|
Name |
Accession |
Description |
Interval |
E-value |
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
1-246 |
4.17e-132 |
|
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: 372.47 E-value: 4.17e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAF--FSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRC 78
Cdd:COG1212 1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkgADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 79 REALDRIEAstgKRFDAVVNIQGDEPFVAEEQLRLITGCF-DDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYF 157
Cdd:COG1212 81 AEAAEKLGL---PDDDIVVNVQGDEPLIPPELIDAVAEPLaEDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 158 SRSAIPYLRgterDRWQRSHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSESLAIDTP 237
Cdd:COG1212 158 SRAPIPYPR----DAFAEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAPPIGVDTP 233
|
....*....
gi 1325668076 238 DDLKAAVEF 246
Cdd:COG1212 234 EDLERVRAL 242
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-248 |
1.23e-124 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 353.65 E-value: 1.23e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAH-AFFSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCR 79
Cdd:PRK05450 1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASkAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 80 EALDRIEAstgKRFDAVVNIQGDEPFVAEEQLRLITGCFDDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYFSR 159
Cdd:PRK05450 81 EAAAKLGL---ADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 160 SAIPYLRGTERDRwqRSHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAET-HSESLAIDTPD 238
Cdd:PRK05450 158 APIPYGRDAFADS--APTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVeEAPSIGVDTPE 235
|
250
....*....|
gi 1325668076 239 DLKAAVEFLR 248
Cdd:PRK05450 236 DLERVRALLA 245
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
2-246 |
2.59e-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: 347.54 E-value: 2.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 2 KFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAF--FSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCR 79
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkgLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 80 EALDRIEAStgkrFDAVVNIQGDEPFVAEEQLRLITGCF-DDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYFS 158
Cdd:cd02517 81 EVAEKLDAD----DDIVVNVQGDEPLIPPEMIDQVVAALkDDPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 159 RSAIPYLRGTERDrwqrsHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSESLAIDTPD 238
Cdd:cd02517 157 RSPIPYPRDSSED-----FPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHESIGVDTPE 231
|
....*...
gi 1325668076 239 DLKAAVEF 246
Cdd:cd02517 232 DLERVEAL 239
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
6-241 |
2.28e-72 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 220.94 E-value: 2.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 6 LIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAFFSD-CYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCREALDR 84
Cdd:TIGR00466 3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADrCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 85 IEASTGKRfdaVVNIQGDEPFVAEEQLRLITgcfDDPATE----IATLVKAFDAhEDIFNPNSPKVVLSTDGYALYFSRS 160
Cdd:TIGR00466 83 LALKDDER---IVNLQGDEPFIPKEIIRQVA---DNLATKnvpmAALAVKIHDA-EEAFNPNAVKVVLDSQGYALYFSRS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 161 AIPYLRGTERDRWQ-RSHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSE-SLAIDTPD 238
Cdd:TIGR00466 156 LIPFDRDFFAKRQTpVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVpSVGVDTQE 235
|
...
gi 1325668076 239 DLK 241
Cdd:TIGR00466 236 DLE 238
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-222 |
2.09e-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: 184.85 E-value: 2.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 4 LALIPARYASTRFPGKPLADLAGKPMIRHVYEKA--HAFFSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCREA 81
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAAlkSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 82 LDRIEASTGkrfDAVVNIQGDEPFVAEEQL-RLITGCFDDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYFSRS 160
Cdd:pfam02348 81 VKAFLNDHD---DIIVNIQGDNPLLQPEVIlKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1325668076 161 AIPYLRgteRDRWQRSHKFLKHIGLYAY-KSSVLRRIAELPQGTLEKLESLEQLRWLENGFRI 222
Cdd:pfam02348 158 VIPYIR---EHPAELYYVYLRHIGIYTFrKNMPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
1-246 |
4.17e-132 |
|
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: 372.47 E-value: 4.17e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAF--FSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRC 78
Cdd:COG1212 1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASkgADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 79 REALDRIEAstgKRFDAVVNIQGDEPFVAEEQLRLITGCF-DDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYF 157
Cdd:COG1212 81 AEAAEKLGL---PDDDIVVNVQGDEPLIPPELIDAVAEPLaEDPEADMATLATPITDEEELFNPNVVKVVTDKNGRALYF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 158 SRSAIPYLRgterDRWQRSHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSESLAIDTP 237
Cdd:COG1212 158 SRAPIPYPR----DAFAEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAPPIGVDTP 233
|
....*....
gi 1325668076 238 DDLKAAVEF 246
Cdd:COG1212 234 EDLERVRAL 242
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-248 |
1.23e-124 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 353.65 E-value: 1.23e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAH-AFFSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCR 79
Cdd:PRK05450 1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASkAGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 80 EALDRIEAstgKRFDAVVNIQGDEPFVAEEQLRLITGCFDDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYFSR 159
Cdd:PRK05450 81 EAAAKLGL---ADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIHDAEEAFNPNVVKVVLDADGRALYFSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 160 SAIPYLRGTERDRwqRSHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAET-HSESLAIDTPD 238
Cdd:PRK05450 158 APIPYGRDAFADS--APTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVeEAPSIGVDTPE 235
|
250
....*....|
gi 1325668076 239 DLKAAVEFLR 248
Cdd:PRK05450 236 DLERVRALLA 245
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
2-246 |
2.59e-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: 347.54 E-value: 2.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 2 KFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAF--FSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCR 79
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAkgLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 80 EALDRIEAStgkrFDAVVNIQGDEPFVAEEQLRLITGCF-DDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYFS 158
Cdd:cd02517 81 EVAEKLDAD----DDIVVNVQGDEPLIPPEMIDQVVAALkDDPGVDMATLATPISDEEELFNPNVVKVVLDKDGYALYFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 159 RSAIPYLRGTERDrwqrsHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSESLAIDTPD 238
Cdd:cd02517 157 RSPIPYPRDSSED-----FPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHESIGVDTPE 231
|
....*...
gi 1325668076 239 DLKAAVEF 246
Cdd:cd02517 232 DLERVEAL 239
|
|
| PRK13368 |
PRK13368 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-247 |
2.50e-103 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 184007 Cd Length: 238 Bit Score: 299.57 E-value: 2.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAH--AFFSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRC 78
Cdd:PRK13368 1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAqaAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 79 REALDRIEAstgkrfDAVVNIQGDEPFVAEEQLRLITGCF-DDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYF 157
Cdd:PRK13368 81 AEVMLKIEA------DIYINVQGDEPMIRPRDIDTLIQPMlDDPSINVATLCAPISTEEEFESPNVVKVVVDKNGDALYF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 158 SRSAIPYLRGTERDRWqrshkfLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSESLAIDTP 237
Cdd:PRK13368 155 SRSPIPSRRDGESARY------LKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRMVEVAATSIGVDTP 228
|
250
....*....|
gi 1325668076 238 DDLKAAVEFL 247
Cdd:PRK13368 229 EDLERVRAIM 238
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
6-241 |
2.28e-72 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 220.94 E-value: 2.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 6 LIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAFFSD-CYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCREALDR 84
Cdd:TIGR00466 3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANESGADrCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 85 IEASTGKRfdaVVNIQGDEPFVAEEQLRLITgcfDDPATE----IATLVKAFDAhEDIFNPNSPKVVLSTDGYALYFSRS 160
Cdd:TIGR00466 83 LALKDDER---IVNLQGDEPFIPKEIIRQVA---DNLATKnvpmAALAVKIHDA-EEAFNPNAVKVVLDSQGYALYFSRS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 161 AIPYLRGTERDRWQ-RSHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSE-SLAIDTPD 238
Cdd:TIGR00466 156 LIPFDRDFFAKRQTpVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVKIAQEVpSVGVDTQE 235
|
...
gi 1325668076 239 DLK 241
Cdd:TIGR00466 236 DLE 238
|
|
| PLN02917 |
PLN02917 |
CMP-KDO synthetase |
6-249 |
2.48e-59 |
|
CMP-KDO synthetase
Pssm-ID: 215495 Cd Length: 293 Bit Score: 189.66 E-value: 2.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 6 LIPARYASTRFPGKPLADLAGKPMIRHVYEKAH--AFFSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCREALD 83
Cdd:PLN02917 51 IIPARFASSRFEGKPLVHILGKPMIQRTWERAKlaTTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCNEALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 84 RIEastgKRFDAVVNIQGDEPFVAEEQL-RLITGCFDDPATEIATLVKAFDAhEDIFNPNSPKVVLSTDGYALYFSRSAI 162
Cdd:PLN02917 131 KLE----KKYDIVVNIQGDEPLIEPEIIdGVVKALQAAPDAVFSTAVTSLKP-EDASDPNRVKCVVDNQGYAIYFSRGLI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 163 PYlrgTERDRWQRSHKFLKHIGLYAYKSSVLRRIAELPQGTLEKLESLEQLRWLENGFRIKAAETHSESLAIDTPDDLkA 242
Cdd:PLN02917 206 PY---NKSGKVNPQFPYLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKVIKVDHEAHGVDTPEDV-E 281
|
....*..
gi 1325668076 243 AVEFLRR 249
Cdd:PLN02917 282 KIEALMR 288
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-222 |
2.09e-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: 184.85 E-value: 2.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 4 LALIPARYASTRFPGKPLADLAGKPMIRHVYEKA--HAFFSDCYVASDDERIVRTVEGFGGQAVMTSAEHRSGTDRCREA 81
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAAlkSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 82 LDRIEASTGkrfDAVVNIQGDEPFVAEEQL-RLITGCFDDPATEIATLVKAFDAHEDIFNPNSPKVVLSTDGYALYFSRS 160
Cdd:pfam02348 81 VKAFLNDHD---DIIVNIQGDNPLLQPEVIlKAIETLLNNGEPYMSTLVVPVGSAEEVLNANALKVVLDDDGYALYFSRS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1325668076 161 AIPYLRgteRDRWQRSHKFLKHIGLYAY-KSSVLRRIAELPQGTLEKLESLEQLRWLENGFRI 222
Cdd:pfam02348 158 VIPYIR---EHPAELYYVYLRHIGIYTFrKNMPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| NeuA |
COG1083 |
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ... |
1-112 |
9.80e-17 |
|
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440700 Cd Length: 228 Bit Score: 76.35 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPGKPLADLAGKPMIRHVYE--KAHAFFSDCYVASDDERIVRTVEGFGGQAVMTSAE----HRSG 74
Cdd:COG1083 1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEaaLKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAElagdTAST 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1325668076 75 TDRCREALDRIEaSTGKRFDAVVNIQGDEPFVAEEQLR 112
Cdd:COG1083 81 IDVILHALEWLE-EQGEEFDYVVLLQPTSPLRTAEDID 117
|
|
| CMP-NeuAc_Synthase |
cd02513 |
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ... |
2-112 |
2.75e-15 |
|
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: 72.57 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 2 KFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHA--FFSDCYVASDDERIVRTVEGFGGQAV-MTSAEHRSGT--- 75
Cdd:cd02513 1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALEskLFDRVVVSTDDEEIAEVARKYGAEVPfLRPAELATDTass 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1325668076 76 -DRCREALDRIEAStGKRFDAVVNIQGDEPFVAEEQLR 112
Cdd:cd02513 81 iDVILHALDQLEEL-GRDFDIVVLLQPTSPLRSAEDID 117
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
1-249 |
1.10e-12 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 65.61 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAF--FSDCYVA----SDDERIVRTVEGFGGQAvmtsaeHR-S 73
Cdd:COG1861 2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSklIDEVVVAtttdPADDPLVDLAKELGVPV------FRgS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 74 GTDrcreALDR-IEASTGKRFDAVVNIQGDEPFVaeeqlrlitgcfdDPATeIATLVKAFDAHEdifnpnspkvvlstdg 152
Cdd:COG1861 76 EDD----VLSRyYQAAEAYGADVVVRITGDCPLI-------------DPAL-IDELIAAFLESG---------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 153 yALYFSRSAIP-YLRG--TE---RDRWQRSHKFLK------HIGLYAYKSSVLRRIAELPQGtleklESLEQLRWlengf 220
Cdd:COG1861 122 -ADYVSNSLPRtYPRGldVEvfsFAALERAWEEAKlpsereHVTPYIYEHPDRFRIGNVEPP-----EDLSDLRL----- 190
|
250 260
....*....|....*....|....*....
gi 1325668076 221 rikaaeThseslaIDTPDDLkaavEFLRR 249
Cdd:COG1861 191 ------T------VDTPEDL----ELIRA 203
|
|
| PseF |
TIGR03584 |
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ... |
4-113 |
7.55e-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: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 4 LALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHA--FFSDCYVASDDERIVRTVEGFGGQAV----MTSAEHRSGT-D 76
Cdd:TIGR03584 1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNsgLFDKVVVSTDDEEIAEVAKSYGASVPflrpKELADDFTGTaP 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1325668076 77 RCREALDRIEasTGKRFDAVVNIQGDEPFVAEEQLRL 113
Cdd:TIGR03584 81 VVKHAIEELK--LQKQYDHACCIYATAPFLQAKILKE 115
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
12-136 |
5.90e-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: 47.96 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 12 ASTRFPG-KPLADLAGKPMIRHVYEKAHAFFSDCYVASDDERIVRTVEGFGGQAVMTSAEH-------RSGTDRCREAld 83
Cdd:pfam12804 8 RSSRMGGdKALLPLGGKPLLERVLERLRPAGDEVVVVANDEEVLAALAGLGVPVVPDPDPGqgplaglLAALRAAPGA-- 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1325668076 84 rieastgkrfDAVVNIQGDEPFVAEEQLRLITGCFDDPATEIATLVKAFDAHE 136
Cdd:pfam12804 86 ----------DAVLVLACDMPFLTPELLRRLLAAAEESGADIVVPVYDGGRGH 128
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
4-249 |
4.72e-06 |
|
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: 46.41 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 4 LALIPARYASTRFPGKPLADLAGKPMIRHVYEKAHAffsdcyVASDDERIVRTVEGFGGQAVMTSAE------HR-SGTD 76
Cdd:cd02518 1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKR------SKLIDEIVIATSTNEEDDPLEALAKklgvkvFRgSEED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 77 rcreALDR-IEASTGKRFDAVVNIQGDEPFVaeeqlrlitgcfdDPATEIATLVKAFDAHED-IFNPNSPKVVLSTDGYA 154
Cdd:cd02518 75 ----VLGRyYQAAEEYNADVVVRITGDCPLI-------------DPEIIDAVIRLFLKSGADyTSNTLPRTYPDGLDVEV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 155 lyFSRSAIPYLRGTERDRWQRshkflKHIGLYAYKSSVLRRIAELPQGtlekLESLEQLRWlengfrikaaethseslAI 234
Cdd:cd02518 138 --FTRDALERAAAEADDPYER-----EHVTPYIRRHPELFRIGYLEAP----PDRLSDLRL-----------------TV 189
|
250
....*....|....*
gi 1325668076 235 DTPDDLKAAVEFLRR 249
Cdd:cd02518 190 DTPEDFELIKEIYEA 204
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-112 |
8.59e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 43.17 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 5 ALIPARYASTRF----PgKPLADLAGKPMIRHVYEKAHAFFSDCyvasdderiVRTVEGFGGQAVMTSAEHRSGTDRCRE 80
Cdd:PRK14356 8 ALILAAGKGTRMhsdkP-KVLQTLLGEPMLRFVYRALRPLFGDN---------VWTVVGHRADMVRAAFPDEDARFVLQE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1325668076 81 -----------ALDRIEAStgkRFDAVVNIQGDEPFVAEEQLR 112
Cdd:PRK14356 78 qqlgtghalqcAWPSLTAA---GLDRVLVVNGDTPLVTTDTID 117
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
5-126 |
2.33e-04 |
|
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: 41.01 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 5 ALIPARYASTRFPG-KPLADLAGKPMIRHVYEKA-HAFFSDCYVAS--DDERIVRTVEGFGGQAVM--TSAEHRSGTDRC 78
Cdd:cd04182 3 AIILAAGRSSRMGGnKLLLPLDGKPLLRHALDAAlAAGLSRVIVVLgaEADAVRAALAGLPVVVVInpDWEEGMSSSLAA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1325668076 79 reALDRIEAstgkRFDAVVNIQGDEPFVAEEQLRLITGCFDDPATEIA 126
Cdd:cd04182 83 --GLEALPA----DADAVLILLADQPLVTAETLRALIDAFREDGAGIV 124
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
13-52 |
3.60e-04 |
|
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: 40.18 E-value: 3.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1325668076 13 STRFPG-KPLADLAGKPMIRHVYEKAHAFFSDCYV-ASDDER 52
Cdd:COG0746 15 SRRMGQdKALLPLGGRPLLERVLERLRPQVDEVVIvANRPER 56
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-126 |
5.31e-04 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 39.76 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 1 MKFLALIPARYASTRFPG-KPLADLAGKPMIRHVYEKA-HAFFSDCYVA--SDDERIVRTVEGFGGQAVmTSAEHRSGtd 76
Cdd:COG2068 2 SKVAAIILAAGASSRMGRpKLLLPLGGKPLLERAVEAAlAAGLDPVVVVlgADAEEVAAALAGLGVRVV-VNPDWEEG-- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1325668076 77 rC----REALDRIEASTgkrfDAVVNIQGDEPFVAEEQLRLITGCFDDPATEIA 126
Cdd:COG2068 79 -MssslRAGLAALPADA----DAVLVLLGDQPLVTAETLRRLLAAFRESPASIV 127
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
13-72 |
2.59e-03 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 37.86 E-value: 2.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1325668076 13 STRFPG--KPLADLAGKPMIRHVYEKAHAFFSD----------CYVASDDERIVRTVEGFGG-----QAVMTSAEHR 72
Cdd:PRK00317 14 SRRMGGvdKGLQELNGKPLIQHVIERLAPQVDEivinanrnlaRYAAFGLPVIPDSLADFPGplagiLAGLKQARTE 90
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
19-121 |
7.03e-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: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325668076 19 KPLADLAGKPMIRHVYEKAHAFfsdcyvasDDERIVrTVEGFGGQAVMTSAEHRS----------GT-DRCREALDRIEA 87
Cdd:COG1207 22 KVLHPLAGKPMLEHVLDAARAL--------GPDRIV-VVVGHGAEQVRAALADLDvefvlqeeqlGTgHAVQQALPALPG 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1325668076 88 STGKrfdaVVNIQGDEPFVAEEQLR--------------LITGCFDDP 121
Cdd:COG1207 93 DDGT----VLVLYGDVPLIRAETLKallaahraagaaatVLTAELDDP 136
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
13-51 |
8.65e-03 |
|
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.
Pssm-ID: 133000 [Multi-domain] Cd Length: 181 Bit Score: 36.01 E-value: 8.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1325668076 13 STRFPG-KPLADLAGKPMIRHVYEKAHAFFSDCYVASDDE 51
Cdd:cd02503 11 SRRMGGdKALLELGGKPLLEHVLERLKPLVDEVVISANRD 50
|
|
| |
