|
Name |
Accession |
Description |
Interval |
E-value |
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
4-351 |
4.32e-179 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 499.98 E-value: 4.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 4 TNNHLVIMAGGVGSRFWPMSTTENPKQFIDVLGvGKTLLQLTVERFGNLVKPENIWVVTNQSYQEIVKKQLPDMPAGNIL 83
Cdd:COG0836 1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLG-EKSLLQQTVERLAGLVPPENILVVTNEEHRFLVAEQLPELGPANIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 84 CEPCRRNTAPCIAYVSWRIKSKDPKANIIVTPSDHIVTDKAEFQRVIKECMQFTsETDAIVTLGMKPNRPETGYGYIQAD 163
Cdd:COG0836 80 LEPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAA-EAGKLVTFGIKPTRPETGYGYIEAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 164 lstSSLRNKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGTDKEQEEI 243
Cdd:COG0836 159 ---EALGGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 244 NRLFPECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSLHEQSKKDLYGNVSIGpDVNLIESHNCIVHTmQEKKVVIQ 323
Cdd:COG0836 236 AEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLG-DVLLIDSSNSLVRS-EGRLVAVI 313
|
330 340
....*....|....*....|....*...
gi 502828281 324 GLDGYIVAENNDTLLICKLSEEQRIKQF 351
Cdd:COG0836 314 GVEDLVVVDTPDALLVAPKDRAQEVKKI 341
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
9-284 |
1.12e-131 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 376.92 E-value: 1.12e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMSTTENPKQFIDVLGvGKTLLQLTVERFGNLVKPENIWVVTNQSYQEIVKKQLPD-MPAGNILCEPC 87
Cdd:cd02509 4 VILAGGSGTRLWPLSRESYPKQFLKLFG-DKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREQLPEgLPEENIILEPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 88 RRNTAPCIAYVSWRIKSKDPKANIIVTPSDHIVTDKAEFQRVIKECMQFtSETDAIVTLGMKPNRPETGYGYIQADLSTS 167
Cdd:cd02509 83 GRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEA-AEEGYLVTFGIKPTRPETGYGYIEAGEKLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 168 slrnKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGTDKEQEEINRLF 247
Cdd:cd02509 162 ----GGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTDDFLRLLEEAF 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 502828281 248 PECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSL 284
Cdd:cd02509 238 AKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
|
|
| GMP_PMI |
TIGR01479 |
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ... |
9-349 |
2.83e-90 |
|
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 273648 [Multi-domain] Cd Length: 468 Bit Score: 278.44 E-value: 2.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMSTTENPKQFIDVLGVGkTLLQLTVERFGNLVKPENIwVVTNQSYQEIVKKQLP--DMPAGNILCEP 86
Cdd:TIGR01479 4 VILAGGSGTRLWPLSRELYPKQFLALVGDL-TMLQQTLKRLAGLPCSSPL-VICNEEHRFIVAEQLReiGKLASNIILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 87 CRRNTAPCIAYVS-WRIKSKDPKANIIVTPSDHIVTDKAEFQRVIKECMQFTSEtDAIVTLGMKPNRPETGYGYIQAdls 165
Cdd:TIGR01479 82 VGRNTAPAIALAAlLAARRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAE-GKLVTFGIVPTHPETGYGYIRR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 166 TSSLRNKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGTD-------K 238
Cdd:TIGR01479 158 GAPLAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDldfirldK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 239 EQeeinrlFPECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSLHEQSKKDLYGNVSIGpDVNLIESHNCIVHTmQEK 318
Cdd:TIGR01479 238 EA------FEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKG-DVLTHDTKNSYIYS-ESR 309
|
330 340 350
....*....|....*....|....*....|.
gi 502828281 319 KVVIQGLDGYIVAENNDTLLICKLSEEQRIK 349
Cdd:TIGR01479 310 LVAVVGVEDLVVVETKDAVLVAHKDRVQDVK 340
|
|
| cpsB |
PRK15460 |
mannose-1-phosphate guanyltransferase; Provisional |
1-350 |
7.93e-68 |
|
mannose-1-phosphate guanyltransferase; Provisional
Pssm-ID: 185357 [Multi-domain] Cd Length: 478 Bit Score: 220.61 E-value: 7.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 1 MARTNNHLVIMAGGVGSRFWPMSTTENPKQFIDVLGvGKTLLQLTVERFgNLVKPENIWVVTNQSYQEIVKKQLPDMP-- 78
Cdd:PRK15460 1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKG-DLTMLQTTICRL-NGVECESPVVICNEQHRFIVAEQLRQLNkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 79 AGNILCEPCRRNTAPCIAYVSWRIKSKDPKAN--IIVTPSDHIVTDKAEFQRVIKECMQFtSETDAIVTLGMKPNRPETG 156
Cdd:PRK15460 79 TENIILEPAGRNTAPAIALAALAAKRHSPESDplMLVLAADHVIADEDAFRAAVRNAMPY-AEAGKLVTFGIVPDLPETG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 157 YGYIQADLSTSSLRNKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGT 236
Cdd:PRK15460 158 YGYIRRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 237 DKEQEEINR-LFPECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSLHEQSKKDLYGNVSIGpDVNLIESHNCIVHTm 315
Cdd:PRK15460 238 DLDFIRVDEeAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHG-DVINHKTENSYVYA- 315
|
330 340 350
....*....|....*....|....*....|....*
gi 502828281 316 QEKKVVIQGLDGYIVAENNDTLLICKLSEEQRIKQ 350
Cdd:PRK15460 316 ESGLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKK 350
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
9-292 |
2.05e-41 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 145.09 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMSTTENPKQFIdvLGVGKTLLQLTVERFGNlVKPENIWVVTNQSYQEIVKKQLPDMP--AGNILC-- 84
Cdd:pfam00483 3 IILAGGSGTRLWPLTRTLAKPLVP--VGGKYPLIDYPLSRLAN-AGIREIIVILTQEHRFMLNELLGDGSkfGVQITYal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 85 EPCRRNTAPCIAYVSWRIKskDPKANIIVTPSDHIVtdKAEFQRVIKECMQftSETDAIVTLGMKPNRPETGYGYIQADl 164
Cdd:pfam00483 80 QPEGKGTAPAVALAADFLG--DEKSDVLVLGGDHIY--RMDLEQAVKFHIE--KAADATVTFGIVPVEPPTGYGVVEFD- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 165 stsslrnkEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFiwnvntiVNAFRIYQPSmakifesllpiygtDKEQEEIN 244
Cdd:pfam00483 153 --------DNGRVIRFVEKPKLPKASNYASMGIYIFNSGVL-------DFLAKYLEEL--------------KRGEDEIT 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 502828281 245 RLFPE-CENISVDYAIMEKaeeifvcpsDFGWSDLGTWGSLHEQSKKDL 292
Cdd:pfam00483 204 DILPKaLEDGKLAYAFIFK---------GYAWLDVGTWDSLWEANLFLL 243
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
4-351 |
4.32e-179 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 499.98 E-value: 4.32e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 4 TNNHLVIMAGGVGSRFWPMSTTENPKQFIDVLGvGKTLLQLTVERFGNLVKPENIWVVTNQSYQEIVKKQLPDMPAGNIL 83
Cdd:COG0836 1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLG-EKSLLQQTVERLAGLVPPENILVVTNEEHRFLVAEQLPELGPANIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 84 CEPCRRNTAPCIAYVSWRIKSKDPKANIIVTPSDHIVTDKAEFQRVIKECMQFTsETDAIVTLGMKPNRPETGYGYIQAD 163
Cdd:COG0836 80 LEPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAA-EAGKLVTFGIKPTRPETGYGYIEAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 164 lstSSLRNKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGTDKEQEEI 243
Cdd:COG0836 159 ---EALGGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 244 NRLFPECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSLHEQSKKDLYGNVSIGpDVNLIESHNCIVHTmQEKKVVIQ 323
Cdd:COG0836 236 AEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLG-DVLLIDSSNSLVRS-EGRLVAVI 313
|
330 340
....*....|....*....|....*...
gi 502828281 324 GLDGYIVAENNDTLLICKLSEEQRIKQF 351
Cdd:COG0836 314 GVEDLVVVDTPDALLVAPKDRAQEVKKI 341
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
9-284 |
1.12e-131 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 376.92 E-value: 1.12e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMSTTENPKQFIDVLGvGKTLLQLTVERFGNLVKPENIWVVTNQSYQEIVKKQLPD-MPAGNILCEPC 87
Cdd:cd02509 4 VILAGGSGTRLWPLSRESYPKQFLKLFG-DKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREQLPEgLPEENIILEPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 88 RRNTAPCIAYVSWRIKSKDPKANIIVTPSDHIVTDKAEFQRVIKECMQFtSETDAIVTLGMKPNRPETGYGYIQADLSTS 167
Cdd:cd02509 83 GRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEA-AEEGYLVTFGIKPTRPETGYGYIEAGEKLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 168 slrnKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGTDKEQEEINRLF 247
Cdd:cd02509 162 ----GGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTDDFLRLLEEAF 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 502828281 248 PECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSL 284
Cdd:cd02509 238 AKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
|
|
| GMP_PMI |
TIGR01479 |
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ... |
9-349 |
2.83e-90 |
|
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 273648 [Multi-domain] Cd Length: 468 Bit Score: 278.44 E-value: 2.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMSTTENPKQFIDVLGVGkTLLQLTVERFGNLVKPENIwVVTNQSYQEIVKKQLP--DMPAGNILCEP 86
Cdd:TIGR01479 4 VILAGGSGTRLWPLSRELYPKQFLALVGDL-TMLQQTLKRLAGLPCSSPL-VICNEEHRFIVAEQLReiGKLASNIILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 87 CRRNTAPCIAYVS-WRIKSKDPKANIIVTPSDHIVTDKAEFQRVIKECMQFTSEtDAIVTLGMKPNRPETGYGYIQAdls 165
Cdd:TIGR01479 82 VGRNTAPAIALAAlLAARRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAE-GKLVTFGIVPTHPETGYGYIRR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 166 TSSLRNKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGTD-------K 238
Cdd:TIGR01479 158 GAPLAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDldfirldK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 239 EQeeinrlFPECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSLHEQSKKDLYGNVSIGpDVNLIESHNCIVHTmQEK 318
Cdd:TIGR01479 238 EA------FEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKG-DVLTHDTKNSYIYS-ESR 309
|
330 340 350
....*....|....*....|....*....|.
gi 502828281 319 KVVIQGLDGYIVAENNDTLLICKLSEEQRIK 349
Cdd:TIGR01479 310 LVAVVGVEDLVVVETKDAVLVAHKDRVQDVK 340
|
|
| cpsB |
PRK15460 |
mannose-1-phosphate guanyltransferase; Provisional |
1-350 |
7.93e-68 |
|
mannose-1-phosphate guanyltransferase; Provisional
Pssm-ID: 185357 [Multi-domain] Cd Length: 478 Bit Score: 220.61 E-value: 7.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 1 MARTNNHLVIMAGGVGSRFWPMSTTENPKQFIDVLGvGKTLLQLTVERFgNLVKPENIWVVTNQSYQEIVKKQLPDMP-- 78
Cdd:PRK15460 1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKG-DLTMLQTTICRL-NGVECESPVVICNEQHRFIVAEQLRQLNkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 79 AGNILCEPCRRNTAPCIAYVSWRIKSKDPKAN--IIVTPSDHIVTDKAEFQRVIKECMQFtSETDAIVTLGMKPNRPETG 156
Cdd:PRK15460 79 TENIILEPAGRNTAPAIALAALAAKRHSPESDplMLVLAADHVIADEDAFRAAVRNAMPY-AEAGKLVTFGIVPDLPETG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 157 YGYIQADLSTSSLRNKEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFIWNVNTIVNAFRIYQPSMAKIFESLLPIYGT 236
Cdd:PRK15460 158 YGYIRRGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 237 DKEQEEINR-LFPECENISVDYAIMEKAEEIFVCPSDFGWSDLGTWGSLHEQSKKDLYGNVSIGpDVNLIESHNCIVHTm 315
Cdd:PRK15460 238 DLDFIRVDEeAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHG-DVINHKTENSYVYA- 315
|
330 340 350
....*....|....*....|....*....|....*
gi 502828281 316 QEKKVVIQGLDGYIVAENNDTLLICKLSEEQRIKQ 350
Cdd:PRK15460 316 ESGLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKK 350
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
9-292 |
2.05e-41 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 145.09 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMSTTENPKQFIdvLGVGKTLLQLTVERFGNlVKPENIWVVTNQSYQEIVKKQLPDMP--AGNILC-- 84
Cdd:pfam00483 3 IILAGGSGTRLWPLTRTLAKPLVP--VGGKYPLIDYPLSRLAN-AGIREIIVILTQEHRFMLNELLGDGSkfGVQITYal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 85 EPCRRNTAPCIAYVSWRIKskDPKANIIVTPSDHIVtdKAEFQRVIKECMQftSETDAIVTLGMKPNRPETGYGYIQADl 164
Cdd:pfam00483 80 QPEGKGTAPAVALAADFLG--DEKSDVLVLGGDHIY--RMDLEQAVKFHIE--KAADATVTFGIVPVEPPTGYGVVEFD- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 165 stsslrnkEIFRVDSFREKPNLETAQEYIKKNYYFWNAGIFiwnvntiVNAFRIYQPSmakifesllpiygtDKEQEEIN 244
Cdd:pfam00483 153 --------DNGRVIRFVEKPKLPKASNYASMGIYIFNSGVL-------DFLAKYLEEL--------------KRGEDEIT 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 502828281 245 RLFPE-CENISVDYAIMEKaeeifvcpsDFGWSDLGTWGSLHEQSKKDL 292
Cdd:pfam00483 204 DILPKaLEDGKLAYAFIFK---------GYAWLDVGTWDSLWEANLFLL 243
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
9-286 |
6.58e-13 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 67.49 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMsTTENPKQFIDVLgvGKTLLQLTVERfgnLVK--PENIWVVTNqsYQ-EIVKKQLPDMPAGNI--- 82
Cdd:COG1208 3 VILAGGLGTRLRPL-TDTRPKPLLPVG--GKPLLEHILER---LAAagITEIVINVG--YLaEQIEEYFGDGSRFGVrit 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 83 -LCEPCRRNTAPCIAYVSWRIKSKDpkanIIVTPSDhIVTDkAEFQRVIKecmqFTSETDAIVTLGMKPNRPETGYGYIQ 161
Cdd:COG1208 75 yVDEGEPLGTGGALKRALPLLGDEP----FLVLNGD-ILTD-LDLAALLA----FHREKGADATLALVPVPDPSRYGVVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 162 ADlstsslrnkEIFRVDSFREKPNlETAQEYIkknyyfwNAGIFIWNvntivnafriyqpsmAKIFESLlpiygTDKEQE 241
Cdd:COG1208 145 LD---------GDGRVTRFVEKPE-EPPSNLI-------NAGIYVLE---------------PEIFDYI-----PEGEPF 187
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 502828281 242 EINRLFPEcenisvdyaiMEKAEEIFVCPSDFGWSDLGTWGSLHE 286
Cdd:COG1208 188 DLEDLLPR----------LIAEGRVYGYVHDGYWLDIGTPEDLLE 222
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
9-279 |
4.42e-10 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 58.75 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMsTTENPKQFIDVLgvGKTLLQLTVERFgNLVKPENIWVVTNqsYQ-EIVKKQLPDMPAGNILCEPC 87
Cdd:cd04181 2 VILAAGKGTRLRPL-TDTRPKPLLPIA--GKPILEYIIERL-ARAGIDEIILVVG--YLgEQIEEYFGDGSKFGVNIEYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 88 ----RRNTAPCIAYVSWRIKSKDpkanIIVTPSDhIVTDKAefqrvIKECMQFTSETDAIVTLGMKPNRPETGYGYIQAD 163
Cdd:cd04181 76 vqeePLGTAGAVRNAEDFLGDDD----FLVVNGD-VLTDLD-----LSELLRFHREKGADATIAVKEVEDPSRYGVVELD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 164 lstsslrnkEIFRVDSFREKPNLETAqeyikknyYFWNAGIFIwnvntivnaFRiyqpsmAKIFEsLLPIYGTDKEqEEI 243
Cdd:cd04181 146 ---------DDGRVTRFVEKPTLPES--------NLANAGIYI---------FE------PEILD-YIPEILPRGE-DEL 191
|
250 260 270
....*....|....*....|....*....|....*.
gi 502828281 244 NRLFPecenisvdyaIMEKAEEIFVCPSDFGWSDLG 279
Cdd:cd04181 192 TDAIP----------LLIEEGKVYGYPVDGYWLDIG 217
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-75 |
1.15e-07 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 51.76 E-value: 1.15e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 6 NHLVIMAGGVGSRFwpmsTTENPKQFIDVLgvGKTLLQLTVERFGNLVKPENIWVVTNQSYQEIVKKQLP 75
Cdd:cd02516 1 VAAIILAAGSGSRM----GADIPKQFLELG--GKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAK 64
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
9-76 |
9.84e-07 |
|
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: 48.97 E-value: 9.84e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502828281 9 VIMAGGVGSRFwpmsTTENPKQFIDVLGvgKTLLQLTVERFGNLVKPENIWVVTNQSYQEIVKKQLPD 76
Cdd:COG1211 1 IIPAAGSGSRM----GAGIPKQFLPLGG--KPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAK 62
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
9-212 |
5.98e-06 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 46.74 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRFWPMstTEN-PKQFIDVlGvGKTLLQLTVERFgNLVKPENIWVVTNqsYQ-EIVKKQLPDMPAGNI---- 82
Cdd:cd06426 2 VIMAGGKGTRLRPL--TENtPKPMLKV-G-GKPILETIIDRF-IAQGFRNFYISVN--YLaEMIEDYFGDGSKFGVnisy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 83 LCEPCRRNTAPCIAYVswrikSKDPKANIIVTPSDhIVTdKAEFQRVIKecmqFTSETDAIVTLGMKPNRPETGYGYIQA 162
Cdd:cd06426 75 VREDKPLGTAGALSLL-----PEKPTDPFLVMNGD-ILT-NLNYEHLLD----FHKENNADATVCVREYEVQVPYGVVET 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502828281 163 DLStsslrnkeifRVDSFREKPNLetaqeyikknYYFWNAGIFIWNVNTI 212
Cdd:cd06426 144 EGG----------RITSIEEKPTH----------SFLVNAGIYVLEPEVL 173
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
5-74 |
4.18e-05 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 44.35 E-value: 4.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 5 NNHLVIMAGGVGSRfwpMSTTEnPKQFIDVLgvGKTLLQLTVERFGNLVKPENIWVVTNQSYQEIVKKQL 74
Cdd:PRK00155 3 MVYAIIPAAGKGSR---MGADR-PKQYLPLG--GKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELL 66
|
|
| PLN02728 |
PLN02728 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase |
9-78 |
7.78e-04 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
Pssm-ID: 215387 Cd Length: 252 Bit Score: 40.49 E-value: 7.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828281 9 VIMAGGVGSRfwpMSTTEnPKQFIDVLGVGKTLLQLtvERFGNLVKPENIWVVTNQSYQEIVKKQLPDMP 78
Cdd:PLN02728 28 ILLAGGVGKR---MGANM-PKQYLPLLGQPIALYSL--YTFARMPEVKEIVVVCDPSYRDVFEEAVENID 91
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
9-49 |
8.83e-04 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 40.22 E-value: 8.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 502828281 9 VIMAGGVGSRFWPMsTTENPKQFIDVLgvGKTLLQLTVERF 49
Cdd:COG1213 3 VILAAGRGSRLGPL-TDDIPKCLVEIG--GKTLLERQLEAL 40
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
9-63 |
2.87e-03 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 38.75 E-value: 2.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 502828281 9 VIMAGGVGSRFWPMsTTENPKQFIDVLgvGKTLLQLTVERFGNlVKPENIWVVTN 63
Cdd:cd02523 2 IILAAGRGSRLRPL-TEDRPKCLLEIN--GKPLLERQIETLKE-AGIDDIVIVTG 52
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
9-75 |
3.03e-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: 38.33 E-value: 3.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502828281 9 VIMAGGVGSRfwpMSTtenPKQFIDvLGvGKTLLQLTVERFGNLVKPenIWVVTNQSYQEIVKKQLP 75
Cdd:cd02503 4 VILAGGKSRR---MGG---DKALLE-LG-GKPLLEHVLERLKPLVDE--VVISANRDQERYALLGVP 60
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
9-80 |
6.83e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 37.09 E-value: 6.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502828281 9 VIMAGGVGSRFWpmstteNPKQFIDvLGvGKTLLQLTVERFGNLVkpENIWVVTN--QSYQEIVKKQLPDMPAG 80
Cdd:COG0746 8 VILAGGRSRRMG------QDKALLP-LG-GRPLLERVLERLRPQV--DEVVIVANrpERYAALGVPVVPDDPPG 71
|
|
| |
