|
Name |
Accession |
Description |
Interval |
E-value |
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
4-245 |
2.45e-149 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 416.62 E-value: 2.45e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 4 TVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLAEVV 83
Cdd:TIGR00466 1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 84 EKLAIPDNEIIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIPYD 163
Cdd:TIGR00466 81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 164 RDQF*NLQDVQKvqlsDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAKEVPAVGVDTAED 243
Cdd:TIGR00466 161 RDFFAKRQTPVG----DNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQED 236
|
..
1VH3_A 244 LE 245
Cdd:TIGR00466 237 LE 238
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
2-252 |
8.44e-149 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 415.28 E-value: 8.44e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLAE 81
Cdd:PRK05450 2 KFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 82 VVEKLAIPDNEIIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIP 161
Cdd:PRK05450 82 AAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 162 YDRDQF*NLQDvqkvqlsDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAKEVPAVGVDTA 241
Cdd:PRK05450 162 YGRDAFADSAP-------TPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTP 234
|
250
....*....|.
1VH3_A 242 EDLEKVRAILA 252
Cdd:PRK05450 235 EDLERVRALLA 245
|
|
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
2-250 |
1.51e-140 |
|
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: 394.43 E-value: 1.51e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQS-GASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLA 80
Cdd:COG1212 2 KFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 81 EVVEKLAIPDNEIIVNIQGDEPLIPPVIVRQVADNLAKF-NVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSV 159
Cdd:COG1212 82 EAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDpEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 160 IPYDRDQF*NlqdvqkvqlSDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAkEVPAVGVD 239
Cdd:COG1212 162 IPYPRDAFAE---------DGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVD 231
|
250
....*....|.
1VH3_A 240 TAEDLEKVRAI 250
Cdd:COG1212 232 TPEDLERVRAL 242
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
2-250 |
1.19e-127 |
|
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: 361.41 E-value: 1.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQS-GASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLA 80
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 81 EVVEKLAIPDnEIIVNIQGDEPLIPPVIVRQVADNLAK-FNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSV 159
Cdd:cd02517 81 EVAEKLDADD-DIVVNVQGDEPLIPPEMIDQVVAALKDdPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 160 IPYDRDQF*NLQdvqkvqlsdaYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAKEVPaVGVD 239
Cdd:cd02517 160 IPYPRDSSEDFP----------YYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHES-IGVD 228
|
250
....*....|.
1VH3_A 240 TAEDLEKVRAI 250
Cdd:cd02517 229 TPEDLERVEAL 239
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-225 |
2.63e-89 |
|
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.
Pssm-ID: 396773 Cd Length: 217 Bit Score: 263.81 E-value: 2.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 4 TVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGA-SRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLAEV 82
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 83 VEKLAIPDNEIIVNIQGDEPLIPP-VIVRQVADNLAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIP 161
Cdd:pfam02348 81 VKAFLNDHDDIIVNIQGDNPLLQPeVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1VH3_A 162 YDRDQF*NLQDVqkvqlsdaYLRHIGIYAYRAG-FIKQYVQWAPTQLENLEKLEQLRVLYNGERI 225
Cdd:pfam02348 161 YIREHPAELYYV--------YLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
4-245 |
2.45e-149 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 416.62 E-value: 2.45e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 4 TVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLAEVV 83
Cdd:TIGR00466 1 MVIIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 84 EKLAIPDNEIIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIPYD 163
Cdd:TIGR00466 81 EKLALKDDERIVNLQGDEPFIPKEIIRQVADNLATKNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 164 RDQF*NLQDVQKvqlsDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAKEVPAVGVDTAED 243
Cdd:TIGR00466 161 RDFFAKRQTPVG----DNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVPSVGVDTQED 236
|
..
1VH3_A 244 LE 245
Cdd:TIGR00466 237 LE 238
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
2-252 |
8.44e-149 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 415.28 E-value: 8.44e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLAE 81
Cdd:PRK05450 2 KFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 82 VVEKLAIPDNEIIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIP 161
Cdd:PRK05450 82 AAAKLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAPIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 162 YDRDQF*NLQDvqkvqlsDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAKEVPAVGVDTA 241
Cdd:PRK05450 162 YGRDAFADSAP-------TPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEAPSIGVDTP 234
|
250
....*....|.
1VH3_A 242 EDLEKVRAILA 252
Cdd:PRK05450 235 EDLERVRALLA 245
|
|
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
2-250 |
1.51e-140 |
|
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: 394.43 E-value: 1.51e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQS-GASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLA 80
Cdd:COG1212 2 KFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 81 EVVEKLAIPDNEIIVNIQGDEPLIPPVIVRQVADNLAKF-NVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSV 159
Cdd:COG1212 82 EAAEKLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDpEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 160 IPYDRDQF*NlqdvqkvqlSDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAkEVPAVGVD 239
Cdd:COG1212 162 IPYPRDAFAE---------DGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVET-DAPPIGVD 231
|
250
....*....|.
1VH3_A 240 TAEDLEKVRAI 250
Cdd:COG1212 232 TPEDLERVRAL 242
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
2-250 |
1.19e-127 |
|
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: 361.41 E-value: 1.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQS-GASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLA 80
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 81 EVVEKLAIPDnEIIVNIQGDEPLIPPVIVRQVADNLAK-FNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSV 159
Cdd:cd02517 81 EVAEKLDADD-DIVVNVQGDEPLIPPEMIDQVVAALKDdPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 160 IPYDRDQF*NLQdvqkvqlsdaYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVELAKEVPaVGVD 239
Cdd:cd02517 160 IPYPRDSSEDFP----------YYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHES-IGVD 228
|
250
....*....|.
1VH3_A 240 TAEDLEKVRAI 250
Cdd:cd02517 229 TPEDLERVEAL 239
|
|
| PRK13368 |
PRK13368 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
2-251 |
1.89e-98 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 184007 Cd Length: 238 Bit Score: 287.63 E-value: 1.89e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQS-GASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLA 80
Cdd:PRK13368 2 KVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAaGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 81 EVVEKLaipDNEIIVNIQGDEPLIPPVIVRQVADN-LAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSV 159
Cdd:PRK13368 82 EVMLKI---EADIYINVQGDEPMIRPRDIDTLIQPmLDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 160 IPYDRDqf*nlqdvqkvQLSDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVeLAKEVPAVGVD 239
Cdd:PRK13368 159 IPSRRD-----------GESARYLKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRM-VEVAATSIGVD 226
|
250
....*....|..
1VH3_A 240 TAEDLEKVRAIL 251
Cdd:PRK13368 227 TPEDLERVRAIM 238
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-225 |
2.63e-89 |
|
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.
Pssm-ID: 396773 Cd Length: 217 Bit Score: 263.81 E-value: 2.63e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 4 TVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGA-SRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLAEV 82
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAfEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 83 VEKLAIPDNEIIVNIQGDEPLIPP-VIVRQVADNLAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIP 161
Cdd:pfam02348 81 VKAFLNDHDDIIVNIQGDNPLLQPeVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1VH3_A 162 YDRDQF*NLQDVqkvqlsdaYLRHIGIYAYRAG-FIKQYVQWAPTQLENLEKLEQLRVLYNGERI 225
Cdd:pfam02348 161 YIREHPAELYYV--------YLRHIGIYTFRKNmPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| PLN02917 |
PLN02917 |
CMP-KDO synthetase |
6-253 |
3.35e-64 |
|
CMP-KDO synthetase
Pssm-ID: 215495 Cd Length: 293 Bit Score: 202.37 E-value: 3.35e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 6 IIPARFASSRLPGKPLADIKGKP*IQHVFEKA-LQSGASRVIIATDNENVADVAKSFGAEVC*TSVNHNSGTERLAEVVE 84
Cdd:PLN02917 51 IIPARFASSRFEGKPLVHILGKPMIQRTWERAkLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 85 KLAiPDNEIIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVKIHDAEELFNPNAVKVLTDKDGYVLYFSRSVIPYDR 164
Cdd:PLN02917 131 KLE-KKYDIVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGLIPYNK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 165 DQF*NLQdvqkvqlsDAYLRHIGIYAYRAGFIKQYVQWAPTQLENLEKLEQLRVLYNGERIHVeLAKEVPAVGVDTAEDL 244
Cdd:PLN02917 210 SGKVNPQ--------FPYLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKV-IKVDHEAHGVDTPEDV 280
|
....*....
1VH3_A 245 EKVRAILAA 253
Cdd:PLN02917 281 EKIEALMRE 289
|
|
| CMP-NeuAc_Synthase |
cd02513 |
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ... |
2-251 |
2.27e-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: 81.05 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGA-SRVIIATDNENVADVAKSFGAEVC-----*TSVNHNSG 75
Cdd:cd02513 1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLfDRVVVSTDDEEIAEVARKYGAEVPflrpaELATDTASS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 76 TERLAEVVEKL--AIPDNEIIVNIQGDEPLIPPVIVRQVadnLAKFNVN*ASLAVKIHDAEELFNPNavkVLTDKDGYVL 153
Cdd:cd02513 81 IDVILHALDQLeeLGRDFDIVVLLQPTSPLRSAEDIDEA---IELLLSEGADSVFSVTEFHRFPWRA---LGLDDNGLEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 154 YFsrsvipYDRDQF*NLQDvqkvqLSDAYLRHIGIYAYRAGFIKQYvqwaptqlenlekleqlRVLYNGERIHVELAKEV 233
Cdd:cd02513 155 VN------YPEDKRTRRQD-----LPPAYHENGAIYIAKREALLES-----------------NSFFGGKTGPYEMPRER 206
|
250
....*....|....*...
1VH3_A 234 pAVGVDTAEDLEKVRAIL 251
Cdd:cd02513 207 -SIDIDTEEDFELAEALL 223
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
5-129 |
4.24e-17 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 77.94 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 5 VIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQS-GASRVIIAT----DNENVADVAKSFGAEVC*TSVNhnsgtERL 79
Cdd:COG1861 6 AIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSkLIDEVVVATttdpADDPLVDLAKELGVPVFRGSEDdv--lSRY 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
1VH3_A 80 AEVVEKLaipDNEIIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVK 129
Cdd:COG1861 84 YQAAEAY---GADVVVRITGDCPLIDPALIDELIAAFLESGADYVSNSLP 130
|
|
| NeuA |
COG1083 |
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ... |
6-254 |
1.00e-15 |
|
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440700 Cd Length: 228 Bit Score: 74.04 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 6 IIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGA-SRVIIATDNENVADVAKSFGAEVC*----TSVNHNSGTERLA 80
Cdd:COG1083 6 IIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLfDRVVVSTDDEEIAEVAREYGAEVFLrpaeLAGDTASTIDVIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 81 EVVEKLAIPDN--EIIVNIQGDEPLIPPVIVRQVadnLAKFNVN*ASLAVKIHDAEelFNP-NAVKVltDKDGYVLYFSr 157
Cdd:COG1083 86 HALEWLEEQGEefDYVVLLQPTSPLRTAEDIDEA---IELLLESGADSVVSVTEAH--HPPyWALKL--DEDGRLEPLN- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 158 svipYDRDQF*NLQDvqkvqLSDAYLRHIGIYAYRAgfikqyvqwaptqlenlEKLEQLRVLYNGERIHVELAKEvPAVG 237
Cdd:COG1083 158 ----PDPHNRPRRQD-----LPPAYRENGAIYIFKR-----------------EALLENKSRFGGKTGAYEMPEE-RSVD 210
|
250
....*....|....*..
1VH3_A 238 VDTAEDLEKVRAILAAN 254
Cdd:COG1083 211 IDTEEDFELAEALLKKR 227
|
|
| PseF |
TIGR03584 |
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ... |
6-111 |
1.47e-14 |
|
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: 70.82 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 6 IIPARFASSRLPGKPLADIKGKP*IQHVFEKALQSGA-SRVIIATDNENVADVAKSFGAEV-----C*TSVNHNSGTERL 79
Cdd:TIGR03584 3 IIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLfDKVVVSTDDEEIAEVAKSYGASVpflrpKELADDFTGTAPVV 82
|
90 100 110
....*....|....*....|....*....|...
1VH3_A 80 AEVVEKLAI-PDNEIIVNIQGDEPLIPPVIVRQ 111
Cdd:TIGR03584 83 KHAIEELKLqKQYDHACCIYATAPFLQAKILKE 115
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
4-129 |
1.43e-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: 67.98 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 4 TVIIPARFASSRLPGKPLADIKGKP*IQHVFEKALQS-GASRVIIAT----DNENVADVAKSFGAEVC*TSVnhNSGTER 78
Cdd:cd02518 1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSkLIDEIVIATstneEDDPLEALAKKLGVKVFRGSE--EDVLGR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
1VH3_A 79 LAEVVEKlAIPDneIIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVK 129
Cdd:cd02518 79 YYQAAEE-YNAD--VVVRITGDCPLIDPEIIDAVIRLFLKSGADYTSNTLP 126
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
2-114 |
6.79e-07 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 48.62 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 2 SFTVIIPARFASSRLPG-KPLADIKGKP*IQHVFEKALQSGASRVIIAT--DNENVADVAKSFGAEVC*tsVNHNS---- 74
Cdd:COG2068 3 KVAAIILAAGASSRMGRpKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgaDAEEVAAALAGLGVRVV---VNPDWeegm 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
1VH3_A 75 ------GTERLAEVVEKLAIpdneiivnIQGDEPLIPPVIVRQVAD 114
Cdd:COG2068 80 ssslraGLAALPADADAVLV--------LLGDQPLVTAETLRRLLA 117
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
14-136 |
2.10e-06 |
|
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: 46.81 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 14 SRL--PGKPLADIKGKP*IQHVFEKALQSGASRVIIAT--DNENVADVAKSFGAEVC*TsvnhnSGT---ERLAEVVEKL 86
Cdd:COG2266 7 TRLggGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVspNTPKTREYLKERGVEVIET-----PGEgyvEDLNEALESI 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
1VH3_A 87 AIPdneiIVNIQGDEPLIPPVIVRQVADNLAKFNVN*ASLAVKIHDAEEL 136
Cdd:COG2266 82 SGP----VLVVPADLPLLTPEIIDDIIDAYLESGKPSLTVVVPAALKREL 127
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-114 |
4.07e-06 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 46.01 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 3 FTVIIPARFASSRLPG-KPLADIKGKP*IQHVFEKALQSGASRVIIATDNENVAdVAKSFGAEVC*TSVNHNSGTERLAE 81
Cdd:cd04182 1 IAAIILAAGRSSRMGGnKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADA-VRAALAGLPVVVVINPDWEEGMSSS 79
|
90 100 110
....*....|....*....|....*....|....*.
1VH3_A 82 V---VEKLAiPDNEIIVNIQGDEPLIPPVIVRQVAD 114
Cdd:cd04182 80 LaagLEALP-ADADAVLILLADQPLVTAETLRALID 114
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-252 |
5.37e-06 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 46.39 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 5 VIIPARFASSRL-------PgKPLADIKGKP*IQHVFEKALQSGASRVIIAT--DNENVADVAKSFGAEVc*TSVNH--- 72
Cdd:COG1213 2 AVILAAGRGSRLgpltddiP-KCLVEIGGKTLLERQLEALAAAGIKDIVVVTgyKAELIEEALARPGPDV-TFVYNPdyd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 73 ---NSGTerLAEVVEKLAipDNEIIVNiqGD---EPLIPPVIVRQVADNLakfnvn*asLAV---KIHDAEElfnpnAVK 143
Cdd:COG1213 80 etnNIYS--LWLAREALD--EDFLLLN--GDvvfDPAILKRLLASDGDIV---------LLVdrkWEKPLDE-----EVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 144 VLTDKDGYVLYFSRsvipydrdqf*nlqdvqKVQLSDAYLRHIGIYAYRAG----FIKQYVQWAPTQLENLEkLEQL--R 217
Cdd:COG1213 140 VRVDEDGRIVEIGK-----------------KLPPEEADGEYIGIFKFSAEgaaaLREALEALIDEGGPNLY-YEDAlqE 201
|
250 260 270
....*....|....*....|....*....|....*
1VH3_A 218 VLYNGERIHVELAKEVPAVGVDTAEDLEKVRAILA 252
Cdd:COG1213 202 LIDEGGPVKAVDIGGLPWVEIDTPEDLERAEELFA 236
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
12-118 |
1.15e-05 |
|
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: 44.49 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 12 ASSRLPG-KPLADIKGKP*IQHVFEkALQSGASRVIIATDNENVADVAKSFGAEVC*TSVNHN---SGterLAEVVEKLA 87
Cdd:pfam12804 8 RSSRMGGdKALLPLGGKPLLERVLE-RLRPAGDEVVVVANDEEVLAALAGLGVPVVPDPDPGQgplAG---LLAALRAAP 83
|
90 100 110
....*....|....*....|....*....|.
1VH3_A 88 IPDNEIIVNiqGDEPLIPPVIVRQVADNLAK 118
Cdd:pfam12804 84 GADAVLVLA--CDMPFLTPELLRRLLAAAEE 112
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
13-136 |
1.22e-04 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 41.71 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 13 SSRLPG--KPLADIKGKP*IQHVFEkALQSGASRVIIATdNENvADVAKSFGAEVC*TSVNHNSGTerLAEVVEKLAIPD 90
Cdd:PRK00317 14 SRRMGGvdKGLQELNGKPLIQHVIE-RLAPQVDEIVINA-NRN-LARYAAFGLPVIPDSLADFPGP--LAGILAGLKQAR 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
1VH3_A 91 NEIIVNIQGDEPLIPPVIVRQVADNLAKfnvN*ASLAVkIHDAEEL 136
Cdd:PRK00317 89 TEWVLVVPCDTPFIPPDLVARLAQAAGK---DDADVAW-AHDGGRL 130
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
14-128 |
2.27e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 39.07 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1VH3_A 14 SRLPgKPLADIKGKP*IQHVFEKALQSGASRVIIAT--DNENVADVAKSFGAEVc*TSVNhnsgTERL--AEVV----EK 85
Cdd:PRK14353 21 SSLP-KVLHPVAGRPMLAHVLAAAASLGPSRVAVVVgpGAEAVAAAAAKIAPDA-EIFVQ----KERLgtAHAVlaarEA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|...
1VH3_A 86 LAIPDNEIIVnIQGDEPLIPPVIVRQVADNLAkfnvN*ASLAV 128
Cdd:PRK14353 95 LAGGYGDVLV-LYGDTPLITAETLARLRERLA----DGADVVV 132
|
|
| |
