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556426074  75 GT----ERLAEVVEkcGFSDDTVIVNvqGDEPMIPAVIIRQVAENLAQRQVGMATLAV 128
Cdd:COG1207   78 GTghavQQALPALP--GDDGTVLVLY--GDVPLIRAETLKALLAAHRAAGAAATVLTA 131
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-129 7.34e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 42.81  E-value: 7.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTRL-PGKP--LVDINGKPMIVHVLERARESGA-DRVIVAT---DHPDVARAVEA--------AGGEv 65
Cdd:PRK00155   2 MMVYAIIPAAGKGSRMgADRPkqYLPLGGKPILEHTLEAFLAHPRiDEIIVVVppdDRPDFAELLLAkdpkvtvvAGGA- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556426074  66 cmTRADH-QSGterLAEVVEkcgfsDDTVIVNvqgD--EPMIPAVIIRQVAEnlAQRQVGMATLAVP 129
Cdd:PRK00155  81 --ERQDSvLNG---LQALPD-----DDWVLVH---DaaRPFLTPDDIDRLIE--AAEETGAAILAVP 132
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-130 1.01e-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: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   6 IIPAryA--STRLPG---KPLVDINGKPMIVHVLERARESGA-DRVIVAT---DHPDVARAVE----------AAGGEvc 66
Cdd:COG1211    1 IIPA--AgsGSRMGAgipKQFLPLGGKPVLEHTLEAFLAHPRiDEIVVVVppdDIEYFEELLAkygidkpvrvVAGGA-- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426074  67 mTRADhqsgTERLAevVEKCGFSDDTVIVNvqgD--EPMIPAVIIRQVAENLaqRQVGMATLAVPI 130
Cdd:COG1211   77 -TRQD----SVRNG--LEALPDDDDWVLVH---DaaRPLVSPELIDRVIEAA--REYGAAIPALPV 130
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 19-49 1.12e-04

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 42.22  E-value: 1.12e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 556426074  19 KPLVDINGKPMIVHVLERARESGADRVIVAT 49
Cdd:cd02523   21 KCLLEINGKPLLERQIETLKEAGIDDIVIVT 51
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 13-56 1.14e-04

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: 41.72  E-value: 1.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 556426074  13 STRLPG-KPLVDINGKPMIVHVLERARESGADRVIVATDHPDVAR 56
Cdd:COG0746   15 SRRMGQdKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERYAA 59
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-151 1.84e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 42.23  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   5 VIIPARYASTRLPG---KPLVDINGKPMIVHVLERARESGADR--VIVATDHPDVARAVEAAGGEVCMTRADHQSGTERL 79
Cdd:PRK14352   7 VIVLAAGAGTRMRSdtpKVLHTLAGRSMLGHVLHAAAGLAPQHlvVVVGHDRERVAPAVAELAPEVDIAVQDEQPGTGHA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074  80 AEvvekCGFS------DDTVIVnVQGDEPMIPAVIIRQVAEnlaqrqvgmatlavpIHHAEeafnPNAVKV----VMDAE 149
Cdd:PRK14352  87 VQ----CALEalpadfDGTVVV-TAGDVPLLDGETLADLVA---------------THTAE----GNAVTVltttLDDPT 142


                 ..
gi 556426074 150 GY 151
Cdd:PRK14352 143 GY 144
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 5-118 1.89e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.27  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   5 VIIPARYASTRLPG---KPLVDINGKPMIVHVLERARESGADRVIVATDHPdvARAVEAA--GGEVCMTRADHQSGT-ER 78
Cdd:PRK14358  10 VVILAAGQGTRMKSalpKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHG--AEQVEAAlqGSGVAFARQEQQLGTgDA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 556426074  79 LAEVVEKCGFSDDTVIVnVQGDEPMI-PAVIIRQVAENLAQ 118
Cdd:PRK14358  88 FLSGASALTEGDADILV-LYGDTPLLrPDTLRALVADHRAQ 127
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-130 3.70e-04

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 40.58  E-value: 3.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   3 FVVIIPARYASTRLPG---KPLVDINGKPMIVHVLERARESGA-DRVIVAT--DHPDVARAVE----------AAGGEvc 66
Cdd:cd02516    1 VAAIILAAGSGSRMGAdipKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVVppDDIDLAKELAkyglskvvkiVEGGA-- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556426074  67 mTRADhqsgTERLA-EVVEKcgfsDDTVIVNVQ-GDEPMIPAVIIRQVAENLaqRQVGMATLAVPI 130
Cdd:cd02516   79 -TRQD----SVLNGlKALPD----ADPDIVLIHdAARPFVSPELIDRLIDAL--KEYGAAIPAVPV 133
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 13-52 6.57e-04

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.48  E-value: 6.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 556426074  13 STRLPG-KPLVDINGKPMIVHVLERARESGADRVIVATDHP 52
Cdd:cd02503   11 SRRMGGdKALLELGGKPLLEHVLERLKPLVDEVVISANRDQ 51
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-129 1.06e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.59  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTR----LPgKPLVDINGKPMIVHVLERARESGAD-RVIVATDHPDVARAVEAAGGEVCMTRADHQ-- 73
Cdd:PRK14359   1 MKLSIIILAAGKGTRmkssLP-KVLHTICGKPMLFYILKEAFAISDDvHVVLHHQKERIKEAVLEYFPGVIFHTQDLEny 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556426074  74 SGTERLAEVVEKCGfsDDTVIVNvqGDEPMIPAVIIRQVAENLAQRQVGMATLAVP 129
Cdd:PRK14359  80 PGTGGALMGIEPKH--ERVLILN--GDMPLVEKDELEKLLENDADIVMSVFHLADP 131
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-106 2.41e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.66  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556426074   1 MSFVVIIPARYASTR----LPgKPLVDINGKPMIVHVLERARESGADRVIVATDHPdvARAVEAA-GGEVCMTRADHQSG 75
Cdd:PRK14354   1 MNRYAIILAAGKGTRmkskLP-KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHG--AEEVKEVlGDRSEFALQEEQLG 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556426074  76 TerlAEVV----EKCGFSDDTVIVnVQGDEPMIPA 106
Cdd:PRK14354  78 T---GHAVmqaeEFLADKEGTTLV-ICGDTPLITA 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH