|
Name |
Accession |
Description |
Interval |
E-value |
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
5-349 |
4.83e-180 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 502.29 E-value: 4.83e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 5 NDIQIIIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPICPVENMWVVTNEKYIRIVKEQIPDMPVDNIL 84
Cdd:COG0836 1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLG-EKSLLQQTVERLAGLVPPENILVVTNEEHRFLVAEQLPELGPANIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 85 AEPEARNTAPCIAYACWKIQKQHPDANIVVTPSDALVINTSEYQRVLSKALSYTSdKNAIVTIGIKPSRPETGYGYIASA 164
Cdd:COG0836 80 LEPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAAE-AGKLVTFGIKPTRPETGYGYIEAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 165 EPTSVDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQLASIMDEMAPSFYTEQEKEVVGKL 244
Cdd:COG0836 159 EALGGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLDAEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 245 FPTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSLRTLLPQDEAGNAKIGkDIRLYECKNCVVHaADESKVVVQGLD 324
Cdd:COG0836 239 FAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLG-DVLLIDSSNSLVR-SEGRLVAVIGVE 316
|
330 340
....*....|....*....|....*
gi 2127557458 325 GYIVAEKNGQLLVCSLKEEQRIKEF 349
Cdd:COG0836 317 DLVVVDTPDALLVAPKDRAQEVKKI 341
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
7-282 |
3.46e-134 |
|
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: 383.08 E-value: 3.46e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 7 IQIIIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPICPVENMWVVTNEKYIRIVKEQIPD-MPVDNILA 85
Cdd:cd02509 1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFG-DKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREQLPEgLPEENIIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 86 EPEARNTAPCIAYACWKIQKQHPDANIVVTPSDALVINTSEYQRVLSKALSYtSDKNAIVTIGIKPSRPETGYGYIASAE 165
Cdd:cd02509 80 EPEGRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEA-AEEGYLVTFGIKPTRPETGYGYIEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 166 PTSvDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQLASIMDEMAPSFYTEQEKEVVGKLF 245
Cdd:cd02509 159 KLG-GGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTDDFLRLLEEAF 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 2127557458 246 PTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSL 282
Cdd:cd02509 238 AKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
|
|
| GMP_PMI |
TIGR01479 |
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ... |
10-348 |
8.90e-84 |
|
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: 261.49 E-value: 8.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPIcPVENMWVVTNEKYIRIVKEQIP--DMPVDNILAEP 87
Cdd:TIGR01479 4 VILAGGSGTRLWPLSRELYPKQFLALVG-DLTMLQQTLKRLAGL-PCSSPLVICNEEHRFIVAEQLReiGKLASNIILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 88 EARNTAPCIAYACWK-IQKQHPDANIVVTPSDALVINTSEYQRVLSKALSYtSDKNAIVTIGIKPSRPETGYGYIASAEP 166
Cdd:TIGR01479 82 VGRNTAPAIALAALLaARRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPA-AAEGKLVTFGIVPTHPETGYGYIRRGAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 167 TSVDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQ-----LASIMDEMAPSFYTEQEKEVv 241
Cdd:TIGR01479 161 LAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDiyeacEAAVEASEPDLDFIRLDKEA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 242 gklFPTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSLRTLLPQDEAGNAKIGkDIRLYECKNCVVHAadESKVV-V 320
Cdd:TIGR01479 240 ---FEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKG-DVLTHDTKNSYIYS--ESRLVaV 313
|
330 340
....*....|....*....|....*...
gi 2127557458 321 QGLDGYIVAEKNGQLLVCSLKEEQRIKE 348
Cdd:TIGR01479 314 VGVEDLVVVETKDAVLVAHKDRVQDVKK 341
|
|
| cpsB |
PRK15460 |
mannose-1-phosphate guanyltransferase; Provisional |
10-332 |
3.73e-68 |
|
mannose-1-phosphate guanyltransferase; Provisional
Pssm-ID: 185357 [Multi-domain] Cd Length: 478 Bit Score: 221.39 E-value: 3.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPIcPVENMWVVTNEKYIRIVKEQIPDMP--VDNILAEP 87
Cdd:PRK15460 9 VVMAGGSGSRLWPLSRVLYPKQFLCLKG-DLTMLQTTICRLNGV-ECESPVVICNEQHRFIVAEQLRQLNklTENIILEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 88 EARNTAPCIAYACWKIQKQHPDAN--IVVTPSDALVINTSEYQRVLSKALSYtSDKNAIVTIGIKPSRPETGYGYIASAE 165
Cdd:PRK15460 87 AGRNTAPAIALAALAAKRHSPESDplMLVLAADHVIADEDAFRAAVRNAMPY-AEAGKLVTFGIVPDLPETGYGYIRRGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 166 PTSVDE---IYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQLAS----IMDEMAPSF-YTEQE 237
Cdd:PRK15460 166 VSAGEQdtvAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDacekAMSAVDPDLdFIRVD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 238 KEVvgklFPTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSLRTLLPQDEAGNAKIGkDIRLYECKNCVVHAAD--- 314
Cdd:PRK15460 246 EEA----FLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHG-DVINHKTENSYVYAESglv 320
|
330 340
....*....|....*....|...
gi 2127557458 315 -----ESKVVVQGLDGYIVAEKN 332
Cdd:PRK15460 321 ttvgvKDLVVVQTKDAVLIADRN 343
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
10-290 |
1.43e-39 |
|
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: 140.08 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFWPMSTPDYPKQFIdvMGVGRSLIQLTVDRLKPIcPVENMWVVTNEKYIRIVKEQIPDMP----VDNILA 85
Cdd:pfam00483 3 IILAGGSGTRLWPLTRTLAKPLVP--VGGKYPLIDYPLSRLANA-GIREIIVILTQEHRFMLNELLGDGSkfgvQITYAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 86 EPEARNTAPCIAYACWKIQKQHPDanIVVTPSDalVINTSEYQRVLSKALSYTSDKnaIVTIGIKPSRPETGYGYIAsae 165
Cdd:pfam00483 80 QPEGKGTAPAVALAADFLGDEKSD--VLVLGGD--HIYRMDLEQAVKFHIEKAADA--TVTFGIVPVEPPTGYGVVE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 166 ptsVDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVwnidtisktirtfqpQLASIMDEMaPSFYTEQEKEvvgkLF 245
Cdd:pfam00483 151 ---FDDNGRVIRFVEKPKLPKASNYASMGIYIFNSGVLD---------------FLAKYLEEL-KRGEDEITDI----LP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2127557458 246 PTCEKISIDYAVMEKskkiytlpaEFGWSDLGSWGSLRTLLPQDE 290
Cdd:pfam00483 208 KALEDGKLAYAFIFK---------GYAWLDVGTWDSLWEANLFLL 243
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
5-349 |
4.83e-180 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 502.29 E-value: 4.83e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 5 NDIQIIIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPICPVENMWVVTNEKYIRIVKEQIPDMPVDNIL 84
Cdd:COG0836 1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLG-EKSLLQQTVERLAGLVPPENILVVTNEEHRFLVAEQLPELGPANIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 85 AEPEARNTAPCIAYACWKIQKQHPDANIVVTPSDALVINTSEYQRVLSKALSYTSdKNAIVTIGIKPSRPETGYGYIASA 164
Cdd:COG0836 80 LEPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAAE-AGKLVTFGIKPTRPETGYGYIEAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 165 EPTSVDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQLASIMDEMAPSFYTEQEKEVVGKL 244
Cdd:COG0836 159 EALGGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLDAEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 245 FPTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSLRTLLPQDEAGNAKIGkDIRLYECKNCVVHaADESKVVVQGLD 324
Cdd:COG0836 239 FAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLG-DVLLIDSSNSLVR-SEGRLVAVIGVE 316
|
330 340
....*....|....*....|....*
gi 2127557458 325 GYIVAEKNGQLLVCSLKEEQRIKEF 349
Cdd:COG0836 317 DLVVVDTPDALLVAPKDRAQEVKKI 341
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
7-282 |
3.46e-134 |
|
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: 383.08 E-value: 3.46e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 7 IQIIIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPICPVENMWVVTNEKYIRIVKEQIPD-MPVDNILA 85
Cdd:cd02509 1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFG-DKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREQLPEgLPEENIIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 86 EPEARNTAPCIAYACWKIQKQHPDANIVVTPSDALVINTSEYQRVLSKALSYtSDKNAIVTIGIKPSRPETGYGYIASAE 165
Cdd:cd02509 80 EPEGRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEA-AEEGYLVTFGIKPTRPETGYGYIEAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 166 PTSvDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQLASIMDEMAPSFYTEQEKEVVGKLF 245
Cdd:cd02509 159 KLG-GGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTDDFLRLLEEAF 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 2127557458 246 PTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSL 282
Cdd:cd02509 238 AKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
|
|
| GMP_PMI |
TIGR01479 |
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ... |
10-348 |
8.90e-84 |
|
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: 261.49 E-value: 8.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPIcPVENMWVVTNEKYIRIVKEQIP--DMPVDNILAEP 87
Cdd:TIGR01479 4 VILAGGSGTRLWPLSRELYPKQFLALVG-DLTMLQQTLKRLAGL-PCSSPLVICNEEHRFIVAEQLReiGKLASNIILEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 88 EARNTAPCIAYACWK-IQKQHPDANIVVTPSDALVINTSEYQRVLSKALSYtSDKNAIVTIGIKPSRPETGYGYIASAEP 166
Cdd:TIGR01479 82 VGRNTAPAIALAALLaARRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPA-AAEGKLVTFGIVPTHPETGYGYIRRGAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 167 TSVDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQ-----LASIMDEMAPSFYTEQEKEVv 241
Cdd:TIGR01479 161 LAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDiyeacEAAVEASEPDLDFIRLDKEA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 242 gklFPTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSLRTLLPQDEAGNAKIGkDIRLYECKNCVVHAadESKVV-V 320
Cdd:TIGR01479 240 ---FEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKG-DVLTHDTKNSYIYS--ESRLVaV 313
|
330 340
....*....|....*....|....*...
gi 2127557458 321 QGLDGYIVAEKNGQLLVCSLKEEQRIKE 348
Cdd:TIGR01479 314 VGVEDLVVVETKDAVLVAHKDRVQDVKK 341
|
|
| cpsB |
PRK15460 |
mannose-1-phosphate guanyltransferase; Provisional |
10-332 |
3.73e-68 |
|
mannose-1-phosphate guanyltransferase; Provisional
Pssm-ID: 185357 [Multi-domain] Cd Length: 478 Bit Score: 221.39 E-value: 3.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFWPMSTPDYPKQFIDVMGvGRSLIQLTVDRLKPIcPVENMWVVTNEKYIRIVKEQIPDMP--VDNILAEP 87
Cdd:PRK15460 9 VVMAGGSGSRLWPLSRVLYPKQFLCLKG-DLTMLQTTICRLNGV-ECESPVVICNEQHRFIVAEQLRQLNklTENIILEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 88 EARNTAPCIAYACWKIQKQHPDAN--IVVTPSDALVINTSEYQRVLSKALSYtSDKNAIVTIGIKPSRPETGYGYIASAE 165
Cdd:PRK15460 87 AGRNTAPAIALAALAAKRHSPESDplMLVLAADHVIADEDAFRAAVRNAMPY-AEAGKLVTFGIVPDLPETGYGYIRRGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 166 PTSVDE---IYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVWNIDTISKTIRTFQPQLAS----IMDEMAPSF-YTEQE 237
Cdd:PRK15460 166 VSAGEQdtvAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDacekAMSAVDPDLdFIRVD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 238 KEVvgklFPTCEKISIDYAVMEKSKKIYTLPAEFGWSDLGSWGSLRTLLPQDEAGNAKIGkDIRLYECKNCVVHAAD--- 314
Cdd:PRK15460 246 EEA----FLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHG-DVINHKTENSYVYAESglv 320
|
330 340
....*....|....*....|...
gi 2127557458 315 -----ESKVVVQGLDGYIVAEKN 332
Cdd:PRK15460 321 ttvgvKDLVVVQTKDAVLIADRN 343
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
10-290 |
1.43e-39 |
|
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: 140.08 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFWPMSTPDYPKQFIdvMGVGRSLIQLTVDRLKPIcPVENMWVVTNEKYIRIVKEQIPDMP----VDNILA 85
Cdd:pfam00483 3 IILAGGSGTRLWPLTRTLAKPLVP--VGGKYPLIDYPLSRLANA-GIREIIVILTQEHRFMLNELLGDGSkfgvQITYAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 86 EPEARNTAPCIAYACWKIQKQHPDanIVVTPSDalVINTSEYQRVLSKALSYTSDKnaIVTIGIKPSRPETGYGYIAsae 165
Cdd:pfam00483 80 QPEGKGTAPAVALAADFLGDEKSD--VLVLGGD--HIYRMDLEQAVKFHIEKAADA--TVTFGIVPVEPPTGYGVVE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 166 ptsVDEIYKVEAFKEKPNLETAEQYLAAGNYYWNAGIFVwnidtisktirtfqpQLASIMDEMaPSFYTEQEKEvvgkLF 245
Cdd:pfam00483 151 ---FDDNGRVIRFVEKPKLPKASNYASMGIYIFNSGVLD---------------FLAKYLEEL-KRGEDEITDI----LP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2127557458 246 PTCEKISIDYAVMEKskkiytlpaEFGWSDLGSWGSLRTLLPQDE 290
Cdd:pfam00483 208 KALEDGKLAYAFIFK---------GYAWLDVGTWDSLWEANLFLL 243
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
10-277 |
5.38e-14 |
|
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: 70.30 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFWPMsTPDYPKQFIDVmgVGRSLIQLTVDRLKPiCPVENMWVVTNEKyirivKEQI---------PDMPV 80
Cdd:cd04181 2 VILAAGKGTRLRPL-TDTRPKPLLPI--AGKPILEYIIERLAR-AGIDEIILVVGYL-----GEQIeeyfgdgskFGVNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 81 DnILAEPEARNTAPCIAYACWKIqkqhPDANIVVTPSDALV-INtseyqrvLSKALSYTSDKNAIVTIGIKPSRPETGYG 159
Cdd:cd04181 73 E-YVVQEEPLGTAGAVRNAEDFL----GDDDFLVVNGDVLTdLD-------LSELLRFHREKGADATIAVKEVEDPSRYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 160 YIAsaeptsVDEIYKVEAFKEKPNLETaeqylaagNYYWNAGIFVwnidtisktirtFQPQLASIMDEMAPSFYTEqEKE 239
Cdd:cd04181 141 VVE------LDDDGRVTRFVEKPTLPE--------SNLANAGIYI------------FEPEILDYIPEILPRGEDE-LTD 193
|
250 260 270
....*....|....*....|....*....|....*...
gi 2127557458 240 VVGKlfptcekisidyavMEKSKKIYTLPAEFGWSDLG 277
Cdd:cd04181 194 AIPL--------------LIEEGKVYGYPVDGYWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
8-206 |
1.18e-12 |
|
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: 66.71 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 8 QIIIMAGGVGSRFWPMsTPDYPKQFIDVMgvGRSLIQLTVDRLKPiCPVENMWVVTNEKyirivKEQIPD-------MPV 80
Cdd:COG1208 1 KAVILAGGLGTRLRPL-TDTRPKPLLPVG--GKPLLEHILERLAA-AGITEIVINVGYL-----AEQIEEyfgdgsrFGV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 81 D-NILAEPEARNTAPCIAYACWKIQkqhpDANIVVTPSDALV-INtseyqrvLSKALSYTSDKNAIVTIGIKPSRPETGY 158
Cdd:COG1208 72 RiTYVDEGEPLGTGGALKRALPLLG----DEPFLVLNGDILTdLD-------LAALLAFHREKGADATLALVPVPDPSRY 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2127557458 159 GYIasaeptSVDEIYKVEAFKEKPnlETAEQYLAagnyywNAGIFVWN 206
Cdd:COG1208 141 GVV------ELDGDGRVTRFVEKP--EEPPSNLI------NAGIYVLE 174
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
10-73 |
4.78e-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: 49.83 E-value: 4.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127557458 10 IIMAGGVGSRFwpmsTPDYPKQFIDVMgvGRSLIQLTVDRLKPICPVENMWVVTNEKYIRIVKE 73
Cdd:cd02516 4 IILAAGSGSRM----GADIPKQFLELG--GKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKE 61
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
9-221 |
8.59e-07 |
|
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: 49.05 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 9 IIIMAGGVGSRFWPMsTPDYPKQFIDVmGvGRSLIQLTVDRLKPiCPVENMWVVTNEKyirivKEQIPD-------MPVD 81
Cdd:cd06426 1 VVIMAGGKGTRLRPL-TENTPKPMLKV-G-GKPILETIIDRFIA-QGFRNFYISVNYL-----AEMIEDyfgdgskFGVN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 82 -NILAEPEARNTAPCIAYAcwkiqKQHPDANIVVTPSDalVINTSEYQRVlskaLSYTSDKNAIVTIGIKPSRPETGYGY 160
Cdd:cd06426 72 iSYVREDKPLGTAGALSLL-----PEKPTDPFLVMNGD--ILTNLNYEHL----LDFHKENNADATVCVREYEVQVPYGV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127557458 161 IASAEPtsvdeiyKVEAFKEKPNLetaeqylaagNYYWNAGIFVWN---IDTISKTIRTFQPQL 221
Cdd:cd06426 141 VETEGG-------RITSIEEKPTH----------SFLVNAGIYVLEpevLDLIPKNEFFDMPDL 187
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
10-81 |
1.47e-05 |
|
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: 45.51 E-value: 1.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2127557458 10 IIMAGGVGSRFwpmsTPDYPKQFIDVmgVGRSLIQLTVDRLKPICPVENMWVVTNEKYIRIVKEQIPDMPVD 81
Cdd:COG1211 1 IIPAAGSGSRM----GAGIPKQFLPL--GGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGID 66
|
|
| MobA |
cd02503 |
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ... |
10-196 |
3.73e-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: 43.72 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFwpmstpDYPKQFIDVMGvgRSLIQLTVDRLKPICpvENMWVVTNEKY-------IRIVKEQIPDM-PVD 81
Cdd:cd02503 4 VILAGGKSRRM------GGDKALLELGG--KPLLEHVLERLKPLV--DEVVISANRDQeryallgVPVIPDEPPGKgPLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 82 NILAepearntapciayACWKIQKQHpdanIVVTPSDALVINTSEYQRVLSKAlsyTSDKNAIVtigikpsrPETGyGYI 161
Cdd:cd02503 74 GILA-------------ALRAAPADW----VLVLACDMPFLPPELLERLLAAA---EEGADAVV--------PKSG-GRL 124
|
170 180 190
....*....|....*....|....*....|....*
gi 2127557458 162 asaEPTSVdeIYKVEAfkekpnLETAEQYLAAGNY 196
Cdd:cd02503 125 ---QPLHA--LYHKSL------LPALEELLEAGER 148
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-196 |
6.56e-05 |
|
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: 43.26 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 1 MNNfnDIQIIIMAGGVGSRFWpmstpdYPKQFIDVMGvgRSLIQLTVDRLKPICpvENMWVVTN--EKY----IRIVKEQ 74
Cdd:COG0746 1 MTM--PITGVILAGGRSRRMG------QDKALLPLGG--RPLLERVLERLRPQV--DEVVIVANrpERYaalgVPVVPDD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 75 IPDM-PVDNILAepearntapciayacwkIQKQHPDANIVVTPSDALVINTSEYQRVLSKAlsyTSDKNAIVtigikpsr 153
Cdd:COG0746 69 PPGAgPLAGILA-----------------ALEAAPAEWVLVLACDMPFLPPDLVRRLLEAL---EEGADAVV-------- 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2127557458 154 PETGyGYIasaEPTSVdeIYKVEAfkekpnLETAEQYLAAGNY 196
Cdd:COG0746 121 PRSG-GRL---EPLFA--LYRRSL------LPALEAALAEGER 151
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
8-51 |
5.86e-04 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 40.99 E-value: 5.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2127557458 8 QIIIMAGGVGSRFWPMsTPDYPKQFIDVMgvGRSLIQLTVDRLK 51
Cdd:COG1213 1 KAVILAAGRGSRLGPL-TDDIPKCLVEIG--GKTLLERQLEALA 41
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
10-69 |
1.04e-03 |
|
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: 39.10 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 10 IIMAGGVGSRFwpmstpDYPKQFIDVmgVGRSLIQLTVDRLKPICpvENMWVVTNEKYIR 69
Cdd:pfam12804 2 VILAGGRSSRM------GGDKALLPL--GGKPLLERVLERLRPAG--DEVVVVANDEEVL 51
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
10-75 |
2.27e-03 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 38.96 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127557458 10 IIMAGGVGSRfwpMSTpDYPKQFIDVMgvGRSLIQLTVDRLKPICPVENMWVVTNEKYIRIVKEQI 75
Cdd:PRK00155 7 IIPAAGKGSR---MGA-DRPKQYLPLG--GKPILEHTLEAFLAHPRIDEIIVVVPPDDRPDFAELL 66
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
9-77 |
2.72e-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: 2.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127557458 9 IIIMAGGVGSRFWPMsTPDYPKQFIDVMgvGRSLIQLTVDRLKPiCPVENMWVVT--NEKYIRIVKEQIPD 77
Cdd:cd02523 1 AIILAAGRGSRLRPL-TEDRPKCLLEIN--GKPLLERQIETLKE-AGIDDIVIVTgyKKEQIEELLKKYPN 67
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
9-117 |
9.58e-03 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 37.23 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127557458 9 IIIMAGgVGSRFWPMSTpDYPKQFIDVMgvGRSLIQLTVDRLKPICPvenmwvvtnEKYIRIV-KEQIPDMPVDNilaep 87
Cdd:cd04183 2 IIPMAG-LGSRFKKAGY-TYPKPLIEVD--GKPMIEWVIESLAKIFD---------SRFIFICrDEHNTKFHLDE----- 63
|
90 100 110
....*....|....*....|....*....|
gi 2127557458 88 earntapciayacwKIQKQHPDANIVVTPS 117
Cdd:cd04183 64 --------------SLKLLAPNATVVELDG 79
|
|
| |
