|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
3-251 |
4.90e-130 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 367.52 E-value: 4.90e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 3 EFVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGAGEVWVATDDQRIADALSGlAEVKVAMTATSHASGTDRLA 82
Cdd:PRK05450 2 KFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEA-FGGEVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 83 ECARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAPI 162
Cdd:PRK05450 81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 163 AWHRDGFARsrdtlPAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPFPAGIDTPE 242
Cdd:PRK05450 161 PYGRDAFAD-----SAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPE 235
|
....*....
gi 896542980 243 DLERAEALL 251
Cdd:PRK05450 236 DLERVRALL 244
|
|
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
4-250 |
4.60e-127 |
|
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: 360.15 E-value: 4.60e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 4 FVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQA-GAGEVWVATDDQRIADALSGlAEVKVAMTATSHASGTDRLA 82
Cdd:COG1212 3 FIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEA-FGGEVVMTSPDHPSGTDRIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 83 ECARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVE-GNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAP 161
Cdd:COG1212 82 EAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEdPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 162 IAWHRDGFArsrdtlpAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPfPAGIDTP 241
Cdd:COG1212 162 IPYPRDAFA-------EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAP-PIGVDTP 233
|
....*....
gi 896542980 242 EDLERAEAL 250
Cdd:COG1212 234 EDLERVRAL 242
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
4-250 |
1.14e-113 |
|
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: 325.97 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 4 FVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQA-GAGEVWVATDDQRIADALSGLAeVKVAMTATSHASGTDRLA 82
Cdd:cd02517 2 VIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFG-GKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 83 ECARIAGWVDDtVVVNLQGDEPFAPAAGIRAVAEALVE-GNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAP 161
Cdd:cd02517 81 EVAEKLDADDD-IVVNVQGDEPLIPPEMIDQVVAALKDdPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 162 IAWHRDGfarsrdtlPAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPfPAGIDTP 241
Cdd:cd02517 160 IPYPRDS--------SEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHE-SIGVDTP 230
|
....*....
gi 896542980 242 EDLERAEAL 250
Cdd:cd02517 231 EDLERVEAL 239
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
5-245 |
1.40e-88 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 262.54 E-value: 1.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 5 VVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGAGEVWVATDDQRIADALSGlAEVKVAMTATSHASGTDRLAEC 84
Cdd:TIGR00466 1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQK-FGIEVCMTSKHHNSGTERLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 85 ARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAPIAW 164
Cdd:TIGR00466 80 VEKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 165 HRDGFARSRDtlPAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPFPAGIDTPEDL 244
Cdd:TIGR00466 160 DRDFFAKRQT--PVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDL 237
|
.
gi 896542980 245 E 245
Cdd:TIGR00466 238 E 238
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
5-222 |
3.78e-58 |
|
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: 184.08 E-value: 3.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 5 VVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGAGE-VWVATDDQRIADALSGLAeVKVAMTATSHASGTDRLAE 83
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEkVIVATDSEEIADVAKEFG-AGVVMTSGSLSSGTDRFYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 84 CARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVEGNAP-MSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAPI 162
Cdd:pfam02348 80 VVKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPyMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896542980 163 AWHRDGFArsrdtlPAGHNWLRHIGIYGYRAG-FLQQFAAMPPGQLEQVESLEQLRVLEAG 222
Cdd:pfam02348 160 PYIREHPA------ELYYVYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNG 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
3-251 |
4.90e-130 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 367.52 E-value: 4.90e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 3 EFVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGAGEVWVATDDQRIADALSGlAEVKVAMTATSHASGTDRLA 82
Cdd:PRK05450 2 KFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEA-FGGEVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 83 ECARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAPI 162
Cdd:PRK05450 81 EAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 163 AWHRDGFARsrdtlPAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPFPAGIDTPE 242
Cdd:PRK05450 161 PYGRDAFAD-----SAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPE 235
|
....*....
gi 896542980 243 DLERAEALL 251
Cdd:PRK05450 236 DLERVRALL 244
|
|
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
4-250 |
4.60e-127 |
|
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: 360.15 E-value: 4.60e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 4 FVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQA-GAGEVWVATDDQRIADALSGlAEVKVAMTATSHASGTDRLA 82
Cdd:COG1212 3 FIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEA-FGGEVVMTSPDHPSGTDRIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 83 ECARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVE-GNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAP 161
Cdd:COG1212 82 EAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEdPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 162 IAWHRDGFArsrdtlpAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPfPAGIDTP 241
Cdd:COG1212 162 IPYPRDAFA-------EDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAP-PIGVDTP 233
|
....*....
gi 896542980 242 EDLERAEAL 250
Cdd:COG1212 234 EDLERVRAL 242
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
4-250 |
1.14e-113 |
|
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: 325.97 E-value: 1.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 4 FVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQA-GAGEVWVATDDQRIADALSGLAeVKVAMTATSHASGTDRLA 82
Cdd:cd02517 2 VIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFG-GKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 83 ECARIAGWVDDtVVVNLQGDEPFAPAAGIRAVAEALVE-GNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAP 161
Cdd:cd02517 81 EVAEKLDADDD-IVVNVQGDEPLIPPEMIDQVVAALKDdPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 162 IAWHRDGfarsrdtlPAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPfPAGIDTP 241
Cdd:cd02517 160 IPYPRDS--------SEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHE-SIGVDTP 230
|
....*....
gi 896542980 242 EDLERAEAL 250
Cdd:cd02517 231 EDLERVEAL 239
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
5-245 |
1.40e-88 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 262.54 E-value: 1.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 5 VVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGAGEVWVATDDQRIADALSGlAEVKVAMTATSHASGTDRLAEC 84
Cdd:TIGR00466 1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQK-FGIEVCMTSKHHNSGTERLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 85 ARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAPIAW 164
Cdd:TIGR00466 80 VEKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 165 HRDGFARSRDtlPAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPFPAGIDTPEDL 244
Cdd:TIGR00466 160 DRDFFAKRQT--PVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDL 237
|
.
gi 896542980 245 E 245
Cdd:TIGR00466 238 E 238
|
|
| PRK13368 |
PRK13368 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
3-251 |
4.24e-86 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 184007 Cd Length: 238 Bit Score: 256.04 E-value: 4.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 3 EFVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQA-GAGEVWVATDDQRIADALSGlAEVKVAMTATSHASGTDRL 81
Cdd:PRK13368 2 KVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAaGVEEVYVATDDQRIEDAVEA-FGGKVVMTSDDHLSGTDRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 82 AECARIagwVDDTVVVNLQGDEPFAPAAGIRAVAEALVEGNAP-MSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRA 160
Cdd:PRK13368 81 AEVMLK---IEADIYINVQGDEPMIRPRDIDTLIQPMLDDPSInVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 161 PIAWHRDGfarsrdtlpAGHNWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVAISPEPfPAGIDT 240
Cdd:PRK13368 158 PIPSRRDG---------ESARYLKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRMVEVAAT-SIGVDT 227
|
250
....*....|.
gi 896542980 241 PEDLERAEALL 251
Cdd:PRK13368 228 PEDLERVRAIM 238
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
5-222 |
3.78e-58 |
|
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: 184.08 E-value: 3.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 5 VVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGAGE-VWVATDDQRIADALSGLAeVKVAMTATSHASGTDRLAE 83
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEkVIVATDSEEIADVAKEFG-AGVVMTSGSLSSGTDRFYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 84 CARIAGWVDDTVVVNLQGDEPFAPAAGIRAVAEALVEGNAP-MSTLATTVEDAHTLFDPNVVKLVRNVRNEAMYFSRAPI 162
Cdd:pfam02348 80 VVKAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPyMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896542980 163 AWHRDGFArsrdtlPAGHNWLRHIGIYGYRAG-FLQQFAAMPPGQLEQVESLEQLRVLEAG 222
Cdd:pfam02348 160 PYIREHPA------ELYYVYLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNG 214
|
|
| PLN02917 |
PLN02917 |
CMP-KDO synthetase |
8-253 |
6.96e-46 |
|
CMP-KDO synthetase
Pssm-ID: 215495 Cd Length: 293 Bit Score: 154.99 E-value: 6.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 8 IPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGA-GEVWVATDDQRIADALSGLAeVKVAMTATSHASGTDRLAEC-A 85
Cdd:PLN02917 52 IPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTlDHIVVATDDERIAECCRGFG-ADVIMTSESCRNGTERCNEAlK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 86 RIAGWVDdtVVVNLQGDEPFAPAAGIRAVAEALVEG-NAPMSTLATTV--EDAhtlFDPNVVKLVRNVRNEAMYFSRAPI 162
Cdd:PLN02917 131 KLEKKYD--IVVNIQGDEPLIEPEIIDGVVKALQAApDAVFSTAVTSLkpEDA---SDPNRVKCVVDNQGYAIYFSRGLI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 163 AWHRDGfaRSRDTLPaghnWLRHIGIYGYRAGFLQQFAAMPPGQLEQVESLEQLRVLEAGFPISVaISPEPFPAGIDTPE 242
Cdd:PLN02917 206 PYNKSG--KVNPQFP----YLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKV-IKVDHEAHGVDTPE 278
|
250
....*....|.
gi 896542980 243 DLERAEALLQA 253
Cdd:PLN02917 279 DVEKIEALMRE 289
|
|
| NeuA |
COG1083 |
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ... |
5-254 |
4.85e-15 |
|
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440700 Cd Length: 228 Bit Score: 72.11 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 5 VVA-IPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGA-GEVWVATDDQRIADalsgLAE---VKVAM----TATSHA 75
Cdd:COG1083 3 ILAiIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLfDRVVVSTDDEEIAE----VAReygAEVFLrpaeLAGDTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 76 SGTDRLAEC---ARIAGWVDDTVVVnLQGDEPFAPAAGIRAVAEALVEGNApmSTLATTVEDAHTLFDPNVVK---LVRN 149
Cdd:COG1083 79 STIDVILHAlewLEEQGEEFDYVVL-LQPTSPLRTAEDIDEAIELLLESGA--DSVVSVTEAHHPPYWALKLDedgRLEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 150 VRNEAMYFSR---APIAWHRDG--FARSRDTlpaghnWLRHIGIYGYRAGFLQqfaaMPPgqleqvesleqLRVLEagfp 224
Cdd:COG1083 156 LNPDPHNRPRrqdLPPAYRENGaiYIFKREA------LLENKSRFGGKTGAYE----MPE-----------ERSVD---- 210
|
250 260 270
....*....|....*....|....*....|
gi 896542980 225 isvaispepfpagIDTPEDLERAEALLQAM 254
Cdd:COG1083 211 -------------IDTEEDFELAEALLKKR 227
|
|
| CMP-NeuAc_Synthase |
cd02513 |
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ... |
8-251 |
1.81e-13 |
|
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.
Pssm-ID: 133006 Cd Length: 223 Bit Score: 67.56 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 8 IPARYAASRLPGKPLRLLGGEPLVLHVARRALQAGA-GEVWVATDDQRIADALSGL-AEVKV---AMTATSHASGTDRLA 82
Cdd:cd02513 6 IPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLfDRVVVSTDDEEIAEVARKYgAEVPFlrpAELATDTASSIDVIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 83 ECARI---AGWVDDTvVVNLQGDEPFAPAAGIRAVAEALVEGNApmSTLATTVEDAH------TLFDPNVVKLVRNVRNE 153
Cdd:cd02513 86 HALDQleeLGRDFDI-VVLLQPTSPLRSAEDIDEAIELLLSEGA--DSVFSVTEFHRfpwralGLDDNGLEPVNYPEDKR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 154 AMYFSRAPiAWHRDG--FARSRDTLPAGHNWL-RHIGIYgyragflqqfaAMPPgqleqvesleqLRVLEagfpisvais 230
Cdd:cd02513 163 TRRQDLPP-AYHENGaiYIAKREALLESNSFFgGKTGPY-----------EMPR-----------ERSID---------- 209
|
250 260
....*....|....*....|.
gi 896542980 231 pepfpagIDTPEDLERAEALL 251
Cdd:cd02513 210 -------IDTEEDFELAEALL 223
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
1-123 |
1.42e-10 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 59.83 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 1 MTEFVVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQA-GAGEVWVAT----DDQRIADAlsgLAEVKVAMTATSHA 75
Cdd:COG1861 1 MMKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSkLIDEVVVATttdpADDPLVDL---AKELGVPVFRGSED 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 896542980 76 SGTDRLAECARIAGWvddTVVVNLQGDEPFAPAAGIRAVAEALVEGNA 123
Cdd:COG1861 78 DVLSRYYQAAEAYGA---DVVVRITGDCPLIDPALIDELIAAFLESGA 122
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
5-123 |
1.05e-07 |
|
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: 51.42 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 5 VVAIPARYAASRLPGKPLRLLGGEPLVLHVARRALQA-GAGEVWVATDDQRIADALSGLAE---VKVAmtatsHASGTD- 79
Cdd:cd02518 1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSkLIDEIVIATSTNEEDDPLEALAKklgVKVF-----RGSEEDv 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 896542980 80 --RLAECARIAGwVDdtVVVNLQGDEPFAPAAGIRAVAEALVEGNA 123
Cdd:cd02518 76 lgRYYQAAEEYN-AD--VVVRITGDCPLIDPEIIDAVIRLFLKSGA 118
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
13-124 |
1.08e-06 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 47.85 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 13 AASRLPG-KPLRLLGGEPLVLHVARRALQAGAGEVWVAT--DDQRIADALSGLaEVKVAMT-------ATSHASGTDRLA 82
Cdd:COG2068 13 ASSRMGRpKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgaDAEEVAAALAGL-GVRVVVNpdweegmSSSLRAGLAALP 91
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 896542980 83 ECAriagwvdDTVVVNLqGDEPFAPAAGIRAVAEALVEGNAP 124
Cdd:COG2068 92 ADA-------DAVLVLL-GDQPLVTAETLRRLLAAFRESPAS 125
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
13-125 |
1.07e-05 |
|
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: 44.86 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 13 AASRLPG-KPLRLLGGEPLVLHVARRALQAGAGEVWVAT--DDQRIADALSGLAEVKVA-------MtATSHASGTDRLA 82
Cdd:cd04182 10 RSSRMGGnKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgaEADAVRAALAGLPVVVVInpdweegM-SSSLAAGLEALP 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 896542980 83 ECAriagwvdDTVVVNLqGDEPFAPAAGIRAVAEALVEGNAPM 125
Cdd:cd04182 89 ADA-------DAVLILL-ADQPLVTAETLRALIDAFREDGAGI 123
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
15-136 |
3.01e-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: 44.63 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 15 SRLPgKPLRLLGGEPLVLHVARRALQAGAGEVWVATDDQR--IADALSGLaEVKVAMTA----TSHAsgtdrlAECAR-- 86
Cdd:COG1207 18 SKLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAeqVRAALADL-DVEFVLQEeqlgTGHA------VQQALpa 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 896542980 87 IAGWVDDTVVVNlqGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVEDAH 136
Cdd:COG1207 90 LPGDDGTVLVLY--GDVPLIRAETLKALLAAHRAAGAAATVLTAELDDPT 137
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
15-134 |
3.41e-05 |
|
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: 43.66 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 15 SRLPgKPLRLLGGEPLVLHVARRALQAGAGEVWVATDDQR--IADALSGLaEVKVA----MTATSHAsgtdrlAECAR-- 86
Cdd:cd02540 14 SDLP-KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAeqVKKALANP-NVEFVlqeeQLGTGHA------VKQALpa 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 896542980 87 IAGWVDDTVVVNlqGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVED 134
Cdd:cd02540 86 LKDFEGDVLVLY--GDVPLITPETLQRLLEAHREAGADVTVLTAELED 131
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
15-123 |
1.53e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 42.54 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 15 SRLPgKPLRLLGGEPLVLHVARRALQAGAGEVWVAT--DDQRIADALSGLAevKVAMTA-------TSHASGTDRLAeca 85
Cdd:PRK14353 21 SSLP-KVLHPVAGRPMLAHVLAAAASLGPSRVAVVVgpGAEAVAAAAAKIA--PDAEIFvqkerlgTAHAVLAAREA--- 94
|
90 100 110
....*....|....*....|....*....|....*...
gi 896542980 86 rIAGWVDDTVVVNlqGDEPFAPAAGIRAVAEALVEGNA 123
Cdd:PRK14353 95 -LAGGYGDVLVLY--GDTPLITAETLARLRERLADGAD 129
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
13-139 |
1.44e-03 |
|
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: 38.33 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 13 AASRLPG-KPLRLLGGEPLVLHVARRALQAGaGEVWVATDDQRIADALSGLaEVKVAMTATSH---ASGtdrLAECARIA 88
Cdd:pfam12804 8 RSSRMGGdKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALAGL-GVPVVPDPDPGqgpLAG---LLAALRAA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 896542980 89 GWVDDTVVVNlqGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVEDAHTLF 139
Cdd:pfam12804 83 PGADAVLVLA--CDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGHPLL 131
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
15-136 |
3.77e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 38.38 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896542980 15 SRLPgKPLRLLGGEPLVLHV--ARRALQAGAGEVWVATDDQRIADALSGLAEvKVAMTATSHASGTDRLAECA--RIAGW 90
Cdd:PRK14352 20 SDTP-KVLHTLAGRSMLGHVlhAAAGLAPQHLVVVVGHDRERVAPAVAELAP-EVDIAVQDEQPGTGHAVQCAleALPAD 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 896542980 91 VDDTVVVnLQGDEPFAPAAGIRAVAEALVEGNAPMSTLATTVEDAH 136
Cdd:PRK14352 98 FDGTVVV-TAGDVPLLDGETLADLVATHTAEGNAVTVLTTTLDDPT 142
|
|
| |
