|
Name |
Accession |
Description |
Interval |
E-value |
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
1-247 |
3.21e-135 |
|
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: 380.56 E-value: 3.21e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 1 MK-HIVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRL 79
Cdd:COG1212 1 MKfIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 80 SEVARIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRA 159
Cdd:COG1212 81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 160 TIPYDRDGAklterKLHNHAYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANlPPGVDTQA 239
Cdd:COG1212 161 PIPYPRDAF-----AEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAP-PIGVDTPE 234
|
....*...
gi 491150613 240 DLDRLNQM 247
Cdd:COG1212 235 DLERVRAL 242
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-247 |
6.20e-129 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 364.82 E-value: 6.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 1 MK-HIVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVqGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRL 79
Cdd:PRK05450 1 MKfLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKA-GADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 80 SEVARIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPAsSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRA 159
Cdd:PRK05450 80 AEAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEA-DMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 160 TIPYDRDGAKLTErklHNHAYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANLPPGVDTQA 239
Cdd:PRK05450 159 PIPYGRDAFADSA---PTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPE 235
|
....*...
gi 491150613 240 DLDRLNQM 247
Cdd:PRK05450 236 DLERVRAL 243
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
4-247 |
4.51e-122 |
|
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: 347.15 E-value: 4.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVA 83
Cdd:cd02517 4 VVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIAEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 84 RIKGWDaDDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRATIPY 163
Cdd:cd02517 84 EKLDAD-DDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSPIPY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRDGAKLTerklhnHAYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANlPPGVDTQADLDR 243
Cdd:cd02517 163 PRDSSEDF------PYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHE-SIGVDTPEDLER 235
|
....
gi 491150613 244 LNQM 247
Cdd:cd02517 236 VEAL 239
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
4-242 |
1.13e-79 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 239.82 E-value: 1.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKvQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVA 83
Cdd:TIGR00466 2 VIIPARLASSRLPGKPLEDIFGKPMIVHVAENANE-SGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 84 RIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPAsSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRATIPY 163
Cdd:TIGR00466 81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNV-PMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRD-GAKLTERKLHNHaYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANLPPGVDTQADLD 242
Cdd:TIGR00466 160 DRDfFAKRQTPVGDNL-LRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-222 |
1.34e-61 |
|
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: 192.94 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVA 83
Cdd:pfam02348 2 AIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 84 RIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRATIPY 163
Cdd:pfam02348 82 KAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIPY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRDGAKLterkLHNHAYRHLGLYAYRVKL-LQEYVTWDMGLLEKLESLEQLRVLENGHQI 222
Cdd:pfam02348 162 IREHPAE----LYYVYLRHIGIYTFRKNMpLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
1-247 |
3.21e-135 |
|
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: 380.56 E-value: 3.21e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 1 MK-HIVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRL 79
Cdd:COG1212 1 MKfIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 80 SEVARIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRA 159
Cdd:COG1212 81 AEAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 160 TIPYDRDGAklterKLHNHAYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANlPPGVDTQA 239
Cdd:COG1212 161 PIPYPRDAF-----AEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAP-PIGVDTPE 234
|
....*...
gi 491150613 240 DLDRLNQM 247
Cdd:COG1212 235 DLERVRAL 242
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-247 |
6.20e-129 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 364.82 E-value: 6.20e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 1 MK-HIVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVqGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRL 79
Cdd:PRK05450 1 MKfLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKA-GADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 80 SEVARIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPAsSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRA 159
Cdd:PRK05450 80 AEAAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEA-DMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 160 TIPYDRDGAKLTErklHNHAYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANLPPGVDTQA 239
Cdd:PRK05450 159 PIPYGRDAFADSA---PTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTPE 235
|
....*...
gi 491150613 240 DLDRLNQM 247
Cdd:PRK05450 236 DLERVRAL 243
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
4-247 |
4.51e-122 |
|
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: 347.15 E-value: 4.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVA 83
Cdd:cd02517 4 VVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIAEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 84 RIKGWDaDDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRATIPY 163
Cdd:cd02517 84 EKLDAD-DDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSPIPY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRDGAKLTerklhnHAYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANlPPGVDTQADLDR 243
Cdd:cd02517 163 PRDSSEDF------PYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHE-SIGVDTPEDLER 235
|
....
gi 491150613 244 LNQM 247
Cdd:cd02517 236 VEAL 239
|
|
| PRK13368 |
PRK13368 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
4-243 |
1.73e-90 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 184007 Cd Length: 238 Bit Score: 267.22 E-value: 1.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVA 83
Cdd:PRK13368 5 VVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRLAEVM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 84 RIKGwdaDDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRATIPY 163
Cdd:PRK13368 85 LKIE---ADIYINVQGDEPMIRPRDIDTLIQPMLDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRSPIPS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRDGAKlterklhNHAYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIaVAEANLPPGVDTQADLDR 243
Cdd:PRK13368 162 RRDGES-------ARYLKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRM-VEVAATSIGVDTPEDLER 233
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
4-242 |
1.13e-79 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 239.82 E-value: 1.13e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKvQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVA 83
Cdd:TIGR00466 2 VIIPARLASSRLPGKPLEDIFGKPMIVHVAENANE-SGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 84 RIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPAsSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRATIPY 163
Cdd:TIGR00466 81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNV-PMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRD-GAKLTERKLHNHaYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQIAIAVAEANLPPGVDTQADLD 242
Cdd:TIGR00466 160 DRDfFAKRQTPVGDNL-LRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQEDLE 238
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-222 |
1.34e-61 |
|
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: 192.94 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVA 83
Cdd:pfam02348 2 AIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 84 RIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSIVKVVMSKHNQALYFSRATIPY 163
Cdd:pfam02348 82 KAFLNDHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIPY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRDGAKLterkLHNHAYRHLGLYAYRVKL-LQEYVTWDMGLLEKLESLEQLRVLENGHQI 222
Cdd:pfam02348 162 IREHPAE----LYYVYLRHIGIYTFRKNMpLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| PLN02917 |
PLN02917 |
CMP-KDO synthetase |
5-244 |
2.96e-50 |
|
CMP-KDO synthetase
Pssm-ID: 215495 Cd Length: 293 Bit Score: 166.16 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 5 VIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPSGTDRLSEVar 84
Cdd:PLN02917 51 IIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEA-- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 85 IKGWDAD-DIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHSLDEFLRDSiVKVVMSKHNQALYFSRATIPY 163
Cdd:PLN02917 129 LKKLEKKyDIVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNR-VKCVVDNQGYAIYFSRGLIPY 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 164 DRDGaKLTERKLHnhaYRHLGLYAYRVKLLQEYVTWDMGLLEKLESLEQLRVLENGHQI-AIAV-AEANlppGVDTQADL 241
Cdd:PLN02917 208 NKSG-KVNPQFPY---LLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMkVIKVdHEAH---GVDTPEDV 280
|
...
gi 491150613 242 DRL 244
Cdd:PLN02917 281 EKI 283
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
4-130 |
2.06e-23 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 94.89 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVAT----DDERIAEVCRAEGIDV-------VLtsadh 72
Cdd:COG1861 6 AIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSKLIDEVVVATttdpADDPLVDLAKELGVPVfrgseddVL----- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 491150613 73 psgtDRLSEVARIKGWdadDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEP 130
Cdd:COG1861 81 ----SRYYQAAEAYGA---DVVVRITGDCPLIDPALIDELIAAFLESGADYVSNSLPR 131
|
|
| NeuA |
COG1083 |
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ... |
5-151 |
2.02e-19 |
|
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440700 Cd Length: 228 Bit Score: 83.67 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 5 VIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVL----TSADHPSGTDRLS 80
Cdd:COG1083 6 IIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLrpaeLAGDTASTIDVIL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491150613 81 EV-ARIKGWDAD-DIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSEPIHS-LDEFLRDSIVKVVMSKHN 151
Cdd:COG1083 86 HAlEWLEEQGEEfDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPpYWALKLDEDGRLEPLNPD 159
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
4-121 |
2.41e-19 |
|
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: 83.78 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVAT----DDERIAEVCRAEGIDVVLTSADHPsgTDRL 79
Cdd:cd02518 2 AIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstneEDDPLEALAKKLGVKVFRGSEEDV--LGRY 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491150613 80 SEVARIKGwdaDDIIVNVQGDEPLLPSLLVKQVAQLLEDQPA 121
Cdd:cd02518 80 YQAAEEYN---ADVVVRITGDCPLIDPEIIDAVIRLFLKSGA 118
|
|
| CMP-NeuAc_Synthase |
cd02513 |
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ... |
5-123 |
6.19e-18 |
|
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: 79.50 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 5 VIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVL-----TSADHPSGTDRL 79
Cdd:cd02513 5 IIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEVPFlrpaeLATDTASSIDVI 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491150613 80 SEVARI---KGWDAdDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASS 123
Cdd:cd02513 85 LHALDQleeLGRDF-DIVVLLQPTSPLRSAEDIDEAIELLLSEGADS 130
|
|
| PseF |
TIGR03584 |
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ... |
5-129 |
2.19e-11 |
|
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: 61.58 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 5 VIPARFSSSRLPGKPLLEIHGRPMILRVVDQAKKVQGFDDLCVATDDERIAEVCRAEGIDVVLT-----SADHPSGTDRL 79
Cdd:TIGR03584 3 IIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVPFLrpkelADDFTGTAPVV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491150613 80 SEVA-RIKGWDADDIIVNVQGDEPLLPSLLVKQVAQLLEDQPASSMSTLSE 129
Cdd:TIGR03584 83 KHAIeELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTS 133
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
13-71 |
2.66e-09 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 55.28 E-value: 2.66e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491150613 13 SRL--PGKPLLEIHGRPMILRVVDQAKKVqGFDDLCVAT--DDERIAEVCRAEGIDVVLTSAD 71
Cdd:COG2266 7 TRLggGEKPLLEICGKPMIDRVIDALEES-CIDKIYVAVspNTPKTREYLKERGVEVIETPGE 68
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
4-122 |
2.20e-08 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 52.47 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPG-KPLLEIHGRPMILRVVDQAKKVqGFDDLCVAT--DDERIAEVCRAEGIDVVLtSADHPSGtdrLS 80
Cdd:COG2068 6 AIILAAGASSRMGRpKLLLPLGGKPLLERAVEAALAA-GLDPVVVVLgaDAEEVAAALAGLGVRVVV-NPDWEEG---MS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491150613 81 E-----VARIKGwDADDIIVNVqGDEPLLPSLLVKQVAQLLEDQPAS 122
Cdd:COG2068 81 SslragLAALPA-DADAVLVLL-GDQPLVTAETLRRLLAAFRESPAS 125
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
12-121 |
1.08e-07 |
|
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: 49.89 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 12 SSRLPG-KPLLEIHGRPMILRVVDQAKKVqgFDDLCVATDDERIAEVCRAEGIDVVLTSADHP-------SGTDRLSeva 83
Cdd:pfam12804 9 SSRMGGdKALLPLGGKPLLERVLERLRPA--GDEVVVVANDEEVLAALAGLGVPVVPDPDPGQgplagllAALRAAP--- 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 491150613 84 rikgwDADDIIVnVQGDEPLLPSLLVKQVAQLLEDQPA 121
Cdd:pfam12804 84 -----GADAVLV-LACDMPFLTPELLRRLLAAAEESGA 115
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
13-126 |
1.73e-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: 44.43 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 13 SRLPgKPLLEIHGRPMILRVVDQAKKVqGFDDLCVAT--DDERIAEVCRAEGIDVVLTsaDHPSGTDRLSEVARIKGWDA 90
Cdd:cd02540 14 SDLP-KVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVghGAEQVKKALANPNVEFVLQ--EEQLGTGHAVKQALPALKDF 89
|
90 100 110
....*....|....*....|....*....|....*..
gi 491150613 91 DDIIVNVQGDEPLL-PSLLVKQVAQLLEDQPASSMST 126
Cdd:cd02540 90 EGDVLVLYGDVPLItPETLQRLLEAHREAGADVTVLT 126
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
4-61 |
2.72e-05 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 44.17 E-value: 2.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491150613 4 IVIPARFSSSR-------LPgKPLLEIHGRPMILRVVDQAKKVqgfddlcvatDDERIAEVCRAE 61
Cdd:cd04183 1 IIIPMAGLGSRfkkagytYP-KPLIEVDGKPMIEWVIESLAKI----------FDSRFIFICRDE 54
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
4-122 |
2.94e-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: 43.32 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 4 IVIPARFSSSRLPG-KPLLEIHGRPMILRVVDQAKKVqGFDDLCVATDDERIAEVCRAEGIDVVLTSADHPS-------- 74
Cdd:cd04182 3 AIILAAGRSSRMGGnKLLLPLDGKPLLRHALDAALAA-GLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEegmsssla 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 491150613 75 -GTDRLSEvarikgwDADDIIVNVqGDEPLLPSLLVKQVAQLLEDQPAS 122
Cdd:cd04182 82 aGLEALPA-------DADAVLILL-ADQPLVTAETLRALIDAFREDGAG 122
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
18-100 |
2.49e-04 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 41.03 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 18 KPLLEIHGRPMILRVVDQAKKVqGFDDLCVAT--DDERIAEV---CRAEGIDVVLTSADHPSGTdrLSEVARIKGWDADD 92
Cdd:cd04181 21 KPLLPIAGKPILEYIIERLARA-GIDEIILVVgyLGEQIEEYfgdGSKFGVNIEYVVQEEPLGT--AGAVRNAEDFLGDD 97
|
....*...
gi 491150613 93 IIVNVQGD 100
Cdd:cd04181 98 DFLVVNGD 105
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
12-66 |
5.57e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 36.71 E-value: 5.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491150613 12 SSRLPG-KPLLEIHGRPMILRVVDQAKKVqgFDDLCVATDDEriaEVCRAEGIDVV 66
Cdd:COG0746 15 SRRMGQdKALLPLGGRPLLERVLERLRPQ--VDEVVIVANRP---ERYAALGVPVV 65
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
18-49 |
6.06e-03 |
|
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: 36.83 E-value: 6.06e-03
10 20 30
....*....|....*....|....*....|..
gi 491150613 18 KPLLEIHGRPMILRVVDQAKKvQGFDDLCVAT 49
Cdd:cd02523 21 KCLLEINGKPLLERQIETLKE-AGIDDIVIVT 51
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
13-104 |
8.03e-03 |
|
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: 37.31 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491150613 13 SRLPgKPLLEIHGRPMILRVVDQAKKVqGFDDLCVAT--DDERIAEVCRAEGIDVVLTsaDHPSGTDRLSEVAR--IKGW 88
Cdd:COG1207 18 SKLP-KVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVghGAEQVRAALADLDVEFVLQ--EEQLGTGHAVQQALpaLPGD 93
|
90
....*....|....*.
gi 491150613 89 DADDIIVNvqGDEPLL 104
Cdd:COG1207 94 DGTVLVLY--GDVPLI 107
|
|
| |
