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Conserved domains on  [gi|514061375|ref|WP_016527686|]
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3-deoxy-manno-octulosonate cytidylyltransferase [Glaesserella parasuis]

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
 1-249 1.44e-158

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


:

Pssm-ID: 235473  Cd Length: 245  Bit Score: 439.55  E-value: 1.44e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  81 EVIEKMAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 161 PFGRDYFPQCDDTfvqqqNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAKEAPQVGVDTAE 240
Cdd:PRK05450 161 PYGRDAFADSAPT-----PVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPE 235


                 ....*....
gi 514061375 241 DLERVRQIL 249
Cdd:PRK05450 236 DLERVRALL 244
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-249 1.44e-158

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 439.55  E-value: 1.44e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  81 EVIEKMAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 161 PFGRDYFPQCDDTfvqqqNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAKEAPQVGVDTAE 240
Cdd:PRK05450 161 PYGRDAFADSAPT-----PVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPE 235


                 ....*....
gi 514061375 241 DLERVRQIL 249
Cdd:PRK05450 236 DLERVRALL 244
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-248 1.69e-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: 424.09  E-value: 1.69e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQA-GATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  80 AEVIEKMAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKH-QVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDpEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 159 TIPFGRDYFPqcddtfvQQQNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAkEAPQVGVDT 238
Cdd:COG1212  161 PIPYPRDAFA-------EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDT 232

                        250
                 ....*....|
gi 514061375 239 AEDLERVRQI 248
Cdd:COG1212  233 PEDLERVRAL 242
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 2-248 6.52e-134

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: 377.20  E-value: 6.52e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   2 SFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQA-GATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  81 EVIEKMAiADDEIIVNIQGDEPLIPPVIVAQVAENLDKH-QVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRAT 159
Cdd:cd02517   81 EVAEKLD-ADDDIVVNVQGDEPLIPPEMIDQVVAALKDDpGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 160 IPFGRDYFPQcddtfvqqQNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAKEAPqVGVDTA 239
Cdd:cd02517  160 IPYPRDSSED--------FPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHES-IGVDTP 230


                 ....*....
gi 514061375 240 EDLERVRQI 248
Cdd:cd02517  231 EDLERVEAL 239
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 4-243 1.06e-125

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


Pssm-ID: 129558  Cd Length: 238  Bit Score: 356.53  E-value: 1.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375    4 TVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLAEVI 83
Cdd:TIGR00466   1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   84 EKMAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATIPFG 163
Cdd:TIGR00466  81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  164 RDYFPQCDDTfvQQQNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAKEAPQVGVDTAEDLE 243
Cdd:TIGR00466 161 RDFFAKRQTP--VGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-223 1.10e-79

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: 238.78  E-value: 1.10e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375    4 TVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   83 IEKMAIADDEIIVNIQGDEPLIPP-VIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPeVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514061375  162 FGRDyfpqcDDTFVQQQnYLRHIGIYAYRAG-FVKQYVAWEPTALEQLESLEQLRALWYGEKI 223
Cdd:pfam02348 161 YIRE-----HPAELYYV-YLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
 
Name Accession Description Interval E-value
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-249 1.44e-158

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 439.55  E-value: 1.44e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLA 80
Cdd:PRK05450   1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  81 EVIEKMAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATI 160
Cdd:PRK05450  81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 161 PFGRDYFPQCDDTfvqqqNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAKEAPQVGVDTAE 240
Cdd:PRK05450 161 PYGRDAFADSAPT-----PVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPE 235


                 ....*....
gi 514061375 241 DLERVRQIL 249
Cdd:PRK05450 236 DLERVRALL 244
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 1-248 1.69e-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: 424.09  E-value: 1.69e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQA-GATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERL 79
Cdd:COG1212    1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  80 AEVIEKMAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKH-QVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRA 158
Cdd:COG1212   81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDpEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 159 TIPFGRDYFPqcddtfvQQQNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAkEAPQVGVDT 238
Cdd:COG1212  161 PIPYPRDAFA-------EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVDT 232

                        250
                 ....*....|
gi 514061375 239 AEDLERVRQI 248
Cdd:COG1212  233 PEDLERVRAL 242
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 2-248 6.52e-134

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: 377.20  E-value: 6.52e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   2 SFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQA-GATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLA 80
Cdd:cd02517    1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  81 EVIEKMAiADDEIIVNIQGDEPLIPPVIVAQVAENLDKH-QVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRAT 159
Cdd:cd02517   81 EVAEKLD-ADDDIVVNVQGDEPLIPPEMIDQVVAALKDDpGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 160 IPFGRDYFPQcddtfvqqQNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAKEAPqVGVDTA 239
Cdd:cd02517  160 IPYPRDSSED--------FPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHES-IGVDTP 230


                 ....*....
gi 514061375 240 EDLERVRQI 248
Cdd:cd02517  231 EDLERVEAL 239
kdsB TIGR00466
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ...
 4-243 1.06e-125

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


Pssm-ID: 129558  Cd Length: 238  Bit Score: 356.53  E-value: 1.06e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375    4 TVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLAEVI 83
Cdd:TIGR00466   1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   84 EKMAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATIPFG 163
Cdd:TIGR00466  81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  164 RDYFPQCDDTfvQQQNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLDLAKEAPQVGVDTAEDLE 243
Cdd:TIGR00466 161 RDFFAKRQTP--VGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 1-249 4.28e-116

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 331.93  E-value: 4.28e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQA-GATRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERL 79
Cdd:PRK13368   1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAaGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  80 AEVIEKMaiaDDEIIVNIQGDEPLIPPVIVAQVAEN-LDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRA 158
Cdd:PRK13368  81 AEVMLKI---EADIYINVQGDEPMIRPRDIDTLIQPmLDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 159 TIPFGRDYFPqcddtfvqqQNYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIHLdLAKEAPQVGVDT 238
Cdd:PRK13368 158 PIPSRRDGES---------ARYLKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRM-VEVAATSIGVDT 227

                        250
                 ....*....|.
gi 514061375 239 AEDLERVRQIL 249
Cdd:PRK13368 228 PEDLERVRAIM 238
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 4-223 1.10e-79

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: 238.78  E-value: 1.10e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375    4 TVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLAEV 82
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   83 IEKMAIADDEIIVNIQGDEPLIPP-VIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATIP 161
Cdd:pfam02348  81 VKAFLNDHDDIIVNIQGDNPLLQPeVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514061375  162 FGRDyfpqcDDTFVQQQnYLRHIGIYAYRAG-FVKQYVAWEPTALEQLESLEQLRALWYGEKI 223
Cdd:pfam02348 161 YIRE-----HPAELYYV-YLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
PLN02917 PLN02917
CMP-KDO synthetase
 6-249 1.45e-59

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 190.43  E-value: 1.45e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   6 IIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVATDHPEIEQVVTSFGGEVCLTSDKHNSGTERLAEVIE 84
Cdd:PLN02917  51 IIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTlDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  85 KMAIADDeIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTLTDKNGMALYFSRATIPFGR 164
Cdd:PLN02917 131 KLEKKYD-IVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGLIPYNK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 165 -----DYFPqcddtfvqqqnYLRHIGIYAYRAGFVKQYVAWEPTALEQLESLEQLRALWYGEKIH-LDLAKEAPqvGVDT 238
Cdd:PLN02917 210 sgkvnPQFP-----------YLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKvIKVDHEAH--GVDT 276

                        250
                 ....*....|.
gi 514061375 239 AEDLERVRQIL 249
Cdd:PLN02917 277 PEDVEKIEALM 287
SpsF COG1861
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ...
 1-252 5.64e-18

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


Pssm-ID: 441466  Cd Length: 245  Bit Score: 80.25  E-value: 5.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQA-GATRVIVAT-DHPE---IEQVVTSFGGEVCltsdkhnSG 75
Cdd:COG1861    2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSkLIDEVVVATtTDPAddpLVDLAKELGVPVF-------RG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  76 TE-----RLAEVIEKMaiaDDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTRE----ELFNPNVVKTLt 146
Cdd:COG1861   75 SEddvlsRYYQAAEAY---GADVVVRITGDCPLIDPALIDELIAAFLESGADYVSNSLPRTYPRgldvEVFSFAALERA- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 147 dkngmalyFSRATIPFGRDyfpqcddtfvqqqnylrHIGIYAYRAG--FVKQYVAWEptaleqlESLEQLRalwygekih 224
Cdd:COG1861  151 --------WEEAKLPSERE-----------------HVTPYIYEHPdrFRIGNVEPP-------EDLSDLR--------- 189

                        250       260
                 ....*....|....*....|....*...
gi 514061375 225 ldlakeapqVGVDTAEDLERVRQILNTL 252
Cdd:COG1861  190 ---------LTVDTPEDLELIRAIYEAL 208
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 2-124 1.47e-16

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: 76.04  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   2 SFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVATDHPEIEQVVTSFGGEVCL-----TSDKHNSG 75
Cdd:cd02513    1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLfDRVVVSTDDEEIAEVARKYGAEVPFlrpaeLATDTASS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514061375  76 TERLAEVIEKM--AIADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMA 124
Cdd:cd02513   81 IDVILHALDQLeeLGRDFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSV 131
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 1-106 4.64e-16

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 74.81  E-value: 4.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVATDHPEIEQVVTSFGGEVCL----TSDKHNSG 75
Cdd:COG1083    1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLfDRVVVSTDDEEIAEVAREYGAEVFLrpaeLAGDTAST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 514061375  76 TERLAEVIEKMAIADD--EIIVNIQGDEPLIPP 106
Cdd:COG1083   81 IDVILHALEWLEEQGEefDYVVLLQPTSPLRTA 113
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 4-131 5.77e-13

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: 66.06  E-value: 5.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   4 TVIIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQA-GATRVIVAT-DHPE---IEQVVTSFGGEV-------CLtsdk 71
Cdd:cd02518    1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSkLIDEIVIATsTNEEddpLEALAKKLGVKVfrgseedVL---- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  72 hnsgtERLAEVIEKmaiADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLT 131
Cdd:cd02518   77 -----GRYYQAAEE---YNADVVVRITGDCPLIDPEIIDAVIRLFLKSGADYTSNTLPRT 128
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 6-121 6.10e-13

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: 66.20  E-value: 6.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375    6 IIPARYASTRLPRKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVATDHPEIEQVVTSFGGEVCLT-----SDKHNSGTERL 79
Cdd:TIGR03584   3 IIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLfDKVVVSTDDEEIAEVAKSYGASVPFLrpkelADDFTGTAPVV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 514061375   80 AEVIEKMAIA-DDEIIVNIQGDEPLIPPVIVAQVAENLDKHQV 121
Cdd:TIGR03584  83 KHAIEELKLQkQYDHACCIYATAPFLQAKILKEAFELLKQPNA 125
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 14-136 9.98e-09

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 53.35  E-value: 9.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  14 TRL--PRKPLLDIAGKPMIQHVWEKAQQAGATRVIVAT--DHPEIEQVVTSFGGEVCLTsdkhnSGT---ERLAEVIEKM 86
Cdd:COG2266    7 TRLggGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVspNTPKTREYLKERGVEVIET-----PGEgyvEDLNEALESI 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 514061375  87 aiadDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREEL 136
Cdd:COG2266   82 ----SGPVLVVPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPAALKREL 127
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-119 1.96e-08

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 52.86  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTRLPR-KPLLDIAGKPMIQHVWEKAQQAGATRVIVAT--DHPEIEQVVTSFGGEVCLTSDKHN---- 73
Cdd:COG2068    2 SKVAAIILAAGASSRMGRpKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgaDAEEVAAALAGLGVRVVVNPDWEEgmss 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 514061375  74 ---SGTERLAEVIEKMAIAddeiivniQGDEPLIPPVIVAQVAENLDKH 119
Cdd:COG2068   82 slrAGLAALPADADAVLVL--------LGDQPLVTAETLRRLLAAFRES 122
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 12-120 2.68e-08

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 51.81  E-value: 2.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   12 ASTRLPR-KPLLDIAGKPMIQHVWEKAQQAGAtRVIVATDHPEIEQVVTSFGGEVcLTSDKHNSGTER-LAEVIEKMAIA 89
Cdd:pfam12804   8 RSSRMGGdKALLPLGGKPLLERVLERLRPAGD-EVVVVANDEEVLAALAGLGVPV-VPDPDPGQGPLAgLLAALRAAPGA 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 514061375   90 DDEIIVNiqGDEPLIPPVIVAQVAENLDKHQ 120
Cdd:pfam12804  86 DAVLVLA--CDMPFLTPELLRRLLAAAEESG 114
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-116 3.25e-08

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 53.71  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTR----LPrKPLLDIAGKPMIQHVWEKAQQAGATRVIVAT--DHPEIEQVVTSFGGEV--CLTSDKH 72
Cdd:PRK14353   4 RTCLAIILAAGEGTRmkssLP-KVLHPVAGRPMLAHVLAAAASLGPSRVAVVVgpGAEAVAAAAAKIAPDAeiFVQKERL 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 514061375  73 NSGTERLA--EVIEKMaiADDEIIVNiqGDEPLIPPVIVAQVAENL 116
Cdd:PRK14353  83 GTAHAVLAarEALAGG--YGDVLVLY--GDTPLITAETLARLRERL 124
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-134 7.86e-08

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: 51.43  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   5 VIIPARYASTRL-------PrKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDH--PEIEQVVTS---FGGEVCLTSDKH 72
Cdd:cd04181    1 AVILAAGKGTRLrpltdtrP-KPLLPIAGKPILEYIIERLARAGIDEIILVVGYlgEQIEEYFGDgskFGVNIEYVVQEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514061375  73 NSGTerlAEVIEKMA--IADDEIIVnIQGDEplippVIVAQVAENLDKHQVNMATLAVKLTTRE 134
Cdd:cd04181   80 PLGT---AGAVRNAEdfLGDDDFLV-VNGDV-----LTDLDLSELLRFHREKGADATIAVKEVE 134
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-133 2.15e-07

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: 51.18  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTR----LPrKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHpEIEQVVTSFGGEVCLTSDKhnsgT 76
Cdd:COG1207    1 SPLAVVILAAGKGTRmkskLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGH-GAEQVRAALADLDVEFVLQ----E 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514061375  77 ERL------AEVIEKMAIADDEIIVnIQGDEPLIPPVIVAQVaenLDKHQVNMATLAVkLTTR 133
Cdd:COG1207   75 EQLgtghavQQALPALPGDDGTVLV-LYGDVPLIRAETLKAL---LAAHRAAGAAATV-LTAE 132
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-131 2.46e-07

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 50.21  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   5 VIIPARYASTR----LPrKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHP--EIEQVVTSFGGEVCLTSDKhnSGTER 78
Cdd:cd02540    1 AVILAAGKGTRmksdLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGaeQVKKALANPNVEFVLQEEQ--LGTGH 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 514061375  79 -LAEVIEKMAIADDEIIVnIQGDEPLIPPVIVAQVAENLDKHQVNMATLAVKLT 131
Cdd:cd02540   78 aVKQALPALKDFEGDVLV-LYGDVPLITPETLQRLLEAHREAGADVTVLTAELE 130
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-55 7.81e-07

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 47.94  E-value: 7.81e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 514061375   3 FTVIIPARYASTRLPR-KPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIE 55
Cdd:cd04182    1 IAAIILAAGRSSRMGGnKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADA 54
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-130 3.32e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 47.71  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTR----LPrKPLLDIAGKPMIQHVWEKAQQAGATRVivatdhpeieQVVTSFGGEVC---LTSDKHN 73
Cdd:PRK09451   4 SAMSVVILAAGKGTRmysdLP-KVLHTLAGKPMVQHVIDAANELGAQHV----------HLVYGHGGDLLkqtLADEPLN 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514061375  74 --SGTERL--AEVIEKMA--IADDEIIVNIQGDEPLIPpvivAQVAENL--DKHQVNMATLAVKL 130
Cdd:PRK09451  73 wvLQAEQLgtGHAMQQAApfFADDEDILMLYGDVPLIS----VETLQRLrdAKPQGGIGLLTVKL 133
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 19-127 3.85e-06

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 46.33  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  19 KPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQvvtSFGGEVCLTSDKHNSGTerLAEVIEKMAIADDEIIVNIQ 98
Cdd:PRK00317  22 KGLQELNGKPLIQHVIERLAPQVDEIVINANRNLARYA---AFGLPVIPDSLADFPGP--LAGILAGLKQARTEWVLVVP 96

                         90       100
                 ....*....|....*....|....*....
gi 514061375  99 GDEPLIPPVIVAQVAENLDKHQVNMATLA 127
Cdd:PRK00317  97 CDTPFIPPDLVARLAQAAGKDDADVAWAH 125
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 19-62 8.22e-06

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


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 45.53  E-value: 8.22e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 514061375  19 KPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEiEQVVTSFG 62
Cdd:COG1208   22 KPLLPVGGKPLLEHILERLAAAGITEIVINVGYLA-EQIEEYFG 64
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-250 8.78e-06

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 45.62  E-value: 8.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   5 VIIPARYASTRL-------PrKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDH--PEIEQVVTSFGGEV-CLTSDK--- 71
Cdd:COG1213    2 AVILAAGRGSRLgpltddiP-KCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYkaELIEEALARPGPDVtFVYNPDyde 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  72 -HNSGTERLAevieKMAIADDEIIVNiqGD---EPLIPPVIVAQVAENL---DKHQVNMATLAVKLTTREELFNPNVVKT 144
Cdd:COG1213   81 tNNIYSLWLA----REALDEDFLLLN--GDvvfDPAILKRLLASDGDIVllvDRKWEKPLDEEVKVRVDEDGRIVEIGKK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375 145 LTDKNGMALYfsratipfgrdyfpqcddtfvqqqnylrhIGIYAYRAGFVKQYVAweptALEQLESLEQLRaLWYgEKIH 224
Cdd:COG1213  155 LPPEEADGEY-----------------------------IGIFKFSAEGAAALRE----ALEALIDEGGPN-LYY-EDAL 199

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 514061375 225 LDLAKEAPQVG-----------VDTAEDLERVRQILN 250
Cdd:COG1213  200 QELIDEGGPVKavdigglpwveIDTPEDLERAEELFA 236
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-128 1.51e-05

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 44.57  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   3 FTVIIPARYASTRLPR------KPLLDIAGKPMIQHVWEKAQQAGATRVIV---ATDHPEIEQVVTSFG------GEVCL 67
Cdd:cd04198    1 FQAVILAGGGGSRLYPltdnipKALLPVANKPMIWYPLDWLEKAGFEDVIVvvpEEEQAEISTYLRSFPlnlkqkLDEVT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514061375  68 TSDKHNSGTerlAEVIEKMA--IADDEIIVNiqGDepLIPPVIVAQVaenLDKHQVNMATLAV 128
Cdd:cd04198   81 IVLDEDMGT---ADSLRHIRkkIKKDFLVLS--CD--LITDLPLIEL---VDLHRSHDASLTV 133
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 13-56 2.65e-05

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: 43.64  E-value: 2.65e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 514061375  13 STRLPR-KPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQ 56
Cdd:COG0746   15 SRRMGQdKALLPLGGRPLLERVLERLRPQVDEVVIVANRPERYAA 59
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 19-51 2.66e-05

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 44.10  E-value: 2.66e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 514061375  19 KPLLDIAGKPMIQHVWEKAQQAGATRVIVATDH 51
Cdd:cd06422   22 KPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHH 54
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 19-131 1.23e-04

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 41.86  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  19 KPLLDIAGKPMIQHVWEKAQQAGATRVIV---ATDHPEIEQVVTSFGGE--------VCLTSDKHNSGT-ERLaevIEKM 86
Cdd:cd02507   23 KALLPVANVPLIDYTLEWLEKAGVEEVFVvccEHSQAIIEHLLKSKWSSlsskmivdVITSDLCESAGDaLRL---RDIR 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 514061375  87 AIADDEIIVnIQGDepLIPPV-IVAQVAENLDKHQVNMATLAVKLT 131
Cdd:cd02507  100 GLIRSDFLL-LSCD--LVSNIpLSELLEERRKKDKNAIATLTVLLA 142
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 15-100 4.44e-04

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


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 40.23  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  15 RLPrKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHpEIEQVVTSFGGevcltsdkHNSGTERLAEVIE---------- 84
Cdd:cd06915   18 DLP-KPLAPVAGRPFLEYLLEYLARQGISRIVLSVGY-LAEQIEEYFGD--------GYRGGIRIYYVIEpeplgtggai 87

                         90
                 ....*....|....*....
gi 514061375  85 KMA---IADDEIIVnIQGD 100
Cdd:cd06915   88 KNAlpkLPEDQFLV-LNGD 105
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-131 5.63e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 40.12  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPA-----RYASTRlpRKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVATDHPEIEQvvtsFGGEVCLTSDKH-- 72
Cdd:PRK00155   2 MMVYAIIPAagkgsRMGADR--PKQYLPLGGKPILEHTLEAFLAHPRiDEIIVVVPPDDRPD----FAELLLAKDPKVtv 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514061375  73 -NSGTER-------LAeviekmAIADDEIIVNIQGDEPLIPPVIVAQVAENLDKHQVnmATLAVKLT 131
Cdd:PRK00155  76 vAGGAERqdsvlngLQ------ALPDDDWVLVHDAARPFLTPDDIDRLIEAAEETGA--AILAVPVK 134
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 13-128 8.22e-04

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


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 40.12  E-value: 8.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375  13 STRLP--RKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQvvtSFGGEVCLTSDKHNSGTERLAEVIEKMAIAD 90
Cdd:PRK14489  16 SRRMNgrDKALILLGGKPLIERVVDRLRPQFARIHLNINRDPARYQ---DLFPGLPVYPDILPGFQGPLSGILAGLEHAD 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 514061375  91 DEIIVNIQGDEPLIPPVIVAQVAENLdkhQVNMATLAV 128
Cdd:PRK14489  93 SEYLFVVACDTPFLPENLVKRLSKAL---AIEGADIAV 127
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-145 1.55e-03

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: 38.66  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   3 FTVIIPARYASTRLPR---KPLLDIAGKPMIQHVWEKAQQAGA-TRVIVAT---DHPEIEQVVTSFGGEVCLTSDkhnSG 75
Cdd:cd02516    1 VAAIILAAGSGSRMGAdipKQFLELGGKPVLEHTLEAFLAHPAiDEIVVVVppdDIDLAKELAKYGLSKVVKIVE---GG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514061375  76 TERLAEV---IEKMAIADDEIIVnIQ-GDEPLIPPVIVAQVAENLDKHQVNMATLAVKLTTREELFNPNVVKTL 145
Cdd:cd02516   78 ATRQDSVlngLKALPDADPDIVL-IHdAARPFVSPELIDRLIDALKEYGAAIPAVPVTDTIKRVDDDGVVVETL 150
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 13-56 2.49e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 37.94  E-value: 2.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 514061375  13 STRLPR-KPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHPEIEQ 56
Cdd:cd02503   11 SRRMGGdKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYA 55
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-139 2.79e-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: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   1 MSFTVIIPARYASTR----LPrKPLLDIAGKPMIQHVWEKAQQAGATRVIVATDHpEIEQVVTSFGGEVCLTSDKHNSGT 76
Cdd:PRK14354   1 MNRYAIILAAGKGTRmkskLP-KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGH-GAEEVKEVLGDRSEFALQEEQLGT 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514061375  77 E---RLAEviEKMAIADDEIIVnIQGDEPLippvIVAQVAENLDKHQVNMATLAVKLTTREElfNP 139
Cdd:PRK14354  79 GhavMQAE--EFLADKEGTTLV-ICGDTPL----ITAETLKNLIDFHEEHKAAATILTAIAE--NP 135
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-58 2.81e-03

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 38.15  E-value: 2.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514061375   6 IIPARYASTRL-PR-----KPLLDIAGKPMIQHVWEKAQQAGATRV-IVATDH--PEIEQVV 58
Cdd:COG1209    4 IILAGGSGTRLrPLtltvsKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEdgPQFERLL 65
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-66 2.84e-03

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 37.93  E-value: 2.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514061375   6 IIPARYASTRLpR-------KPLLDIAGKPMIQHVWEKAQQAGATRVIVatdhpeieqVVTSFGGEVC 66
Cdd:cd04189    4 LILAGGKGTRL-RpltytrpKQLIPVAGKPIIQYAIEDLREAGIEDIGI---------VVGPTGEEIK 61
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-131 3.68e-03

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: 37.80  E-value: 3.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514061375   6 IIPAryA--STRL----PrKPLLDIAGKPMIQHVWEKAQQAGA-TRVIVAT---DHPEIEQVVTSFGgevcltSDKH--- 72
Cdd:COG1211    1 IIPA--AgsGSRMgagiP-KQFLPLGGKPVLEHTLEAFLAHPRiDEIVVVVppdDIEYFEELLAKYG------IDKPvrv 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514061375  73 -NSGTERLAEV---IEkmAIADDEIIVNIQ-GDEPLIPPVIVAQVAENLDKHQVnmATLAVKLT 131
Cdd:COG1211   72 vAGGATRQDSVrngLE--ALPDDDDWVLVHdAARPLVSPELIDRVIEAAREYGA--AIPALPVT 131
PRK02726 PRK02726
molybdenum cofactor guanylyltransferase;
1-53 6.59e-03

molybdenum cofactor guanylyltransferase;


Pssm-ID: 235063  Cd Length: 200  Bit Score: 36.55  E-value: 6.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 514061375   1 MSFTVIIPARYASTRLPR-KPLLDIAGKPMIQHVWEKAQQAgATRVIVATDHPE 53
Cdd:PRK02726   6 NNLVALILAGGKSSRMGQdKALLPWQGVPLLQRVARIAAAC-ADEVYIITPWPE 58
 
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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