|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
2-394 |
4.59e-97 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 295.02 E-value: 4.59e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 2 KLLIVTPHFYPEN----FKVNDMAFELQKRGHDVSVMTAIPDYPEGRFYKGygifkkRRESINGVKVHRSLIIPRHSGSS 77
Cdd:cd03794 1 KILLISQYYPPPKgaaaARVYELAKELVRRGHEVTVLTPSPNYPLGRIFAG------ATETKDGIRVIRVKLGPIKKNGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 78 FWLAMNYLSYTFFASLKSLWFGiaKKYDAIIVHEPsPILVGIPAVIIKKLQKIPVHFWVLDLWPESLTAAGGITNKNIIY 157
Cdd:cd03794 75 IRRLLNYLSFALAALLKLLVRE--ERPDVIIAYSP-PITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 158 PFEKLTKWIYDNCTTLMIGSKGYEKSICNKGDFKDKIEFFPNWVED----SLESQKMIDVPKLPKGFNVVIAGNMGDAQD 233
Cdd:cd03794 152 LLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWADLeefkPPPKDELRKKLGLDDKFVVVYAGNIGKAQG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 234 LPHIMETARMLKGS-NIRFNFIGDGRKREYVENYARENGLMNNIFcLGRYPLEAMPAFFAQADILFMALKDTPIFALTVP 312
Cdd:cd03794 232 LETLLEAAERLKRRpDIRFLFVGDGDEKERLKELAKARGLDNVTF-LGRVPKEEVPELLSAADVGLVPLKDNPANRGSSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 313 SRLQAYMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLSTlNKDELTQKGANGKEYSRKYYDFTKCINH 392
Cdd:cd03794 311 SKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLD-DPELRRAMGENGRELAEEKFSREKLADR 389
|
..
gi 1624566921 393 LE 394
Cdd:cd03794 390 LL 391
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
1-385 |
2.58e-26 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 109.30 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 1 MKLLIVTPHFYPENFKVN----DMAFELQKRGHDVSVMTAIPDYPEGRFYKGYGIFKKRRESINGVKVHRS-LIIPRH-S 74
Cdd:PRK10307 1 MKILVYGINYAPELTGIGkytgEMAEWLAARGHEVRVITAPPYYPQWRVGEGYSAWRYRRESEGGVTVWRCpLYVPKQpS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 75 G-------SSFWLAmnylsytffaSLKSLWFGIAKKYDAIIVHEPSpiLVGIP-AVIIKKLQKIPVHFWVLDLWPE---S 143
Cdd:PRK10307 81 GlkrllhlGSFALS----------SFFPLLAQRRWRPDRVIGVVPT--LFCAPgARLLARLSGARTWLHIQDYEVDaafG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 144 LTAAGGITNKNIIYPFEKltkWI---YDNCTTlmIGSKGYEKSIcNKGDFKDKIEFFPNWVEdsLESQKMIDVPK----- 215
Cdd:PRK10307 149 LGLLKGGKVARLATAFER---SLlrrFDNVST--ISRSMMNKAR-EKGVAAEKVIFFPNWSE--VARFQPVADADvdalr 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 216 ----LPKGFNVVI-AGNMGDAQDLPHIMETARMLKG-SNIRFNFIGDGRKREYVENYARENGLMNNIFcLGRYPLEAMPA 289
Cdd:PRK10307 221 aqlgLPDGKKIVLySGNIGEKQGLELVIDAARRLRDrPDLIFVICGQGGGKARLEKMAQCRGLPNVHF-LPLQPYDRLPA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 290 FFAQADILFMALK----DtpifaLTVPSRLQAYMSSGKPVVAMINgEGADTIRE-ADCGWSVPAGDSEQLANLLKHLSTl 364
Cdd:PRK10307 300 LLKMADCHLLPQKagaaD-----LVLPSKLTNMLASGRNVVATAE-PGTELGQLvEGIGVCVEPESVEALVAAIAALAR- 372
|
410 420
....*....|....*....|.
gi 1624566921 365 NKDELTQKGANGKEYSRKYYD 385
Cdd:PRK10307 373 QALLRPKLGTVAREYAERTLD 393
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
2-397 |
8.57e-24 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 101.46 E-value: 8.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 2 KLLIVTPHFYP-----ENFkVNDMAFELQKRGHDVSVMTAIPDYPEGRFYKGYGIFKKRRESINGVKVHRslIIPRHSGS 76
Cdd:cd03801 1 KILLLSPELPPpvggaERH-VRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARR--LLRELRPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 77 SFWLamnylsytffaslkslwfgiakKYDAIIVHEPSPILvgiPAVIIKKLQKIPVhFWVLDLWPESLTAAGGITNKNII 156
Cdd:cd03801 78 LRLR----------------------KFDVVHAHGLLAAL---LAALLALLLGAPL-VVTLHGAEPGRLLLLLAAERRLL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 157 YPFEKLTKWiYDNCTTLmigSKgYEKSICNK--GDFKDKIEFFPNWVEDSLES-QKMIDVPKLPKGFNVVIAGNMGDAQD 233
Cdd:cd03801 132 ARAEALLRR-ADAVIAV---SE-ALRDELRAlgGIPPEKIVVIPNGVDLERFSpPLRRKLGIPPDRPVLLFVGRLSPRKG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 234 LPHIMETARMLK--GSNIRFNFIG-DGRKREYVEnyARENGLMNNIFCLGRYPLEAMPAFFAQADILFMALKDTPiFALT 310
Cdd:cd03801 207 VDLLLEALAKLLrrGPDVRLVIVGgDGPLRAELE--ELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEG-FGLV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 311 VpsrLQAyMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLSTlNKDELTQKGANGKEYSRKYYDFTKCI 390
Cdd:cd03801 284 V---LEA-MAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLA-DPELRARLGRAARERVAERFSWERVA 358
|
....*..
gi 1624566921 391 NHLEKII 397
Cdd:cd03801 359 ERLLDLY 365
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
3-396 |
4.21e-23 |
|
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.
Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 99.76 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 3 LLIVTpHFYPENFK------VNDMAFELQKRGHDVSVMTAIPDYPegrfykgygifKKRRESINGVKVHRSLIIPRHSGS 76
Cdd:cd03798 1 VLILT-NIYPNANSpgrgifVRRQVRALSRRGVDVEVLAPAPWGP-----------AAARLLRKLLGEAVPPRDGRRLLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 77 SFWLAmnYLSYTFFAS--LKSLWFGIAKKYDAIIVHEPSPilVGIPAVIIKKLQKIPVhfwvldlwpeSLTAAGGITNKN 154
Cdd:cd03798 69 LKPRL--RLLAPLRAPslAKLLKRRRRGPPDLIHAHFAYP--AGFAAALLARLYGVPY----------VVTEHGSDINVF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 155 IIYP-FEKLTKWIYDNCTTLMIGSKGYEKSICNKGDFKDKIEFFPNWVeDSLESQKMIDVPKLP-KGFNVVIAGNMGD-- 230
Cdd:cd03798 135 PPRSlLRKLLRWALRRAARVIAVSKALAEELVALGVPRDRVDVIPNGV-DPARFQPEDRGLGLPlDAFVILFVGRLIPrk 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 231 -AQDLPHIMetARMLKGS-NIRFNFIGDGRKREYVENYARENGLMNNIFCLGRYPLEAMPAFFAQADIlfmalkdtpiFA 308
Cdd:cd03798 214 gIDLLLEAF--ARLAKARpDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDV----------FV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 309 LtvPSR--------LQAyMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLstLNKDELTQKGANGKEYS 380
Cdd:cd03798 282 L--PSRhegfglvlLEA-MACGLPVVATDVGGIPEVVGDPETGLLVPPGDADALAAALRRA--LAEPYLRELGEAARARV 356
|
410
....*....|....*.
gi 1624566921 381 RKYYDFTKCINHLEKI 396
Cdd:cd03798 357 AERFSWVKAADRIAAA 372
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
2-383 |
7.77e-16 |
|
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 78.09 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 2 KLLIVTPHFYPE-N---FKVNDMAFELQKRGHDVSVMTaiPDYPEGRFYKGYGIFkkRRESINGVKVHRsliiprhsgss 77
Cdd:cd03817 1 KIAIFTDTYLPQvNgvaTSVRNLARALEKRGHEVYVIT--PSDPGAEDEEEVVRY--RSFSIPIRKYHR----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 78 fwlamnylsYTFFASLKSLWFGIAKKYDAIIVHEPSPILVGIPAVIIKKLQKIPV----HFwvldLWPESL--TAAGGIT 151
Cdd:cd03817 66 ---------QHIPFPFKKAVIDRIKELGPDIIHTHTPFSLGKLGLRIARKLKIPIvhtyHT----MYEDYLhyIPKGKLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 152 NKNIIypfEKLTKWIYDNCTTLMIGSKGYEKSICNKGdFKDKIEFFPNWV-----EDSLESQKMIDVPKLPKGFNVVIAG 226
Cdd:cd03817 133 VKAVV---RKLVRRFYNHTDAVIAPSEKIKDTLREYG-VKGPIEVIPNGIdldkfEKPLNTEERRKLGLPPDEPILLYVG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 227 NMGDAQDLPHIMETARMLKGS-NIRFNFIGDGRKREYVENYARENGLMNNIFCLGRYPLEAMPAFFAQADiLFMALKDTP 305
Cdd:cd03817 209 RLAKEKNIDFLLRAFAELKKEpNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAAD-LFVFASTTE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 306 IFALTVpsrLQAyMSSGKPVVAmINGEGA-DTIREADCGWSVPAGDsEQLANLLKHLstLNKDELTQK-GANGKEYSRKY 383
Cdd:cd03817 288 TQGLVY---LEA-MAAGLPVVA-AKDPAAsELVEDGENGFLFEPND-ETLAEKLLHL--RENLELLRKlSKNAEISAREF 359
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
289-397 |
1.13e-14 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 70.02 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 289 AFFAQADILFMALKDTPiFALTVpsrLQAyMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLSTlNKDE 368
Cdd:COG0438 16 ALLAAADVFVLPSRSEG-FGLVL---LEA-MAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE-DPEL 89
|
90 100
....*....|....*....|....*....
gi 1624566921 369 LTQKGANGKEYSRKYYDFTKCINHLEKII 397
Cdd:COG0438 90 RRRLGEAARERAEERFSWEAIAERLLALY 118
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
190-385 |
2.87e-14 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 73.16 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 190 FKDKIEFFPNWVEDSL----ESQKMIDVPKLPKG-FNVVIAGNMGDAQDLPHIMETARMLKGS-NIRFNFIGDGRKREYV 263
Cdd:cd03819 148 DPERIRVIPNGVDTDRfppeAEAEERAQLGLPEGkPVVGYVGRLSPEKGWLLLVDAAAELKDEpDFRLLVAGDGPERDEI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 264 ENYARENGLMNNIFCLGryPLEAMPAFFAQADILFMALKDtPIFALTVpsrLQAyMSSGKPVVAMINGEGADTIREADCG 343
Cdd:cd03819 228 RRLVERLGLRDRVTFTG--FREDVPAALAASDVVVLPSLH-EEFGRVA---LEA-MACGTPVVATDVGGAREIVVHGRTG 300
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1624566921 344 WSVPAGDSEQLANLLKHLSTLNKD--ELTQKGANGKEYSRKYYD 385
Cdd:cd03819 301 LLVPPGDAEALADAIRAAKLLPEAreKLQAAAALTEAVRELLLR 344
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
19-394 |
1.25e-13 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.
Pssm-ID: 340837 [Multi-domain] Cd Length: 358 Bit Score: 71.47 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 19 DMAFELQKRGHDVSVMTAipdypegrfYKGYGIFKKRREsinGVKVHrSLIIPRHSgssfwlaMNYLSytFFASLKSLWF 98
Cdd:cd03808 18 PLIKALVKKGYEVHVIAP---------DGDKLSDELKEL---GVKVI-DIPILRRG-------INPLK--DLKALFKLYK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 99 GIAK-KYDAIIVHEPSPILVGIPAVIIKKlqKIPVHFWVLDLwpeSLTAAGGITNKNIIYPFEKltkWIYDNCTTLMIGS 177
Cdd:cd03808 76 LLKKeKPDIVHCHTPKPGILGRLAARLAG--VPKVIYTVHGL---GFVFTEGKLLRLLYLLLEK---LALLFTDKVIFVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 178 KGYEKSICNKGDFKDK-----------IEFFPNWVEDSLESQ-KMIDVPKL--PKGFNVVIagnmgdaqdlphimETARM 243
Cdd:cd03808 148 EDDRDLAIKKGIIKKKktvlipgsgvdLDRFQYSPESLPSEKvVFLFVARLlkDKGIDELI--------------EAAKI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 244 LK--GSNIRFNFIGDGRKREYVENYARENGLMNNIFCLGryPLEAMPAFFAQADilfmalkdtpIFALtvPSR------- 314
Cdd:cd03808 214 LKkkGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLG--FRSDVPELLAESD----------VFVL--PSYreglprs 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 315 LQAYMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLAnllKHLSTLNKD-ELTQK-GANGKEYSRKYYDFTKCINH 392
Cdd:cd03808 280 LLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALA---DAIEKLIEDpELRKEmGEAARKRVEEKFDEEKVVNK 356
|
..
gi 1624566921 393 LE 394
Cdd:cd03808 357 LL 358
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
19-384 |
2.20e-13 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 70.85 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 19 DMAFELQKRGHDVSVMtaipdypegrFYKGYGIFKKRRESINGVKVHRSLIIPRHSGSSFWLAMNYLSYtffasLKslwf 98
Cdd:cd03811 20 NLANALDKRGYDVTLV----------LLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKRI-----LK---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 99 giAKKYDAIIVHEPSP--ILVGIPAVIIKKLQKIpvHFWVLDLWPesltaaggitnkniIYPFEKLTKWIYDNCTTLMIG 176
Cdd:cd03811 81 --RAKPDVVISFLGFAtyIVAKLAAARSKVIAWI--HSSLSKLYY--------------LKKKLLLKLKLYKKADKIVCV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 177 SKGYEKS-ICNKGDFKDKIEFFPNWVEDSL---ESQKMIDVPKlPKGFNVVIAGNMGDAQDLPHIMETARML--KGSNIR 250
Cdd:cd03811 143 SKGIKEDlIRLGPSPPEKIEVIYNPIDIDRiraLAKEPILNEP-EDGPVILAVGRLDPQKGHDLLIEAFAKLrkKYPDVK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 251 FNFIGDGRKREYVENYARENGLMNNIFCLGR----YPleampaFFAQADILFMALKDTPiFALTVpsrLQAyMSSGKPVV 326
Cdd:cd03811 222 LVILGDGPLREELEKLAKELGLAERVIFLGFqsnpYP------YLKKADLFVLSSRYEG-FPNVL---LEA-MALGTPVV 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624566921 327 AMiNGEGADTI-READCGWSVPAGDSEQLANLLKHLSTLNKDELTQK--GANGKEYSRKYY 384
Cdd:cd03811 291 ST-DCPGPREIlDDGENGLLVPDGDAAALAGILAALLQKKLDAALRErlAKAQEAVFREYT 350
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
80-396 |
2.86e-13 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 70.42 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 80 LAMNYLSYtfFASLKSLWFGIAK-KYDAIIVHEPSPILVGIPAviiKKLQKIPVHFW-VLDLW-PESLTaagGITNKniI 156
Cdd:cd03807 57 LGLSSGKD--PGVLLRLAKLIRKrNPDVVHTWMYHADLIGGLA---AKLAGGVKVIWsVRSSNiPQRLT---RLVRK--L 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 157 YPFekLTKWIYDNCTTlmigSKGYEKSICNKGDFKDKIEFFPNWVE---------DSLESQKMIDVPKlpKGFNVVIAGN 227
Cdd:cd03807 127 CLL--LSKFSPATVAN----SSAVAEFHQEQGYAKNKIVVIYNGIDlfklspddaSRARARRRLGLAE--DRRVIGIVGR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 228 MGDAQDLPHIMETARMLK--GSNIRFNFIGDGRKREYVENYARENGLMNNIFCLGryPLEAMPAFFAQADILFMAlKDTP 305
Cdd:cd03807 199 LHPVKDHSDLLRAAALLVetHPDLRLLLVGRGPERPNLERLLLELGLEDRVHLLG--ERSDVPALLPAMDIFVLS-SRTE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 306 IFALTVpsrLQAyMSSGKPVVAMINGEGADTIREAdCGWSVPAGDSEQLANLLKHLsTLNKDELTQKGANGKEYSRKYYD 385
Cdd:cd03807 276 GFPNAL---LEA-MACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAIRAL-LEDPEKRARLGRAARERIANEFS 349
|
330
....*....|.
gi 1624566921 386 FTKCINHLEKI 396
Cdd:cd03807 350 IDAMVRRYETL 360
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
222-378 |
4.75e-12 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 63.45 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 222 VVIAGNMGDAQDLPHIMETARMLK--GSNIRFNFIGDGRKREYVENYARENGLMNNIFCLGRYPLEAMPAFFAQADILFM 299
Cdd:pfam00534 5 ILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 300 ALKDTPiFALTVpsrLQAyMSSGKPVVAmINGEG-ADTIREADCGWSVPAGDSEQLANLLKHLstLNKDELTQK-GANGK 377
Cdd:pfam00534 85 PSRYEG-FGIVL---LEA-MACGLPVIA-SDVGGpPEVVKDGETGFLVKPNNAEALAEAIDKL--LEDEELRERlGENAR 156
|
.
gi 1624566921 378 E 378
Cdd:pfam00534 157 K 157
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
2-363 |
1.01e-11 |
|
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).
Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 65.81 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 2 KLLIVTPHFYP------ENFkVNDMAFELQKRGHDVSVMTAipdypegrfykgygifkkrrESINGVKVHRSLIIPRHSG 75
Cdd:cd03823 1 KILLVNSLYPPqrvggaEIS-VHDLAEALVAEGHEVAVLTA--------------------GVGPPGQATVARSVVRYRR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 76 SSFWLAMNYLSYTFFASLKSLWFGIAKKYDAII-------VHEPSPILVGIPAVIIKKLQKIPVHFWVLDLWPesltaag 148
Cdd:cd03823 60 APDETLPLALKRRGYELFETYNPGLRRLLARLLedfrpdvVHTHNLSGLGASLLDAARDLGIPVVHTLHDYWL------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 149 gitnkniIYPFEKLTKWIYDncttLMIGSKGYEKSIC-NKGDFKDKIEFFPNWVEdsLESQKMIDVPKLPKGFNVVIAGN 227
Cdd:cd03823 133 -------LCPRQFLFKKGGD----AVLAPSRFTANLHeANGLFSARISVIPNAVE--PDLAPPPRRRPGTERLRFGYIGR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 228 MGDAQDLPHIMETARMLKGSNIRFNFIGDGRkreyvENYARENGLMNNIFCLGRYPLEAMPAFFAQADILFmalkdtpif 307
Cdd:cd03823 200 LTEEKGIDLLVEAFKRLPREDIELVIAGHGP-----LSDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLV--------- 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624566921 308 altVPSR---------LQAyMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLST 363
Cdd:cd03823 266 ---VPSIwpepfglvvREA-IAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLT 326
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
219-361 |
1.45e-10 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 58.68 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 219 GFNVVIAGNMGDAQD--------LPHIMEtarmlKGSNIRFNFIGDGRKREYVEnyaRENGLMNNIFCLGRypLEAMPAF 290
Cdd:pfam13692 1 RPVILFVGRLHPNVKgvdylleaVPLLRK-----RDNDVRLVIVGDGPEEELEE---LAAGLEDRVIFTGF--VEDLAEL 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1624566921 291 FAQADILFMALKDTPiFALTVpsrLQAyMSSGKPVVAMINGEGADTIREaDCGWSVPAGDSEQLANLLKHL 361
Cdd:pfam13692 71 LAAADVFVLPSLYEG-FGLKL---LEA-MAAGLPVVATDVGGIPELVDG-ENGLLVPPGDPEALAEAILRL 135
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
2-383 |
6.27e-09 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 57.30 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 2 KLLIVTPHFYPE----NFKVNDMAFELQKRGHDVSVMTAIPDYPEGRfykgygifkkRRESINGVkvhRSLIIPRHSGSs 77
Cdd:cd03814 1 RIALVTDTYHPQvngvVRTLERLVDHLRRRGHEVRVVAPGPFDEAES----------AEGRVVSV---PSFPLPFYPEY- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 78 fwlamnYLSYTFFASLKSLWfgiaKKYDAIIVHEPSPILVGIPAVIIKKLQKIPVHFWVLDLWPESLTAAGGItnkniiy 157
Cdd:cd03814 67 ------RLALPLPRRVRRLI----KEFQPDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYTLG------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 158 PFEKLT----KWIYDNCTTLMIGSKGYEKSICNKGDFK--------DKIEFFPnwvedSLESQKMIDVPKLPKGFNVVIA 225
Cdd:cd03814 130 PLSWLAwaylRWFHNPFDTTLVPSPSIARELEGHGFERvrlwprgvDTELFHP-----SRRDAALRRRLGPPGRPLLLYV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 226 GNMGDAQDLPHIMETARMLKGSN-IRFNFIGDGRKREYVEnyARengLMNNIFC--LGRyplEAMPAFFAQADILFMAlK 302
Cdd:cd03814 205 GRLAPEKNLEALLDADLPLAASPpVRLVVVGDGPARAELE--AR---GPDVIFTgfLTG---EELARAYASADVFVFP-S 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 303 DTPIFALTVpsrLQAyMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLsTLNKDELTQKGANGKEYSRK 382
Cdd:cd03814 276 RTETFGLVV---LEA-MASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRAL-LEDPELRRRMAARARAEAER 350
|
.
gi 1624566921 383 Y 383
Cdd:cd03814 351 Y 351
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
17-200 |
1.81e-07 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 50.48 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 17 VNDMAFELQKRGHDVSVMTaiPDYPEGRFykgygifkkrRESINGVKVHRsLIIPRHSGSSFWLAMnylSYTFFASLKsl 96
Cdd:pfam13579 7 VLELARALAALGHEVRVVT--PGGPPGRP----------ELVGDGVRVHR-LPVPPRPSPLADLAA---LRRLRRLLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 97 wfgiAKKYDAIIVHEPspiLVGIPAVIIKKLQKIP-VHFWVLDLWPESLTAAGGItnkniiypFEKLTKWIYDNCTTLMI 175
Cdd:pfam13579 69 ----AERPDVVHAHSP---TAGLAARLARRRRGVPlVVTVHGLALDYGSGWKRRL--------ARALERRLLRRADAVVV 133
|
170 180
....*....|....*....|....*
gi 1624566921 176 GSKGYEKSICNKGDFKDKIEFFPNW 200
Cdd:pfam13579 134 VSEAEAELLRALGVPAARVVVVPNG 158
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
218-346 |
6.09e-07 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 50.10 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 218 KGFNVVIAGNMGDAQDLPHIMETARMLK--GSNIRFNFIGDGRKREYVENYARENGLM-NNIFCLGRYPLEAMPAFFAQA 294
Cdd:cd01635 109 PLADKVSVGRLVPEKGIDLLLEALALLKarLPDLVLVLVGGGGEREEEEALAAALGLLeRVVIIGGLVDDEVLELLLAAA 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1624566921 295 DILFMALKDTPiFALTVpsrLQAyMSSGKPVVAMINGEGADTIREADCGWSV 346
Cdd:cd01635 189 DVFVLPSRSEG-FGLVL---LEA-MAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
217-383 |
1.82e-06 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 49.71 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 217 PKGFNVVIAGNMG---DAQDLPHIMEtarmlKGSNIRFNFIGDGRKREYVENYAREnglMNNIFcLGRYPLEAMPAFFAQ 293
Cdd:PLN02871 261 PEKPLIVYVGRLGaekNLDFLKRVME-----RLPGARLAFVGDGPYREELEKMFAG---TPTVF-TGMLQGDELSQAYAS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 294 ADIlFMALKDTPIFALTVpsrLQAyMSSGKPVVAMINGEGADTIREADCGWS---VPAGDSEQLANLLKHLSTlNKDELT 370
Cdd:PLN02871 332 GDV-FVMPSESETLGFVV---LEA-MASGVPVVAARAGGIPDIIPPDQEGKTgflYTPGDVDDCVEKLETLLA-DPELRE 405
|
170
....*....|...
gi 1624566921 371 QKGANGKEYSRKY 383
Cdd:PLN02871 406 RMGAAAREEVEKW 418
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
290-385 |
3.49e-06 |
|
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.
Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 48.48 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 290 FFAQADILFM-ALKDTpiFALTVpsrLQAyMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLsTLNKDE 368
Cdd:cd03825 260 IYSAADLFVHpSLADN--LPNTL---LEA-MACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWL-LANPKE 332
|
90
....*....|....*..
gi 1624566921 369 LTQKGANGKEYSRKYYD 385
Cdd:cd03825 333 RESLGERARALAENHFD 349
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
222-396 |
5.34e-06 |
|
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340860 [Multi-domain] Cd Length: 365 Bit Score: 48.22 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 222 VVIAGNMGDAQDLPHIMETARML--KGSNIRFNFIGDGRKREYVENYARENGlmnNIFCLGRYPLEAMPAFFAQADILfm 299
Cdd:cd05844 192 ILFVGRLVEKKGCDVLIEAFRRLaaRHPTARLVIAGDGPLRPALQALAAALG---RVRFLGALPHAEVQDWMRRAEIF-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 300 alkdtpifalTVPSRLQA-------------YMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLstLNK 366
Cdd:cd05844 267 ----------CLPSVTAAsgdseglgivlleAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQAL--LAD 334
|
170 180 190
....*....|....*....|....*....|.
gi 1624566921 367 DELTQK-GANGKEYSRKYYDFTKCINHLEKI 396
Cdd:cd05844 335 RALADRmGGAARAFVCEQFDIRVQTAKLEAI 365
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
245-388 |
7.21e-06 |
|
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.
Pssm-ID: 340829 [Multi-domain] Cd Length: 350 Bit Score: 47.45 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 245 KGSNIRFNFIGDGRKREYVENYARENGLMNNIFCLGRYPLEAMPAFFAQADILF---MALKDTPIFAltVPSRLQAYMSS 321
Cdd:cd03799 202 KYPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIapsVTAADGDQDG--PPNTLKEAMAM 279
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566921 322 GKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLSTlNKDELTQKGANGKEYSRKYYDFTK 388
Cdd:cd03799 280 GLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIE-HPAIWPEMGKAGRARVEEEYDINK 345
|
|
| GT4_TuaH-like |
cd04950 |
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ... |
193-344 |
7.72e-06 |
|
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340856 [Multi-domain] Cd Length: 373 Bit Score: 47.75 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 193 KIEFFPNWVE-----------DSLESQKMIDVPKLpkGFNVVIAGNMgdaqDLPHIMETARMLKGSNirFNFIGDGRKRE 261
Cdd:cd04950 174 NVHPIPNGVDvehfaaarqplDDPIDLREIPGPVL--GFFGAIDEKL----DFDLIEELAKARPQWN--FVFIGPVVKID 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 262 YVEnyarengLMN--NIFCLGRYPLEAMPAFFAQADILFMALKDTPIFALTVPSRLQAYMSSGKPVVAM-IngegADTIR 338
Cdd:cd04950 246 PSS-------LPRapNIHWLGPKPYKELPAYLAGFDVALLPFALNEYTRFISPLKLFEYLAAGKPVVATsI----PSVVR 314
|
....*.
gi 1624566921 339 EADCGW 344
Cdd:cd04950 315 FYGEAV 320
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
159-396 |
1.39e-04 |
|
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340841 [Multi-domain] Cd Length: 474 Bit Score: 43.86 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 159 FEKLTKWIYDNC---TTLMIGSKGYEKSIcnkGDFKDKIEFFPNWVEdsleSQKMIDVPKLPK---GFNVVIAGNMGDAQ 232
Cdd:cd03813 234 FERLGKLAYQQAdkiISLYEGNRRRQIRL---GADPDKTRVIPNGID----IQRFAPAREERPekePPVVGLVGRVVPIK 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 233 DLPHIMETARMLK--GSNIRFNFIG-DGRKREYVEN---YARENGLMNNIFCLGRyplEAMPAFFAQADIlfMALkdTPI 306
Cdd:cd03813 307 DVKTFIRAFKLVRraMPDAEGWLIGpEDEDPEYAQEckrLVASLGLENKVKFLGF---QNIKEYYPKLGL--LVL--TSI 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 307 ---FALTVpsrLQAyMSSGKPVVAMINGEGADTIREAD-----CGWSVPAGDSEQLANLLKHLSTlNKDELTQKGANGKE 378
Cdd:cd03813 380 segQPLVI---LEA-MASGVPVVATDVGSCRELIYGADdalgqAGLVVPPADPEALAEALIKLLR-DPELRQAFGEAGRK 454
|
250
....*....|....*...
gi 1624566921 379 YSRKYYDFTKCINHLEKI 396
Cdd:cd03813 455 RVEKYYTLEGMIDSYRKL 472
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
241-385 |
2.64e-04 |
|
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.
Pssm-ID: 340859 [Multi-domain] Cd Length: 370 Bit Score: 42.72 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 241 ARMLKGSNIRFNFIGDGRKREYVENYARENGLMNNIFCLGRypLEAMPAFFAQADiLFMALKDTPIFALTVpsrLQAyMS 320
Cdd:cd04962 219 ARVRRKIPAKLLLVGDGPERVPAEELARELGVEDRVLFLGK--QDDVEELLSIAD-LFLLPSEKESFGLAA---LEA-MA 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624566921 321 SGKPVVAMINGEGADTIREADCGWSVPAGDSEQLAnllKH-LSTLNKDELTQK-GANGKEYSRKYYD 385
Cdd:cd04962 292 CGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMA---KSaLSILEDDELYNRmGRAARKRAAERFD 355
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
17-141 |
4.33e-04 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 40.59 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 17 VNDMAFELQKRGHDVSVMTaiPDYPEgrfykgygifKKRRESINGVKVHRSLIIPRHSgssfwlamNYLSYTFFASLKSL 96
Cdd:pfam13439 7 VLELARALARRGHEVTVVT--PGGPG----------PLAEEVVRVVRVPRVPLPLPPR--------LLRSLAFLRRLRRL 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1624566921 97 WFgiAKKYDAIIVHEPSPILVGIPAviIKKLQKIPV----HFWVLDLWP 141
Cdd:pfam13439 67 LR--RERPDVVHAHSPFPLGLAALA--ARLRLGIPLvvtyHGLFPDYKR 111
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
225-396 |
4.63e-04 |
|
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.
Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 42.05 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 225 AGNMGDAQDLPHIMETARML--KGSNIRFNFIGDGRKREYVENYARENGLMNNIFCLGrypleampaffAQADIL-FMAL 301
Cdd:cd04951 194 VGRLTEAKDYPNLLLAISELilSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLG-----------QISNISeYYNA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 302 KDtpIFALtvPSRLQAY-------MSSGKPVVAMINGEGADTIREADcgWSVPAGDSEQLANLLKHLSTLNKDELTQKGa 374
Cdd:cd04951 263 AD--LFVL--SSEWEGFglvvaeaMACERPVVATDAGGVAEVVGDHN--YVVPVSDPQLLAEKIKEIFDMSDEERDILG- 335
|
170 180
....*....|....*....|..
gi 1624566921 375 NGKEYSRKYYDFTKCINHLEKI 396
Cdd:cd04951 336 NKNEYIAKNFSINTIVNEWERL 357
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
2-138 |
6.85e-04 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 39.61 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 2 KLLIVTPHFYPENFKVNDmafELQKRGHDVSVMTAIPDYpegrfykgygifkKRRESINGVKVHRsLIIPRHSgssfwlA 81
Cdd:pfam13477 1 KILLLANADSIHTLRWAD---ALADRGYDVHVISSKGPA-------------KDELIAEGIHVHR-LKVPRKG------P 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566921 82 MNYLSYtffASLKSLWFGIakKYDAIIVHEPSP-ILVGIPAVIIKKLQKIPVHFWVLD 138
Cdd:pfam13477 58 LGYLKA---FRLKKLIKKI--KPDVVHVHYAKPyGLLAGLAARLSGFPPVVLSAWGLD 110
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
239-395 |
9.04e-04 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 41.19 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 239 ETARMLKGSNIRFNFI---GDGRKREYVENYARENGLMNNIFCLGRYPLEAMPAFFAQADILfmalkdtpIFaltvPSR- 314
Cdd:cd03809 212 KAFALLKKQGGDLKLVivgGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAF--------VF----PSLy 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 315 -------LQAyMSSGKPVVAmingegADT--IRE--ADCGWSVPAGDSEQLANLLKHLSTlNKDELTQKGANGKEYSRKy 383
Cdd:cd03809 280 egfglpvLEA-MACGTPVIA------SNIsvLPEvaGDAALYFDPLDPESIADAILRLLE-DPSLREELIRKGLERAKK- 350
|
170
....*....|..
gi 1624566921 384 YDFTKCINHLEK 395
Cdd:cd03809 351 FSWEKTAEKTLE 362
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
307-384 |
2.69e-03 |
|
sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.
Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 39.53 E-value: 2.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624566921 307 FALTVpsrLQAyMSSGKPVVAMINGEGADTIREADCGWSVPAGDSEQLANLLKHLstLNKDELTQK-GANGKEYSRKYY 384
Cdd:cd03800 315 FGLTA---IEA-MACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRL--LDDPALWQRlSRAGLERARAHY 387
|
|
| GT4_ALG2-like |
cd03805 |
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ... |
19-109 |
3.29e-03 |
|
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
Pssm-ID: 340834 [Multi-domain] Cd Length: 392 Bit Score: 39.49 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566921 19 DMAFELQKRGHDVSVMTAipDYPEGRFYKgygifkkrrESING-VKVH-RSLIIPRHSGSSFWLAMNYLSyTFFASLKSL 96
Cdd:cd03805 21 DAALALQSRGHEVTIYTS--HHDPSHCFE---------ETKDGtLPVRvRGDWLPRSIFGRFHALCAYLR-MLYLALYLL 88
|
90
....*....|...
gi 1624566921 97 WFGIaKKYDAIIV 109
Cdd:cd03805 89 LFSG-EKYDVFIV 100
|
|
| |
