|
Name |
Accession |
Description |
Interval |
E-value |
| KdsB |
COG1212 |
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ... |
1-238 |
1.91e-155 |
|
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: 431.02 E-value: 1.91e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRL 80
Cdd:COG1212 1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 81 AEVA--LNYPDVDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATLKVAM-NEEDYNNPAAVKVVTDLNGYALYFSRS 157
Cdd:COG1212 81 AEAAekLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPItDEEELFNPNVVKVVTDKNGRALYFSRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 158 LMPYPRNK-PEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESDFQGIGVDTPEDLAAVN 236
Cdd:COG1212 161 PIPYPRDAfAEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAPPIGVDTPEDLERVR 240
|
..
gi 496436145 237 EL 238
Cdd:COG1212 241 AL 242
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
2-238 |
1.31e-148 |
|
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: 413.79 E-value: 1.31e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 2 KVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRLA 81
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 82 EVALNYP-DVDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATLKVAM-NEEDYNNPAAVKVVTDLNGYALYFSRSLM 159
Cdd:cd02517 81 EVAEKLDaDDDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPIsDEEELFNPNVVKVVLDKDGYALYFSRSPI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496436145 160 PYPRNKPEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESDFQGIGVDTPEDLAAVNEL 238
Cdd:cd02517 161 PYPRDSSEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHESIGVDTPEDLERVEAL 239
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-240 |
1.19e-141 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 396.41 E-value: 1.19e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLpDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRL 80
Cdd:PRK05450 1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGA-DRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 81 AEVA--LNYPDVDVIVNVQGDEPMIPPEVIDRLAECFTgDSELQMATLKVA-MNEEDYNNPAAVKVVTDLNGYALYFSRS 157
Cdd:PRK05450 80 AEAAakLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLA-NPEADMATLAVPiHDAEEAFNPNVVKVVLDADGRALYFSRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 158 LMPYPRN---KPEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESD-FQGIGVDTPEDLA 233
Cdd:PRK05450 159 PIPYGRDafaDSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEeAPSIGVDTPEDLE 238
|
....*..
gi 496436145 234 AVNELFA 240
Cdd:PRK05450 239 RVRALLA 245
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
6-232 |
3.05e-84 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 250.99 E-value: 3.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 6 VIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAkLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRLAEVA- 84
Cdd:TIGR00466 3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANES-GADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 85 -LNYPDVDVIVNVQGDEPMIPPEVIDRLAECFtGDSELQMATLKVAM-NEEDYNNPAAVKVVTDLNGYALYFSRSLMPYP 162
Cdd:TIGR00466 82 kLALKDDERIVNLQGDEPFIPKEIIRQVADNL-ATKNVPMAALAVKIhDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496436145 163 RNK------PEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKV-LESDFQGIGVDTPEDL 232
Cdd:TIGR00466 161 RDFfakrqtPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVkIAQEVPSVGVDTQEDL 237
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-214 |
7.83e-69 |
|
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: 211.04 E-value: 7.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 4 LCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRLAEV 83
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 84 ALNYP--DVDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATL-KVAMNEEDYNNPAAVKVVTDLNGYALYFSRSLMP 160
Cdd:pfam02348 81 VKAFLndHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLvVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496436145 161 YPRNKPEGYKV--YKHVGIYAYR-RSFLLKYAALQPTPLERAESLEQLRALENGYKI 214
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]; ... |
1-238 |
1.91e-155 |
|
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: 431.02 E-value: 1.91e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRL 80
Cdd:COG1212 1 MKFIVVIPARYASTRLPGKPLADIAGKPMIQRVYERALASKGADRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 81 AEVA--LNYPDVDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATLKVAM-NEEDYNNPAAVKVVTDLNGYALYFSRS 157
Cdd:COG1212 81 AEAAekLGLPDDDIVVNVQGDEPLIPPELIDAVAEPLAEDPEADMATLATPItDEEELFNPNVVKVVTDKNGRALYFSRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 158 LMPYPRNK-PEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESDFQGIGVDTPEDLAAVN 236
Cdd:COG1212 161 PIPYPRDAfAEDGPYYRHIGIYAYRRDFLRRFVSLPPSPLEQAESLEQLRALENGYRIKVVETDAPPIGVDTPEDLERVR 240
|
..
gi 496436145 237 EL 238
Cdd:COG1212 241 AL 242
|
|
| CMP-KDO-Synthetase |
cd02517 |
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ... |
2-238 |
1.31e-148 |
|
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: 413.79 E-value: 1.31e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 2 KVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRLA 81
Cdd:cd02517 1 KVIVVIPARYASSRLPGKPLADIAGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVMTSPDHPSGTDRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 82 EVALNYP-DVDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATLKVAM-NEEDYNNPAAVKVVTDLNGYALYFSRSLM 159
Cdd:cd02517 81 EVAEKLDaDDDIVVNVQGDEPLIPPEMIDQVVAALKDDPGVDMATLATPIsDEEELFNPNVVKVVLDKDGYALYFSRSPI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496436145 160 PYPRNKPEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESDFQGIGVDTPEDLAAVNEL 238
Cdd:cd02517 161 PYPRDSSEDFPYYKHIGIYAYRRDFLLRFAALPPSPLEQIESLEQLRALENGYKIKVVETDHESIGVDTPEDLERVEAL 239
|
|
| PRK05450 |
PRK05450 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-240 |
1.19e-141 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 235473 Cd Length: 245 Bit Score: 396.41 E-value: 1.19e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLpDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRL 80
Cdd:PRK05450 1 MKFLIIIPARYASTRLPGKPLADIGGKPMIVRVYERASKAGA-DRVVVATDDERIADAVEAFGGEVVMTSPDHPSGTDRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 81 AEVA--LNYPDVDVIVNVQGDEPMIPPEVIDRLAECFTgDSELQMATLKVA-MNEEDYNNPAAVKVVTDLNGYALYFSRS 157
Cdd:PRK05450 80 AEAAakLGLADDDIVVNVQGDEPLIPPEIIDQVAEPLA-NPEADMATLAVPiHDAEEAFNPNVVKVVLDADGRALYFSRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 158 LMPYPRN---KPEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESD-FQGIGVDTPEDLA 233
Cdd:PRK05450 159 PIPYGRDafaDSAPTPVYRHIGIYAYRRGFLRRFVSLPPSPLEKIESLEQLRALENGYRIHVVVVEeAPSIGVDTPEDLE 238
|
....*..
gi 496436145 234 AVNELFA 240
Cdd:PRK05450 239 RVRALLA 245
|
|
| PRK13368 |
PRK13368 |
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional |
1-235 |
1.34e-114 |
|
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
Pssm-ID: 184007 Cd Length: 238 Bit Score: 327.69 E-value: 1.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRL 80
Cdd:PRK13368 1 MKVVVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKVVMTSDDHLSGTDRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 81 AEVALnYPDVDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATLKVAM-NEEDYNNPAAVKVVTDLNGYALYFSRSLM 159
Cdd:PRK13368 81 AEVML-KIEADIYINVQGDEPMIRPRDIDTLIQPMLDDPSINVATLCAPIsTEEEFESPNVVKVVVDKNGDALYFSRSPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496436145 160 PYPRNKPegYKVY-KHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESDFQGIGVDTPEDLAAV 235
Cdd:PRK13368 160 PSRRDGE--SARYlKHVGIYAFRRDVLQQFSQLPETPLEQIESLEQLRALEHGEKIRMVEVAATSIGVDTPEDLERV 234
|
|
| kdsB |
TIGR00466 |
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and ... |
6-232 |
3.05e-84 |
|
3-deoxy-D-manno-octulosonate cytidylyltransferase; [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 129558 Cd Length: 238 Bit Score: 250.99 E-value: 3.05e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 6 VIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAkLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRLAEVA- 84
Cdd:TIGR00466 3 IIPARLASSRLPGKPLEDIFGKPMIVHVAENANES-GADRCIVATDDESVAQTCQKFGIEVCMTSKHHNSGTERLAEVVe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 85 -LNYPDVDVIVNVQGDEPMIPPEVIDRLAECFtGDSELQMATLKVAM-NEEDYNNPAAVKVVTDLNGYALYFSRSLMPYP 162
Cdd:TIGR00466 82 kLALKDDERIVNLQGDEPFIPKEIIRQVADNL-ATKNVPMAALAVKIhDAEEAFNPNAVKVVLDSQGYALYFSRSLIPFD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496436145 163 RNK------PEGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKV-LESDFQGIGVDTPEDL 232
Cdd:TIGR00466 161 RDFfakrqtPVGDNLLRHIGIYGYRAGFIEEYVAWKPCVLEEIEKLEQLRVLYYGEKIHVkIAQEVPSVGVDTQEDL 237
|
|
| PLN02917 |
PLN02917 |
CMP-KDO synthetase |
2-243 |
1.29e-71 |
|
CMP-KDO synthetase
Pssm-ID: 215495 Cd Length: 293 Bit Score: 220.86 E-value: 1.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 2 KVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRLA 81
Cdd:PLN02917 47 RVVGIIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADVIMTSESCRNGTERCN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 82 EvALNYPD--VDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATLKVAMNEEDYNNPAAVKVVTDLNGYALYFSRSLM 159
Cdd:PLN02917 127 E-ALKKLEkkYDIVVNIQGDEPLIEPEIIDGVVKALQAAPDAVFSTAVTSLKPEDASDPNRVKCVVDNQGYAIYFSRGLI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 160 PYprNKP----EGYKVYKHVGIYAYRRSFLLKYAALQPTPLERAESLEQLRALENGYKIKVLESDFQGIGVDTPEDLAAV 235
Cdd:PLN02917 206 PY--NKSgkvnPQFPYLLHLGIQSYDAKFLKIYPELPPTPLQLEEDLEQLKVLENGYKMKVIKVDHEAHGVDTPEDVEKI 283
|
....*...
gi 496436145 236 NELFAKMN 243
Cdd:PLN02917 284 EALMRERN 291
|
|
| CTP_transf_3 |
pfam02348 |
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ... |
4-214 |
7.83e-69 |
|
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: 211.04 E-value: 7.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 4 LCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMMTSPDHPSGTDRLAEV 83
Cdd:pfam02348 1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 84 ALNYP--DVDVIVNVQGDEPMIPPEVIDRLAECFTGDSELQMATL-KVAMNEEDYNNPAAVKVVTDLNGYALYFSRSLMP 160
Cdd:pfam02348 81 VKAFLndHDDIIVNIQGDNPLLQPEVILKAIETLLNNGEPYMSTLvVPVGSAEEVLNANALKVVLDDDGYALYFSRSVIP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 496436145 161 YPRNKPEGYKV--YKHVGIYAYR-RSFLLKYAALQPTPLERAESLEQLRALENGYKI 214
Cdd:pfam02348 161 YIREHPAELYYvyLRHIGIYTFRkNMPLIELVIDTPTALEYIEKLEQLRVLYNGEKI 217
|
|
| SpsF |
COG1861 |
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall ... |
1-244 |
2.88e-27 |
|
Spore coat polysaccharide biosynthesis protein SpsF, cytidylyltransferase family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441466 Cd Length: 245 Bit Score: 104.90 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVAT-----DNELVKKA----VDGFGGkammtSP 71
Cdd:COG1861 2 MKIVAIIQARMGSTRLPGKVLKPLGGKPVLEHVIERLKRSKLIDEVVVATttdpaDDPLVDLAkelgVPVFRG-----SE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 72 DhpsgtD---RLAEVALNYpDVDVIVNVQGDEPMIPPEVIDRLAECFtgdselqmatlkvamNEEDYNnpaavkvvtdln 148
Cdd:COG1861 77 D-----DvlsRYYQAAEAY-GADVVVRITGDCPLIDPALIDELIAAF---------------LESGAD------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 149 gyalYFSRSLmpyPRNKPEG-----------YKVYK---------HVGIYAYRRSFLLKYAALQPtplerAESLEQLRal 208
Cdd:COG1861 124 ----YVSNSL---PRTYPRGldvevfsfaalERAWEeaklpsereHVTPYIYEHPDRFRIGNVEP-----PEDLSDLR-- 189
|
250 260 270
....*....|....*....|....*....|....*.
gi 496436145 209 engykikvlesdfqgIGVDTPEDLAAVNELFAKMNK 244
Cdd:COG1861 190 ---------------LTVDTPEDLELIRAIYEALYP 210
|
|
| GT2_SpsF |
cd02518 |
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ... |
4-244 |
4.72e-22 |
|
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: 90.71 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 4 LCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVAT-----DNELVKKA----VDGFGGkammtspdhp 74
Cdd:cd02518 1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstneeDDPLEALAkklgVKVFRG---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 75 SGTD---RLAEVALNYPdVDVIVNVQGDEPMIPPEVIDR-LAECFTGDSELqmatlkvAMNEEDYNNPA--AVKVVTdLN 148
Cdd:cd02518 71 SEEDvlgRYYQAAEEYN-ADVVVRITGDCPLIDPEIIDAvIRLFLKSGADY-------TSNTLPRTYPDglDVEVFT-RD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 149 GYALYFSRSLMPYPRnkpegykvyKHVGIYAYRRSFLLKYAALQPTPleraESLEQLRalengykikvlesdfqgIGVDT 228
Cdd:cd02518 142 ALERAAAEADDPYER---------EHVTPYIRRHPELFRIGYLEAPP----DRLSDLR-----------------LTVDT 191
|
250
....*....|....*.
gi 496436145 229 PEDLAAVNELFAKMNK 244
Cdd:cd02518 192 PEDFELIKEIYEALYP 207
|
|
| NeuA |
COG1083 |
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ... |
1-115 |
6.25e-16 |
|
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: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGGKAMM--------TSPD 72
Cdd:COG1083 1 MKILAIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLrpaelagdTAST 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496436145 73 HPSGTDRLAEVALNYPDVDVIVNVQGDEPMIPPEVIDRLAECF 115
Cdd:COG1083 81 IDVILHALEWLEEQGEEFDYVVLLQPTSPLRTAEDIDEAIELL 123
|
|
| CMP-NeuAc_Synthase |
cd02513 |
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ... |
2-239 |
1.50e-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: 72.96 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 2 KVLCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNELVKKAVDGFGG-------KAMMTspDHP 74
Cdd:cd02513 1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAevpflrpAELAT--DTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 75 SGTDRLAEVALNYP----DVDVIVNVQGDEPMIPPEVIDRLAECFTgDSELQMAtlkVAMNEedYNNPAAVKVVTDLNGY 150
Cdd:cd02513 79 SSIDVILHALDQLEelgrDFDIVVLLQPTSPLRSAEDIDEAIELLL-SEGADSV---FSVTE--FHRFPWRALGLDDNGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 151 ALYFSRSLMPYPRNKPEgyKVYKHVG-IYAYRRSFLLKYAALQ---PTPLEraesLEQLRALEngykikvlesdfqgigV 226
Cdd:cd02513 153 EPVNYPEDKRTRRQDLP--PAYHENGaIYIAKREALLESNSFFggkTGPYE----MPRERSID----------------I 210
|
250
....*....|...
gi 496436145 227 DTPEDLAAVNELF 239
Cdd:cd02513 211 DTEEDFELAEALL 223
|
|
| PseF |
TIGR03584 |
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ... |
4-53 |
1.62e-09 |
|
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: 56.19 E-value: 1.62e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 496436145 4 LCVIPARYASTRLPGKPLSLIAGKPMIQHVYERACQAKLPDEVVVATDNE 53
Cdd:TIGR03584 1 IAIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDE 50
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
1-115 |
1.09e-08 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 53.24 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPG-KPLSLIAGKPMIQHVYERACQAKLpDEVVVAT--DNELVKKAVDGFGGKAmMTSPDHPSGt 77
Cdd:COG2068 2 SKVAAIILAAGASSRMGRpKLLLPLGGKPLLERAVEAALAAGL-DPVVVVLgaDAEEVAAALAGLGVRV-VVNPDWEEG- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 496436145 78 drLAE---VALNY--PDVDVIVNVQGDEPMIPPEVIDRLAECF 115
Cdd:COG2068 79 --MSSslrAGLAAlpADADAVLVLLGDQPLVTAETLRRLLAAF 119
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
12-118 |
1.29e-08 |
|
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: 52.58 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 12 ASTRLPG-KPLSLIAGKPMIQHVYERACQAklPDEVVVATDNELVKKAVDGFGGKAMMTSPDH--PSGTdrLAEVALNYP 88
Cdd:pfam12804 8 RSSRMGGdKALLPLGGKPLLERVLERLRPA--GDEVVVVANDEEVLAALAGLGVPVVPDPDPGqgPLAG--LLAALRAAP 83
|
90 100 110
....*....|....*....|....*....|
gi 496436145 89 DVDVIVNVQGDEPMIPPEVIDRLAECFTGD 118
Cdd:pfam12804 84 GADAVLVLACDMPFLTPELLRRLLAAAEES 113
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
19-240 |
2.35e-08 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 52.94 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 19 KPLSLIAGKPMIQHVYERACQAKLpDEVVVAT--DNELVKKAVDGFGGKAMMTSPDHPSGTDRLAEV--ALNYPDVDVIV 94
Cdd:COG1213 22 KCLVEIGGKTLLERQLEALAAAGI-KDIVVVTgyKAELIEEALARPGPDVTFVYNPDYDETNNIYSLwlAREALDEDFLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 95 nVQGDepMI-PPEVIDRLAECFTGDSelqmatlkVAMNEEDYNNPA-AVKVVTDLNGYALYFSRSLMPYPRNkpegykvY 172
Cdd:COG1213 101 -LNGD--VVfDPAILKRLLASDGDIV--------LLVDRKWEKPLDeEVKVRVDEDGRIVEIGKKLPPEEAD-------G 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496436145 173 KHVGIYAYRRSFLLKYAALQPTPLERA---ESLEQL--RALENGYKIKVLE-SDFQGIGVDTPEDLAAVNELFA 240
Cdd:COG1213 163 EYIGIFKFSAEGAAALREALEALIDEGgpnLYYEDAlqELIDEGGPVKAVDiGGLPWVEIDTPEDLERAEELFA 236
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-113 |
3.60e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 53.33 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTR----LPgKPLSLIAGKPMIQHVYeRACQAKLPDEVVVAT--DNELVKKAVDGFGGKAMMTSPDHP 74
Cdd:PRK14353 4 RTCLAIILAAGEGTRmkssLP-KVLHPVAGRPMLAHVL-AAAASLGPSRVAVVVgpGAEAVAAAAAKIAPDAEIFVQKER 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 496436145 75 SGTD---RLAEVALNYPDVDVIVnVQGDEPMIPPEVIDRLAE 113
Cdd:PRK14353 82 LGTAhavLAAREALAGGYGDVLV-LYGDTPLITAETLARLRE 122
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
14-114 |
1.30e-07 |
|
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: 50.59 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 14 TR----LPgKPLSLIAGKPMIQHVYERACQAKlPDEVVVAT--DNELVKKAVDGFG------------GKAMMTspdhps 75
Cdd:cd02540 10 TRmksdLP-KVLHPLAGKPMLEHVLDAARALG-PDRIVVVVghGAEQVKKALANPNvefvlqeeqlgtGHAVKQ------ 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 496436145 76 gtdrlAEVALNYPDVDVIVnVQGDEPMIPPEVIDRLAEC 114
Cdd:cd02540 82 -----ALPALKDFEGDVLV-LYGDVPLITPETLQRLLEA 114
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
3-120 |
1.82e-07 |
|
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: 49.87 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 3 VLCVIPARYASTRLPG-KPLSLIAGKPMIQHVYERACQAKLpDEVVVAT--DNELVKKAVDGFGGKAmMTSPDHPSG-TD 78
Cdd:cd04182 1 IAAIILAAGRSSRMGGnKLLLPLDGKPLLRHALDAALAAGL-SRVIVVLgaEADAVRAALAGLPVVV-VINPDWEEGmSS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 496436145 79 RLAeVALNY--PDVDVIVNVQGDEPMIPPEVIDRLAECFTGDSE 120
Cdd:cd04182 79 SLA-AGLEAlpADADAVLILLADQPLVTAETLRALIDAFREDGA 121
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
15-113 |
1.15e-06 |
|
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: 48.87 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 15 RLPgKPLSLIAGKPMIQHVYERACQAKlPDEVVVAT--DNELVKKAVDGFG------------GKAMMtspdhpsgtdrL 80
Cdd:COG1207 19 KLP-KVLHPLAGKPMLEHVLDAARALG-PDRIVVVVghGAEQVRAALADLDvefvlqeeqlgtGHAVQ-----------Q 85
|
90 100 110
....*....|....*....|....*....|...
gi 496436145 81 AEVALNYPDVDVIVnVQGDEPMIPPEVIDRLAE 113
Cdd:COG1207 86 ALPALPGDDGTVLV-LYGDVPLIRAETLKALLA 117
|
|
| mobA |
PRK00317 |
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed |
1-115 |
1.37e-06 |
|
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
Pssm-ID: 234725 [Multi-domain] Cd Length: 193 Bit Score: 47.49 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTRLPG--KPLSLIAGKPMIQHVYERAcqAKLPDEVVV----------ATDNELVKKAVDGFGGkamm 68
Cdd:PRK00317 2 PPITGVILAGGRSRRMGGvdKGLQELNGKPLIQHVIERL--APQVDEIVInanrnlaryaAFGLPVIPDSLADFPG---- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 496436145 69 tsPdhpsgtdrLAEV--ALNYPDVDVIVNVQGDEPMIPPEVIDRLAECF 115
Cdd:PRK00317 76 --P--------LAGIlaGLKQARTEWVLVVPCDTPFIPPDLVARLAQAA 114
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
13-118 |
5.31e-05 |
|
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: 42.56 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 13 STRLPG-KPLSLIAGKPMIQHVYERAcqAKLPDEVVVATDNELvkKAVDGFGGKAMmtsPDHPSGTDRLA--EVALNYPD 89
Cdd:cd02503 11 SRRMGGdKALLELGGKPLLEHVLERL--KPLVDEVVISANRDQ--ERYALLGVPVI---PDEPPGKGPLAgiLAALRAAP 83
|
90 100
....*....|....*....|....*....
gi 496436145 90 VDVIVNVQGDEPMIPPEVIDRLAECFTGD 118
Cdd:cd02503 84 ADWVLVLACDMPFLPPELLERLLAAAEEG 112
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
13-120 |
1.39e-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: 41.33 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 13 STRLPG-KPLSLIAGKPMIQHVYERAcqAKLPDEVVVATDNElvkKAVDGFGGKAMmtsPDHPSGTDRLA--EVALNYPD 89
Cdd:COG0746 15 SRRMGQdKALLPLGGRPLLERVLERL--RPQVDEVVIVANRP---ERYAALGVPVV---PDDPPGAGPLAgiLAALEAAP 86
|
90 100 110
....*....|....*....|....*....|.
gi 496436145 90 VDVIVNVQGDEPMIPPEVIDRLAECFTGDSE 120
Cdd:COG0746 87 AEWVLVLACDMPFLPPDLVRRLLEALEEGAD 117
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
6-113 |
3.43e-04 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 40.50 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 6 VIPAryA--STRLPG---KPLSLIAGKPMIQHVYERACQAKLPDEVVVAT---DNELVKKAVDGFGgkammTSPDH---P 74
Cdd:COG1211 1 IIPA--AgsGSRMGAgipKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVppdDIEYFEELLAKYG-----IDKPVrvvA 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 496436145 75 SGTDRLAEV--ALNY--PDVDVIVnVQ-GDEPMIPPEVIDRLAE 113
Cdd:COG1211 74 GGATRQDSVrnGLEAlpDDDDWVL-VHdAARPLVSPELIDRVIE 116
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
14-111 |
5.31e-04 |
|
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: 39.87 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 14 TRL--PGKPLSLIAGKPMIQHVYErACQAKLPDEVVVAT--DNELVKKAVDGFGGKAMMTSpdhpsGTDRLAEV--ALNY 87
Cdd:COG2266 7 TRLggGEKPLLEICGKPMIDRVID-ALEESCIDKIYVAVspNTPKTREYLKERGVEVIETP-----GEGYVEDLneALES 80
|
90 100
....*....|....*....|....
gi 496436145 88 PDVDVIVnVQGDEPMIPPEVIDRL 111
Cdd:COG2266 81 ISGPVLV-VPADLPLLTPEIIDDI 103
|
|
| glmU |
PRK14356 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
19-238 |
8.65e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237686 [Multi-domain] Cd Length: 456 Bit Score: 40.09 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 19 KPLSLIAGKPMIQHVYeRACQAKLPDEV--VVATDNELVKKAVD-------------GFGGKAMMTSPD-HPSGTDRLae 82
Cdd:PRK14356 25 KVLQTLLGEPMLRFVY-RALRPLFGDNVwtVVGHRADMVRAAFPdedarfvlqeqqlGTGHALQCAWPSlTAAGLDRV-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 83 valnypdvdVIVNvqGDEPMIPPEVIDRLAeCFTGDSELQMATLKVamneedyNNPAAVKVVTDLNG--YALYFSRSLMP 160
Cdd:PRK14356 102 ---------LVVN--GDTPLVTTDTIDDFL-KEAAGADLAFMTLTL-------PDPGAYGRVVRRNGhvAAIVEAKDYDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 161 yPRNKPEGYKVykHVGIYayrrsfLLKYAALQPTpLERAES-----------LEQLrALENGYKIKVLE--SDFQGIGVD 227
Cdd:PRK14356 163 -ALHGPETGEV--NAGIY------YLRLDAVESL-LPRLTNanksgeyyitdLVGL-AVAEGMNVLGVNcgEDPNLLGVN 231
|
250
....*....|.
gi 496436145 228 TPEDLAAVNEL 238
Cdd:PRK14356 232 TPAELVRSEEL 242
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-113 |
1.00e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 39.81 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496436145 1 MKVLCVIPARYASTR----LPgKPLSLIAGKPMIQHVYERACQAKLPDEVVVA-TDNELVKKAVDG----------FG-G 64
Cdd:PRK14354 1 MNRYAIILAAGKGTRmkskLP-KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVgHGAEEVKEVLGDrsefalqeeqLGtG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 496436145 65 KAMMTSPDHpsgtdrLAEValnypDVDVIVnVQGDEPMIPPEVIDRLAE 113
Cdd:PRK14354 80 HAVMQAEEF------LADK-----EGTTLV-ICGDTPLITAETLKNLID 116
|
|
| |
