|
Name |
Accession |
Description |
Interval |
E-value |
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
5-238 |
1.97e-122 |
|
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: 347.82 E-value: 1.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 5 ILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRIIE 84
Cdd:COG1212 3 FIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 85 VAEK--FPNYGIIVNIQGDEPGMEPNLIEGVLALKTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPI 162
Cdd:COG1212 83 AAEKlgLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRAPI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490924573 163 PA---SFKGEATYHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKANLGVDSPADLEVVIR 238
Cdd:COG1212 163 PYprdAFAEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAPPIGVDTPEDLERVRA 241
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
4-238 |
7.68e-117 |
|
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: 333.67 E-value: 7.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 4 QILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRII 83
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 84 EVAEKFP-NYGIIVNIQGDEPGMEPNLIEGVLALKTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPI 162
Cdd:cd02517 81 EVAEKLDaDDDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSPI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490924573 163 PASFKG--EATYHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKANLGVDSPADLEVVIR 238
Cdd:cd02517 161 PYPRDSseDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHESIGVDTPEDLERVEA 238
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
4-241 |
5.06e-116 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 331.70 E-value: 5.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 4 QILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSkSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRII 83
Cdd:PRK05450 2 KFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKA-GADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 84 EVAEK--FPNYGIIVNIQGDEPGMEPNLIEGVLALkTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSP 161
Cdd:PRK05450 81 EAAAKlgLADDDIVVNVQGDEPLIPPEIIDQVAEP-LANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 162 IPASFKGEA-----TYHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKA-NLGVDSPADLEV 235
Cdd:PRK05450 160 IPYGRDAFAdsaptPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEApSIGVDTPEDLER 239
|
....*.
gi 490924573 236 VIRDFK 241
Cdd:PRK05450 240 VRALLA 245
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
8-234 |
6.87e-64 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 199.37 E-value: 6.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 8 VIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSkSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRIIEVAE 87
Cdd:TIGR00466 3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANES-GADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 88 K--FPNYGIIVNIQGDEPGMEPNLIEGVLALKTKhRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPIP-- 163
Cdd:TIGR00466 82 KlaLKDDERIVNLQGDEPFIPKEIIRQVADNLAT-KNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPfd 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490924573 164 --ASFKGEAT----YHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLS-DKANLGVDSPADLE 234
Cdd:TIGR00466 161 rdFFAKRQTPvgdnLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAqEVPSVGVDTQEDLE 238
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
6-215 |
6.49e-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: 183.31 E-value: 6.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 6 LGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRIIEV 85
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 86 AEKFPNY--GIIVNIQGDEPGMEPNLIEGVLALKTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPIP 163
Cdd:pfam02348 81 VKAFLNDhdDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490924573 164 ASFKGEA----TYHRHLGIYAYE-REFLMKYNHLPASDWETVESLEQLRALQNGSTI 215
Cdd:pfam02348 161 YIREHPAelyyVYLRHIGIYTFRkNMPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
5-238 |
1.97e-122 |
|
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: 347.82 E-value: 1.97e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 5 ILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRIIE 84
Cdd:COG1212 3 FIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 85 VAEK--FPNYGIIVNIQGDEPGMEPNLIEGVLALKTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPI 162
Cdd:COG1212 83 AAEKlgLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYFSRAPI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490924573 163 PA---SFKGEATYHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKANLGVDSPADLEVVIR 238
Cdd:COG1212 163 PYprdAFAEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAPPIGVDTPEDLERVRA 241
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
4-238 |
7.68e-117 |
|
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: 333.67 E-value: 7.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 4 QILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRII 83
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 84 EVAEKFP-NYGIIVNIQGDEPGMEPNLIEGVLALKTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPI 162
Cdd:cd02517 81 EVAEKLDaDDDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFSRSPI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490924573 163 PASFKG--EATYHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKANLGVDSPADLEVVIR 238
Cdd:cd02517 161 PYPRDSseDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHESIGVDTPEDLERVEA 238
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
4-241 |
5.06e-116 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 331.70 E-value: 5.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 4 QILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSkSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRII 83
Cdd:PRK05450 2 KFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKA-GADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 84 EVAEK--FPNYGIIVNIQGDEPGMEPNLIEGVLALkTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSP 161
Cdd:PRK05450 81 EAAAKlgLADDDIVVNVQGDEPLIPPEIIDQVAEP-LANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSRAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 162 IPASFKGEA-----TYHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKA-NLGVDSPADLEV 235
Cdd:PRK05450 160 IPYGRDAFAdsaptPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEEApSIGVDTPEDLER 239
|
....*.
gi 490924573 236 VIRDFK 241
Cdd:PRK05450 240 VRALLA 245
|
|
| PRK13368 |
PRK13368 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
5-238 |
4.91e-89 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 184007 Cd Length: 238 Bit Score: 262.98 E-value: 4.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 5 ILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRIIE 84
Cdd:PRK13368 3 VVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRLAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 85 VAEKFpNYGIIVNIQGDEPGMEPNLIEGVLALKTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPIPA 164
Cdd:PRK13368 83 VMLKI-EADIYINVQGDEPMIRPRDIDTLIQPMLDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYFSRSPIPS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490924573 165 SFKGE-ATYHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKANLGVDSPADLEVVIR 238
Cdd:PRK13368 162 RRDGEsARYLKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRMVEVAATSIGVDTPEDLERVRA 236
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
8-234 |
6.87e-64 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 199.37 E-value: 6.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 8 VIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSkSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRIIEVAE 87
Cdd:TIGR00466 3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANES-GADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 88 K--FPNYGIIVNIQGDEPGMEPNLIEGVLALKTKhRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPIP-- 163
Cdd:TIGR00466 82 KlaLKDDERIVNLQGDEPFIPKEIIRQVADNLAT-KNVPMAALAVKIHDAEEAFNPNAVKVVLDSQGYALYFSRSLIPfd 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490924573 164 --ASFKGEAT----YHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLS-DKANLGVDSPADLE 234
Cdd:TIGR00466 161 rdFFAKRQTPvgdnLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAqEVPSVGVDTQEDLE 238
|
|
| PLN02917 |
PLN02917 |
CMP-KDO synthetase |
4-245 |
9.37e-64 |
|
CMP-KDO synthetase
Pssm-ID: 215495 Cd Length: 293 Bit Score: 200.83 E-value: 9.37e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 4 QILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRII 83
Cdd:PLN02917 47 RVVGIIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 84 EVAEKF-PNYGIIVNIQGDEPGMEPNLIEG-VLALKTKHRnwEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSP 161
Cdd:PLN02917 127 EALKKLeKKYDIVVNIQGDEPLIEPEIIDGvVKALQAAPD--AVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 162 IPASFKGEAT----YHRHLGIYAYEREFLMKYNHLPASDWETVESLEQLRALQNGSTIGVYLSDKANLGVDSPADLEVVI 237
Cdd:PLN02917 205 IPYNKSGKVNpqfpYLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKVIKVDHEAHGVDTPEDVEKIE 284
|
....*...
gi 490924573 238 RDFKEKGL 245
Cdd:PLN02917 285 ALMRERNI 292
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
6-215 |
6.49e-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: 183.31 E-value: 6.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 6 LGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSPDHPTGTDRIIEV 85
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 86 AEKFPNY--GIIVNIQGDEPGMEPNLIEGVLALKTKHRNWEMTTAAVPFTASEDPKDPNKVKVVFDRNARANYFSRSPIP 163
Cdd:pfam02348 81 VKAFLNDhdDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490924573 164 ASFKGEA----TYHRHLGIYAYE-REFLMKYNHLPASDWETVESLEQLRALQNGSTI 215
Cdd:pfam02348 161 YIREHPAelyyVYLRHIGIYTFRkNMPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| CMP-NeuAc_Synthase |
cd02513 |
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ... |
5-236 |
1.04e-19 |
|
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: 84.13 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 5 ILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSP-----DHPTGT 79
Cdd:cd02513 2 ILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAEVPFLRPaelatDTASSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 80 DRIIEVAEKFPN----YGIIVNIQGDEPGMEPNLIEGVLALKTKHRnwemttAAVPFTASEDPKDPNKVKVVFDRNARAN 155
Cdd:cd02513 82 DVILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSEG------ADSVFSVTEFHRFPWRALGLDDNGLEPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 156 YFSRSPIPASFKGEATYHRHLGIYAYEREFLMKYNHlpasdwetvesleqlraLQNGSTIGVYLSDKANLGVDSPADLEV 235
Cdd:cd02513 156 NYPEDKRTRRQDLPPAYHENGAIYIAKREALLESNS-----------------FFGGKTGPYEMPRERSIDIDTEEDFEL 218
|
.
gi 490924573 236 V 236
Cdd:cd02513 219 A 219
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
6-236 |
1.84e-18 |
|
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: 81.08 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 6 LGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISF---GGESVFT-SPDHPtgTDR 81
Cdd:cd02518 1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATSTNEEDDPLEALakkLGVKVFRgSEEDV--LGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 82 IIEVAEKFpNYGIIVNIQGDEPGMEPNLIEGVLALKTKHrNWEMTTAAVPFTAS-----EdpkdpnkvkvVFDRNA--RA 154
Cdd:cd02518 79 YYQAAEEY-NADVVVRITGDCPLIDPEIIDAVIRLFLKS-GADYTSNTLPRTYPdgldvE----------VFTRDAleRA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 155 NYFSRSPipasfkgeaTYHRHLGIYAYEREFLMKYNHLPASDwetvESLEQLRalqngstigvylsdkanLGVDSPADLE 234
Cdd:cd02518 147 AAEADDP---------YEREHVTPYIRRHPELFRIGYLEAPP----DRLSDLR-----------------LTVDTPEDFE 196
|
..
gi 490924573 235 VV 236
Cdd:cd02518 197 LI 198
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
4-236 |
1.26e-14 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 71.00 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 4 QILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGE---SVFT-SPDhptgt 79
Cdd:COG1861 3 KIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSKLIDEVVVATTTDPADDPLVDLAKElgvPVFRgSED----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 80 D---RIIEVAEKFpNYGIIVNIQGDEPGMEPNLIEGVLAlKTKHRNWEMTTAAVPFT-----ASEdpkdpnkvkvVFDRN 151
Cdd:COG1861 78 DvlsRYYQAAEAY-GADVVVRITGDCPLIDPALIDELIA-AFLESGADYVSNSLPRTyprglDVE----------VFSFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 152 A--RANYFSRSPipasfkgeatYHR-HLGIYAYEREFLMKYNHLPASdwetvESLEQLRalqngstigvylsdkanLGVD 228
Cdd:COG1861 146 AleRAWEEAKLP----------SEReHVTPYIYEHPDRFRIGNVEPP-----EDLSDLR-----------------LTVD 193
|
....*...
gi 490924573 229 SPADLEVV 236
Cdd:COG1861 194 TPEDLELI 201
|
|
| NeuA |
COG1083 |
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ... |
5-192 |
9.46e-13 |
|
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440700 Cd Length: 228 Bit Score: 65.57 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 5 ILGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGEsVFTSP-----DHPTGT 79
Cdd:COG1083 3 ILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAE-VFLRPaelagDTASTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 80 DRIIEVAEKFPNYG----IIVNIQGDEPGMEPNLIEGVLALktkhrnWEMTTAAVPFTASEDPKDPNK-VKVVFDRNARA 154
Cdd:COG1083 82 DVILHALEWLEEQGeefdYVVLLQPTSPLRTAEDIDEAIEL------LLESGADSVVSVTEAHHPPYWaLKLDEDGRLEP 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 490924573 155 NYFSRSPIPASFKGEATYHRHLGIYAYEREFLMKYNHL 192
Cdd:COG1083 156 LNPDPHNRPRRQDLPPAYRENGAIYIFKREALLENKSR 193
|
|
| PseF |
TIGR03584 |
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ... |
6-135 |
7.23e-08 |
|
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: 51.56 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490924573 6 LGVIPARFASTRFPGKPLALIGTKPMIQWTYHHASLSKSIHRLVVATDDRRIHDTVISFGGESVFTSP-----DHPTGTD 80
Cdd:TIGR03584 1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVPFLRPkeladDFTGTAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 490924573 81 RI---IEVAEKFPNYGIIVNIQGDEPGMEPN-LIEGVLALKTKHRNWEMTtaAVPFTAS 135
Cdd:TIGR03584 81 VVkhaIEELKLQKQYDHACCIYATAPFLQAKiLKEAFELLKQPNAHFVFS--VTSFAFP 137
|
|
| |
