|
Name |
Accession |
Description |
Interval |
E-value |
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
9-374 |
3.19e-50 |
|
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: 172.72 E-value: 3.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 9 ILHCFRSPVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSLFDDIRPYLSLGLTRVPIRRSISPSDIATMWdtyk 88
Cdd:cd03801 5 LSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 89 kiksLRPDVLHGHGAKGGVLARLAGSalrvnRYRVARLYTAHGGSLHYSRSTFSGQ-FVLRMERLQEYFTDALVFICEYE 167
Cdd:cd03801 81 ----RKFDVVHAHGLLAALLAALLAL-----LLGAPLVVTLHGAEPGRLLLLLAAErRLLARAEALLRRADAVIAVSEAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 168 RDIYARKVGRPRTKTRLIYNGIGERDFEPIPTRS-----DAVHFIYVGMLRDLKGPDLFVDAFAKTERLLGRpLSALMIG 242
Cdd:cd03801 152 RDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKlgippDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPD-VRLVIVG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 243 -DGPDRDRYREMmvERGLGKRIGMLPAM---RVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGA 318
Cdd:cd03801 231 gDGPLRAELEEL--ELGLGDRVRFLGFVpdeELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVED 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1586791992 319 DSAALV-EPGNSDDLARVMAETLSTPDWhARTMPKP--EAVKAVFSSAVMARDVLKLYH 374
Cdd:cd03801 309 GEGGLVvPPDDVEALADALLRLLADPEL-RARLGRAarERVAERFSWERVAERLLDLYR 366
|
|
| GT4_CapM-like |
cd03808 |
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ... |
8-344 |
9.88e-50 |
|
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: 171.24 E-value: 9.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 8 RILHCFRSPvGGIFRHVRDLVEEHSKAGHEIGILCdsstggEYEDSLFDDIRpylSLGLTRVPI---RRSISP-SDIATM 83
Cdd:cd03808 1 KILFIVNVD-GGFQSFRLPLIKALVKKGYEVHVIA------PDGDKLSDELK---ELGVKVIDIpilRRGINPlKDLKAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 84 WDTYKKIKSLRPDVLHGHGAKGGVLARLAGSALRVNRyrvaRLYTAHGGSLHYSRSTFSGQFVLRMERLQEYFTDALVFI 163
Cdd:cd03808 71 FKLYKLLKKEKPDIVHCHTPKPGILGRLAARLAGVPK----VIYTVHGLGFVFTEGKLLRLLYLLLEKLALLFTDKVIFV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 164 CEYERDiYARKVGRPRTKTRLIYNGIG----ERDFEPIPTRSDAVHFIYVG-MLRDlKGPDLFVDAFAKtERLLGRPLSA 238
Cdd:cd03808 147 NEDDRD-LAIKKGIIKKKKTVLIPGSGvdldRFQYSPESLPSEKVVFLFVArLLKD-KGIDELIEAAKI-LKKKGPNVRF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 239 LMIGDGPDRDRYREMMVERGLGKRIGML-PAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPE-VL 316
Cdd:cd03808 224 LLVGDGELENPSEILIEKLGLEGRIEFLgFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRElVI 303
|
330 340
....*....|....*....|....*...
gi 1586791992 317 GADSAALVEPGNSDDLARVMAETLSTPD 344
Cdd:cd03808 304 DGVNGFLVPPGDVEALADAIEKLIEDPE 331
|
|
| GT4_WlbH-like |
cd03798 |
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ... |
7-376 |
7.27e-38 |
|
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: 140.21 E-value: 7.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 7 LRILHCF---RSPVGGIFrhVRDLVEEHSKAGHEIGILC----DSSTGGEYEDSLFDDIRPYLSLGLTRVPIR-RSISPS 78
Cdd:cd03798 2 LILTNIYpnaNSPGRGIF--VRRQVRALSRRGVDVEVLApapwGPAAARLLRKLLGEAVPPRDGRRLLPLKPRlRLLAPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 79 DIATMWDTYKKIKSLRPDVLHGHGAKG-GVLARLAGSalrvnRYRVARLYTAHGGSLHysrsTFSGQFVLRMERLQEYF- 156
Cdd:cd03798 80 RAPSLAKLLKRRRRGPPDLIHAHFAYPaGFAAALLAR-----LYGVPYVVTEHGSDIN----VFPPRSLLRKLLRWALRr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 157 TDALVFICEYERDIyARKVGRPRTKTRLIYNGIGERDFEPIPTR----SDAVHFIYVGMLRDLKGPDLFVDAFAKtERLL 232
Cdd:cd03798 151 AARVIAVSKALAEE-LVALGVPRDRVDVIPNGVDPARFQPEDRGlglpLDAFVILFVGRLIPRKGIDLLLEAFAR-LAKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 233 GRPLSALMIGDGPDRDRYREMMVERGLGKRI---GMLPAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRV 309
Cdd:cd03798 229 RPDVVLLIVGDGPLREALRALAEDLGLGDRVtftGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDV 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586791992 310 GGIPEVLGADSAA-LVEPGNSDDLARVMAETLSTPdWHARTMPKPEA-VKAVFSSAVMARDVLKLYHEL 376
Cdd:cd03798 309 GGIPEVVGDPETGlLVPPGDADALAAALRRALAEP-YLRELGEAARArVAERFSWVKAADRIAAAYRDV 376
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
7-359 |
1.11e-32 |
|
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: 125.55 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 7 LRILHCFRspVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGgEYEDSLFDDIRPYLSLGLTRVPIRRSISpsdiatmwdt 86
Cdd:cd03819 2 LMLTPALE--IGGAETYILDLARALAERGHRVLVVTAGGPL-LPRLRQIGIGLPGLKVPLLRALLGNVRL---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 87 YKKIKSLRPDVLHGHGAKGGVLARLAgsalrVNRYRVARLYTAHGgslHYSRSTFSGQFVLRMErlqeYFTDALVFICEY 166
Cdd:cd03819 69 ARLIRRERIDLIHAHSRAPAWLGWLA-----SRLTGVPLVTTVHG---SYLATYHPKDFALAVR----ARGDRVIAVSEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 167 ERDIYARKVGRPRTKTRLIYNGIGERDFEPIPTR---------SDAVHFIYVGMLRDLKGPDLFVDAFAKTERllGRPLS 237
Cdd:cd03819 137 VRDHLIEALGVDPERIRVIPNGVDTDRFPPEAEAeeraqlglpEGKPVVGYVGRLSPEKGWLLLVDAAAELKD--EPDFR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 238 ALMIGDGPDRDRYREMMVERGLGKRIGML-PAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVL 316
Cdd:cd03819 215 LLVAGDGPERDEIRRLVERLGLRDRVTFTgFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIV 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1586791992 317 GAD-SAALVEPGNSDDLARVMAETLSTPDWHARTMPKPEAVKAV 359
Cdd:cd03819 295 VHGrTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALTEAV 338
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
16-374 |
6.26e-31 |
|
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: 120.88 E-value: 6.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 16 PVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGgEYEDSLFDDIRPYLSLGLTrvpirrsiSPSDIATMWDTYKKIKSLRP 95
Cdd:cd03807 10 NVGGAETMLLRLLEHMDKSRFEHVVISLTGDG-VLGEELLAAGVPVVCLGLS--------SGKDPGVLLRLAKLIRKRNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 96 DVLHGHGAKGGVLARLAGSALRVNRYrvarLYTAHGgSLHYSRSTfsgQFVLRMERLQEYFTDALVFICEYERDIYaRKV 175
Cdd:cd03807 81 DVVHTWMYHADLIGGLAAKLAGGVKV----IWSVRS-SNIPQRLT---RLVRKLCLLLSKFSPATVANSSAVAEFH-QEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 176 GRPRTKTRLIYNGIGERDFEP-----------IPTRSDAVHFIYVGMLRDLKGPDLFVDAFAK-TERllgRP-LSALMIG 242
Cdd:cd03807 152 GYAKNKIVVIYNGIDLFKLSPddasrararrrLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALlVET---HPdLRLLLVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 243 DGPDRDRYREMMVERGLGKRI----------GMLPAMRVHeafsmaqnlVVPSRAEAMPYIVLEGLGAGKTIIASRVGGI 312
Cdd:cd03807 229 RGPERPNLERLLLELGLEDRVhllgersdvpALLPAMDIF---------VLSSRTEGFPNALLEAMACGLPVVATDVGGA 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586791992 313 PEVLGADSAALVEPGNSDDLARVMAETLSTPD-WHARTMPKPEAVKAVFSSAVMARDVLKLYH 374
Cdd:cd03807 300 AELVDDGTGFLVPAGDPQALADAIRALLEDPEkRARLGRAARERIANEFSIDAMVRRYETLYY 362
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
8-343 |
1.17e-29 |
|
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: 117.46 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 8 RILHCFRS-PVGGIFRHVRDLVEEHSKAGHEIGILCDsstggEYEDSLFDDIRPYLSLGLTRVPIRRSISPSDIATMWDT 86
Cdd:cd03811 1 KILFVIPSlSGGGAERVLLNLANALDKRGYDVTLVLL-----RDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 87 YKKIKSLRPDVLHGHGAKGGVLARLagsalrVNRYRVARLYTAHGgslHYSRSTFSGQFVLRmERLQEYFTDALVFICEY 166
Cdd:cd03811 76 KRILKRAKPDVVISFLGFATYIVAK------LAAARSKVIAWIHS---SLSKLYYLKKKLLL-KLKLYKKADKIVCVSKG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 167 ERDIYARKVGRPRTKTRLIYNGIgerDFEPIPTRSDAVH---------FIYVGMLRDLKGPDLFVDAFAK-TERLLGRPL 236
Cdd:cd03811 146 IKEDLIRLGPSPPEKIEVIYNPI---DIDRIRALAKEPIlnepedgpvILAVGRLDPQKGHDLLIEAFAKlRKKYPDVKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 237 saLMIGDGPDRDRYREMMVERGLGKRIGML-------PAMRVheafsmAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRV 309
Cdd:cd03811 223 --VILGDGPLREELEKLAKELGLAERVIFLgfqsnpyPYLKK------ADLFVLSSRYEGFPNVLLEAMALGTPVVSTDC 294
|
330 340 350
....*....|....*....|....*....|....
gi 1586791992 310 GGIPEVLGADSAALVEPGNSDDLARVMAETLSTP 343
Cdd:cd03811 295 PGPREILDDGENGLLVPDGDAAALAGILAALLQK 328
|
|
| GT4_ExpE7-like |
cd03823 |
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ... |
8-373 |
3.93e-24 |
|
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: 102.02 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 8 RIL---HCFRSP-VGGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDslfdDIRPYLSLGLTRVPIRRSISPSDIATM 83
Cdd:cd03823 1 KILlvnSLYPPQrVGGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQAT----VARSVVRYRRAPDETLPLALKRRGYEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 84 WDTYKK---------IKSLRPDVLHGHGakggvLARLAGSALRVNRYRVARlyTAHggSLH--YSRSTFSGQFVLRmerl 152
Cdd:cd03823 77 FETYNPglrrllarlLEDFRPDVVHTHN-----LSGLGASLLDAARDLGIP--VVH--TLHdyWLLCPRQFLFKKG---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 153 qeyfTDALVFICEYERDIYaRKVGRPRTKTRLIYNGI-GERDFEPIPTRSDA-VHFIYVGMLRDLKGPDLFVDAFaktER 230
Cdd:cd03823 144 ----GDAVLAPSRFTANLH-EANGLFSARISVIPNAVePDLAPPPRRRPGTErLRFGYIGRLTEEKGIDLLVEAF---KR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 231 LLGRPLSALMIGDGPDRDrYREMMVERGLgKRIGMLPAMRVHEAFSMAQNLVVPSR-AEAMPYIVLEGLGAGKTIIASRV 309
Cdd:cd03823 216 LPREDIELVIAGHGPLSD-ERQIEGGRRI-AFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586791992 310 GGIPEVLGAD-SAALVEPGNSDDLARVMAETLSTPDWHARtmpKPEAVKAVFSSAVMARDVLKLY 373
Cdd:cd03823 294 GGIAELIQPGvNGLLFAPGDAEDLAAAMRRLLTDPALLER---LRAGAEPPRSTESQAEEYLKLY 355
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
206-355 |
1.89e-22 |
|
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: 92.72 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 206 FIYVGMLRDLKGPDLFVDAFAKTERLlGRPLSALMIGDGPDRDRYREMMVERGLGKRIGMLPAM---RVHEAFSMAQNLV 282
Cdd:pfam00534 5 ILFVGRLEPEKGLDLLIKAFALLKEK-NPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVsdeDLPELLKIADVFV 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586791992 283 VPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLG-ADSAALVEPGNSDDLARVMAETLStpDWHARTMPKPEA 355
Cdd:pfam00534 84 LPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKdGETGFLVKPNNAEALAEAIDKLLE--DEELRERLGENA 155
|
|
| GT4-like |
cd05844 |
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ... |
93-350 |
3.76e-22 |
|
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: 96.37 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 93 LRPDVLHGHGAKGGVLARLAGSALRVnryrvARLYTAHGGSLHYSRSTFSG------QFVLRMERLQEYftdALVFIC-- 164
Cdd:cd05844 80 LAPALVHAHFGRDGVYALPLARALGV-----PLVVTFHGFDITTSRAWLAAspgwpsQFQRHRRALQRP---AALFVAvs 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 165 EYERDiYARKVGRPRTKTRLIYNGIGERDFEPIPTRSDAVHFIYVGMLRDLKGPDLFVDAFAkteRLLGRPLSA--LMIG 242
Cdd:cd05844 152 GFIRD-RLLARGLPAERIHVHYIGIDPAKFAPRDPAERAPTILFVGRLVEKKGCDVLIEAFR---RLAARHPTArlVIAG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 243 DGPDRDRYREMMVERGLGKRIGMLPAMRVHEAFSMAQNLVVPS------RAEAMPYIVLEGLGAGKTIIASRVGGIPE-V 315
Cdd:cd05844 228 DGPLRPALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEaI 307
|
250 260 270
....*....|....*....|....*....|....*
gi 1586791992 316 LGADSAALVEPGNSDDLARVMaETLSTPDWHARTM 350
Cdd:cd05844 308 LDGETGFLVPEGDVDALADAL-QALLADRALADRM 341
|
|
| Glyco_transf_4 |
pfam13439 |
Glycosyltransferase Family 4; |
18-189 |
4.04e-20 |
|
Glycosyltransferase Family 4;
Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 86.43 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 18 GGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSLFDDIRPYLSLGLTRVPIRrsispsDIATMWDTYKKIKSLRPDV 97
Cdd:pfam13439 1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLR------SLAFLRRLRRLLRRERPDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 98 LHGHGAKGGVLARLAGSAlrvnRYRVARLYTAHGGSLHYSRSTFSGQFVLRMERLQEYF----TDALVFICEYERDIYAR 173
Cdd:pfam13439 75 VHAHSPFPLGLAALAARL----RLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRllrrADRVIAVSEAVADELRR 150
|
170
....*....|....*.
gi 1586791992 174 KVGRPRTKTRLIYNGI 189
Cdd:pfam13439 151 LYGVPPEKIRVIPNGV 166
|
|
| Glyco_trans_1_4 |
pfam13692 |
Glycosyl transferases group 1; |
206-341 |
3.72e-19 |
|
Glycosyl transferases group 1;
Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 82.94 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 206 FIYVG-MLRDLKGPDLFVDAFAkteRLLGRPLSA--LMIGDGPDRdRYREMmvERGLGKRI---GMLPAMRvhEAFSMAQ 279
Cdd:pfam13692 4 ILFVGrLHPNVKGVDYLLEAVP---LLRKRDNDVrlVIVGDGPEE-ELEEL--AAGLEDRViftGFVEDLA--ELLAAAD 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1586791992 280 NLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGADSAALVEPGNSDDLARVMAETLS 341
Cdd:pfam13692 76 VFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVPPGDPEALAEAILRLLE 137
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
13-345 |
2.78e-17 |
|
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: 82.41 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 13 FRSPVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSLFDDIRpyLSLGLTRVPIRRSISPSDiatmWDTYKKIKS 92
Cdd:cd03809 9 LAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPE--LSLGVIKIKLWRELALLR----WLQILLPKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 93 LRPDVLHGHGakggvlarlagSALRVNRYRVARLYTAHGGSLHYSRSTFSGQFVLRMERLQEY---FTDALVFICEYERD 169
Cdd:cd03809 83 DKPDLLHSPH-----------NTAPLLLKGCPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPIslrRADAIITVSEATRD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 170 IYARKVGRPRTKTRLIYNGIGERDFEPIPTRSDAVH-------FIYVGMLRDLKGPDLFVDAFAKTeRLLGRPLSALMIG 242
Cdd:cd03809 152 DIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKyllpepyFLYVGTLEPRKNHERLLKAFALL-KKQGGDLKLVIVG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 243 -DGPDRDRYREMMVERGLGKRI---GMLPAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGa 318
Cdd:cd03809 231 gKGWEDEELLDLVKKLGLGGRVrflGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAG- 309
|
330 340
....*....|....*....|....*..
gi 1586791992 319 DSAALVEPGNSDDLARVMAETLSTPDW 345
Cdd:cd03809 310 DAALYFDPLDPESIADAILRLLEDPSL 336
|
|
| GT4_WbdM_like |
cd04951 |
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ... |
17-340 |
8.11e-17 |
|
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: 80.95 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 17 VGGIFRHVRDLVEEHSKAGHEIGILCdsSTGGEYEDSLFDDIRPYlSLGLTRVPIrrsispSDIATMWDTYKKIKSLRPD 96
Cdd:cd04951 11 LGGAEKQTVLLADQMFIRGHDVNIVY--LTGEVEVKPLNNNIIIY-NLGMDKNPR------SLLKALLKLKKIISAFKPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 97 VLHGHGAKGGVLARLagsaLRVNRYRVARLYTAHGGSLhysrstfSGQFVLRMERLQEYFTDALVFICEYERDIYARKVG 176
Cdd:cd04951 82 VVHSHMFHANIFARF----LRMLYPIPLLICTAHNKNE-------GGRIRMFIYRLTDFLCDITTNVSREALDEFIAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 177 RPRTKTRLIYNGIGERDFEPIPTRSDAVH-----------FIYVGMLRDLKGPDLFVDAFAKTERLLGRpLSALMIGDGP 245
Cdd:cd04951 151 FSKNKSVPVYNGIDLNKFKKDINVRLKIRnklnlkndefvILNVGRLTEAKDYPNLLLAISELILSKND-FKLLIAGDGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 246 DRDRYREMMVERGLGKRIGMLPAM-RVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGaDSAALV 324
Cdd:cd04951 230 LRNELERLICNLNLVDRVILLGQIsNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVG-DHNYVV 308
|
330
....*....|....*.
gi 1586791992 325 EPGNSDDLARVMAETL 340
Cdd:cd04951 309 PVSDPQLLAEKIKEIF 324
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
15-344 |
3.48e-16 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 78.82 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 15 SPVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSLFDDIRpYLSLGLTRVpirrsispSDIATMWDTYKKIKSLR 94
Cdd:cd03820 10 SNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIK-IKNLGDRKY--------SHFKLLLKYFKKVRRLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 95 -------PDVLHGHGakGGVLARLAGSALRVNRYrvarlytahgGSLHYSRSTFSGQFVLRMERLQEYFTdALVFICEYE 167
Cdd:cd03820 81 kylknnkPDVVISFR--TSLLTFLALIGLKSKLI----------VWEHNNYEAYNKGLRRLLLRRLLYKR-ADKIVVLTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 168 RDIYARKVgRPRTKTRLIYNGIGERDFEPIPTRSDAVhFIYVGMLRDLKGPDLFVDAFAK-TERLLGRPLsaLMIGDGPD 246
Cdd:cd03820 148 ADKLKKYK-QPNSNVVVIPNPLSFPSEEPSTNLKSKR-ILAVGRLTYQKGFDLLIEAWALiAKKHPDWKL--RIYGDGPE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 247 RDRYREMMVERGLGKRIGMLPAMR-VHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIAS-RVGGIPE-VLGADSAAL 323
Cdd:cd03820 224 REELEKLIDKLGLEDRVKLLGPTKnIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFdCPTGPSEiIEDGENGLL 303
|
330 340
....*....|....*....|.
gi 1586791992 324 VEPGNSDDLARVMAETLSTPD 344
Cdd:cd03820 304 VPNGDVDALAEALLRLMEDEE 324
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
271-378 |
5.95e-16 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 73.49 E-value: 5.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 271 VHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLG-ADSAALVEPGNSDDLARVMAETLSTPDwHART 349
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdGETGLLVPPGDPEALAEAILRLLEDPE-LRRR 92
|
90 100 110
....*....|....*....|....*....|.
gi 1586791992 350 MPK--PEAVKAVFSSAVMARDVLKLYHELVN 378
Cdd:COG0438 93 LGEaaRERAEERFSWEAIAERLLALYEELLA 123
|
|
| GT4_UGDG-like |
cd03817 |
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ... |
12-376 |
8.42e-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: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 12 CFRSPVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSlfDDIRPYLSlGLTRVPIRRSIspsdIATMWDTY-KKI 90
Cdd:cd03817 8 TYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEE--VVRYRSFS-IPIRKYHRQHI----PFPFKKAViDRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 91 KSLRPDVLHGHG--AKGGVLARLAGsalrvnRYRVARLYTAHggsLHYSRST--FSGQF------VLRMERLQEYFTDAL 160
Cdd:cd03817 81 KELGPDIIHTHTpfSLGKLGLRIAR------KLKIPIVHTYH---TMYEDYLhyIPKGKllvkavVRKLVRRFYNHTDAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 161 VFICEYERDiYARKVGRPRTKtRLIYNGIGERDFEPIPT---------RSDAVHFIYVGMLRDLKGPDLFVDAFAKterL 231
Cdd:cd03817 152 IAPSEKIKD-TLREYGVKGPI-EVIPNGIDLDKFEKPLNteerrklglPPDEPILLYVGRLAKEKNIDFLLRAFAE---L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 232 LGRPLSALMI-GDGPDRDRYREMMVERGLGKRI---GMLPAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIAS 307
Cdd:cd03817 227 KKEPNIKLVIvGDGPEREELKELARELGLADKViftGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAA 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586791992 308 RVGGIPEVLGADSAALVEPGNSDDLARVMAETLSTPDwhARTMPKPEAVKAVFSSAVmARDVLKLYHEL 376
Cdd:cd03817 307 KDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLE--LLRKLSKNAEISAREFAF-AKSVEKLYEEV 372
|
|
| GT4_BshA-like |
cd04962 |
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ... |
178-348 |
1.16e-15 |
|
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: 77.78 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 178 PRTKTRLIYNGIGERDFEPIPTRSDAVHF---------IYVGMLRDLKGPDLFVDAFAKTERllGRPLSALMIGDGPDRD 248
Cdd:cd04962 162 VDKDIEVIHNFIDEDVFKRKPAGALKRRLlappdekvvIHVSNFRPVKRIDDVVRVFARVRR--KIPAKLLLVGDGPERV 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 249 RYREMMVERGLGKRIGMLPAM-RVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLG-ADSAALVEP 326
Cdd:cd04962 240 PAEELARELGVEDRVLFLGKQdDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKhGETGFLSDV 319
|
170 180
....*....|....*....|..
gi 1586791992 327 GNSDDLARVMAETLSTPDWHAR 348
Cdd:cd04962 320 GDVDAMAKSALSILEDDELYNR 341
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
18-188 |
1.41e-15 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 73.59 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 18 GGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEdslfddiRPYLSLGLTRVPIRRSISPS-DIATMWDTYKKIKSLRPD 96
Cdd:pfam13579 1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPE-------LVGDGVRVHRLPVPPRPSPLaDLAALRRLRRLLRAERPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 97 VLHGHGAKGGVLARLAGSalrvnRYRVARLYTAHGGSLHYSrSTFSGQFVLRMERLQEYFTDALVFICEYERDIYARKvG 176
Cdd:pfam13579 74 VVHAHSPTAGLAARLARR-----RRGVPLVVTVHGLALDYG-SGWKRRLARALERRLLRRADAVVVVSEAEAELLRAL-G 146
|
170
....*....|..
gi 1586791992 177 RPRTKTRLIYNG 188
Cdd:pfam13579 147 VPAARVVVVPNG 158
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
94-345 |
8.79e-15 |
|
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: 75.35 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 94 RPDVLHGHGAKGGvlarLAGSALRvNRYRVARLYTAHG-GSLHYSRSTFSGQFVLrMERLQ-EYF----TDALVFICEYE 167
Cdd:cd03800 101 RYDLIHSHYWDSG----LVGALLA-RRLGVPLVHTFHSlGRVKYRHLGAQDTYHP-SLRITaEEQileaADRVIASTPQE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 168 RDIYARKVGRPRTKTRLIYNGIGERDFEPIPtRSDAVHF-----------IYVGMLRDLKGPDLFVDAFAKTERLlgRPL 236
Cdd:cd03800 175 ADELISLYGADPSRINVVPPGVDLERFFPVD-RAEARRArlllppdkpvvLALGRLDPRKGIDTLVRAFAQLPEL--REL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 237 SALMIGDGPDRD-------RYREMMVERGLGKRIGMLPAMR---VHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIA 306
Cdd:cd03800 252 ANLVLVGGPSDDplsmdreELAELAEELGLIDRVRFPGRVSrddLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVA 331
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1586791992 307 SRVGGIPEVLgAD--SAALVEPGNSDDLARVMAETLSTPDW 345
Cdd:cd03800 332 TAVGGLQDIV-RDgrTGLLVDPHDPEALAAALRRLLDDPAL 371
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
7-316 |
4.21e-14 |
|
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: 71.28 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 7 LRILHCFRSPVGGIFRHVRDLVEEHSKAGHEIGILCdsstggeyedslfddirpylslgLTRVPIRRSIspsdiatmwdt 86
Cdd:cd01635 2 LLVTGEYPPLRGGLELHVRALARALAALGHEVTVLA-----------------------LLLLALRRIL----------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 87 yKKIKSLRPDVLHGHGAKGGVLARLagsaLRVNRYRVARLYTAHGGSLHYSRstfsgqfvlrmerLQEYFTDALVFICEY 166
Cdd:cd01635 48 -KKLLELKPDVVHAHSPHAAALAAL----LAARLLGIPIVVTVHGPDSLEST-------------RSELLALARLLVSLP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 167 ERDiyarkvgrprtktrliyngigerdfepiptrsdavhFIYVGMLRDLKGPDLFVDAFAKtERLLGRPLSALMIGDGPD 246
Cdd:cd01635 110 LAD------------------------------------KVSVGRLVPEKGIDLLLEALAL-LKARLPDLVLVLVGGGGE 152
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586791992 247 RDRYREMMVERGLGKRIGMLPAMRVHEAFSMAQN----LVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVL 316
Cdd:cd01635 153 REEEEALAAALGLLERVVIIGGLVDDEVLELLLAaadvFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
9-370 |
6.43e-14 |
|
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: 72.37 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 9 ILHCFRSP-VGGIFRHVRDLVEEHSKAGHEIGILCdsSTGGEYEDSLFDDIRPYLsLGLT--RVPIRRSISPSDIATMWD 85
Cdd:cd03794 4 LISQYYPPpKGAAAARVYELAKELVRRGHEVTVLT--PSPNYPLGRIFAGATETK-DGIRviRVKLGPIKKNGLIRRLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 86 -------TYKKI--KSLRPDVLHGH------GAKGGVLARLAGSALRVNryrVARLYTAHGGSLHYSRSTFSGQFVLRME 150
Cdd:cd03794 81 ylsfalaALLKLlvREERPDVIIAYsppitlGLAALLLKKLRGAPFILD---VRDLWPESLIALGVLKKGSLLKLLKKLE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 151 RLQeYFT-DALVFICEYERDIYARKvGRPRTKTRLIYNGIGERDFEPIPTRSDAVH--------FIYVGMLRDLKGPDLF 221
Cdd:cd03794 158 RKL-YRLaDAIIVLSPGLKEYLLRK-GVPKEKIIVIPNWADLEEFKPPPKDELRKKlglddkfvVVYAGNIGKAQGLETL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 222 VDAFAKTERLLGRPLsaLMIGDGPDRDRYREMMVERGLGKR--IGMLPAMRVHEAFSMAQNLVVPSRAEAMPYIV----- 294
Cdd:cd03794 236 LEAAERLKRRPDIRF--LFVGDGDEKERLKELAKARGLDNVtfLGRVPKEEVPELLSAADVGLVPLKDNPANRGSspskl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 295 LEGLGAGKTIIASRVGGIPE-VLGADSAALVEPGNSDDLARVMAETLSTPDW------HARtmpkpEAVKAVFSSAVMAR 367
Cdd:cd03794 314 FEYMAAGKPILASDDGGSDLaVEINGCGLVVEPGDPEALADAILELLDDPELrramgeNGR-----ELAEEKFSREKLAD 388
|
...
gi 1586791992 368 DVL 370
Cdd:cd03794 389 RLL 391
|
|
| GT4_WcaC-like |
cd03825 |
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ... |
270-376 |
7.12e-14 |
|
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: 72.36 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 270 RVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGADSAA-LVEPGNSDDLARVMAETLSTPDW--- 345
Cdd:cd03825 256 QLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGyLVPPGDVQALAEAIEWLLANPKEres 335
|
90 100 110
....*....|....*....|....*....|....
gi 1586791992 346 ---HARtmpkpEAVKAVFSSAVMARDVLKLYHEL 376
Cdd:cd03825 336 lgeRAR-----ALAENHFDQRVQAQRYLELYKDL 364
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
8-343 |
1.06e-12 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 68.55 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 8 RILHCFRSPV---GGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSLFDDIRP----YLSLGLTRVPIRRSISPSDI 80
Cdd:cd03821 1 KILHVTPSISpkaGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPpqdgFASIPLLRQGAGRTDFSPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 81 ATMwdtyKKIKSLRPDVLHGHGAKGGVLARLAGSALRVNRYRVARlytAHGGSLHYSRS-TFSGQFVLRMerLQEYF--- 156
Cdd:cd03821 81 PNW----LRRNLREYDVVHIHGVWTYTSLAACKLARRRGIPYVVS---PHGMLDPWALQqKHWKKRIALH--LIERRnln 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 157 -TDALVFICEYERDIYARKVgrPRTKTRLIYNGIGERDFEP-------IPTRSDAVHFIYVGMLRDLKGPDLFVDAFAKt 228
Cdd:cd03821 152 nAALVHFTSEQEADELRRFG--LEPPIAVIPNGVDIPEFDPglrdrrkHNGLEDRRIILFLGRIHPKKGLDLLIRAARK- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 229 erLLGRPLSALMIGDGPDRDRY---REMMVERGLGKRI---GMLPAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGK 302
Cdd:cd03821 229 --LAEQGRDWHLVIAGPDDGAYpafLQLQSSLGLGDRVtftGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1586791992 303 TIIASRVGGIPEVLGADSAALVEPgNSDDLARVMAETLSTP 343
Cdd:cd03821 307 PVVITDKCGLSELVEAGCGVVVDP-NVSSLAEALAEALRDP 346
|
|
| GT4-like |
cd03813 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
165-373 |
1.19e-12 |
|
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: 68.90 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 165 EYERdIYARKVGRPRTKTRLIYNGIGERDFEPIP-TRSDAVHFIYVGMLR-----DLKgpdLFVDAFaKTERLLGRPLSA 238
Cdd:cd03813 253 EGNR-RRQIRLGADPDKTRVIPNGIDIQRFAPAReERPEKEPPVVGLVGRvvpikDVK---TFIRAF-KLVRRAMPDAEG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 239 LMIGDGPDRDRY----REMMVERGLGKRIGMLPAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPE 314
Cdd:cd03813 328 WLIGPEDEDPEYaqecKRLVASLGLENKVKFLGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRE 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586791992 315 VLGADSAAL------VEPGNSDDLARVMAETLSTPD-WHArtmpkpeavkavFSSAVMARdVLKLY 373
Cdd:cd03813 408 LIYGADDALgqaglvVPPADPEALAEALIKLLRDPElRQA------------FGEAGRKR-VEKYY 460
|
|
| GT4_PIG-A-like |
cd03796 |
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ... |
17-379 |
8.71e-11 |
|
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.
Pssm-ID: 340827 [Multi-domain] Cd Length: 398 Bit Score: 63.03 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 17 VGGIFRHVRDLVEEHSKAGHEIgILCDSSTGGEYedslfdDIRpYLSLGLT--RVPIRRSISPSDIATMWDTYKKIKSL- 93
Cdd:cd03796 13 LGGVETHIYQLSQCLIKRGHKV-IVITHAYGNRV------GVR-YLTNGLKvyYLPFKVFYNQSTLPTLFSTFPLLRNIl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 94 ---RPDVLHGHGAkggvLARLAGSALRVNR---YRVarLYTAHggSLhYSRSTFSGQFVLRMERLQEYFTDALVFICEYE 167
Cdd:cd03796 85 ireRIQIVHGHQA----FSSLAHEALFHARtlgLKT--VFTDH--SL-FGFADASSILTNKLLRFSLADIDHVICVSHTS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 168 RDIYARKVGRPRTKTRLIYNGIGERDFEPIPTR--SDAVHFIYVGMLRDLKGPDLFVDAFAKTERLLgRPLSALMIGDGP 245
Cdd:cd03796 156 KENTVLRASLDPRIVSVIPNAVDSSDFTPDPSKpdPNKITIVVISRLVYRKGIDLLVGIIPRICKKH-PNVRFIIGGDGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 246 DRDRYREMMVERGLGKR---IGMLPAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGADSAA 322
Cdd:cd03796 235 KRIELEEMREKYQLQDRvelLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLPPDMIL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586791992 323 LVEPGNSDDLARVM-------AETLSTPDWHartmpkpEAVKAVFSSAVMARDVLKLYHELVNP 379
Cdd:cd03796 315 LAEPDPEDIVRKLEeaisilrTGKHDPWSFH-------NRVKKMYSWEDVARRTEKVYDRILST 371
|
|
| GT4_WfcD-like |
cd03795 |
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ... |
8-344 |
9.17e-11 |
|
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar 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 and eukaryotes.
Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 62.68 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 8 RILHCFRS---PVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSLFDD--IRPYLSLGLTRVPIrrsiSPSDIAT 82
Cdd:cd03795 1 KVLHVFKFyypDIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIriHRVKSFLNVASTPF----SPSYIKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 83 MWDTYKKikslrPDVLHGHGAKGgvLARLAGSALRVNRYRVarlytahggsLHYsRSTFSGQFVLRM--ERLQEYF-TDA 159
Cdd:cd03795 77 FKKLAKE-----YDIIHYHFPNP--LADLLLFFSGAKKPVV----------VHW-HSDIVKQKKLLKlyKPLMTRFlRRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 160 LVFICEyeRDIYARK---VGRPRTKTRLIYNGIGERDFePIPTRSDAVH---------FIYVGMLRDLKGPDLFVDAfak 227
Cdd:cd03795 139 DRIIAT--SPNYVETsptLREFKNKVRVIPLGIDKNVY-NIPRVDFENIkrekkgkkiFLFIGRLVYYKGLDYLIEA--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 228 tERLLGRPLsaLMIGDGPDRDrYREMMVERGLGKRIGMLPamRVHEA-----FSMAQNLVVPS--RAEAMPYIVLEGLGA 300
Cdd:cd03795 213 -AQYLNYPI--VIGGEGPLKP-DLEAQIELNLLDNVKFLG--RVDDEekviyLHLCDVFVFPSvlRSEAFGIVLLEAMMC 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1586791992 301 GKTIIASRV--GGIPEVLGADSAALVEPGNSDDLARVMAETLSTPD 344
Cdd:cd03795 287 GKPVISTNIgtGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEE 332
|
|
| Glyco_trans_4_2 |
pfam13477 |
Glycosyl transferase 4-like; |
12-164 |
1.81e-10 |
|
Glycosyl transferase 4-like;
Pssm-ID: 433241 [Multi-domain] Cd Length: 139 Bit Score: 58.49 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 12 CFRSPVGGIfrHVRDLVEEHSKAGHEIGILCdsSTGGEYEDSLFDDIRPYlslgltRVPIRRSISPSDIAtMWDTYKKIK 91
Cdd:pfam13477 3 LLLANADSI--HTLRWADALADRGYDVHVIS--SKGPAKDELIAEGIHVH------RLKVPRKGPLGYLK-AFRLKKLIK 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586791992 92 SLRPDVLHGHGAKG-GVLARLAGSALRVNRYrvarLYTAHGgsLHYSRSTFSGQFVLRMERLQEYFTDALVFIC 164
Cdd:pfam13477 72 KIKPDVVHVHYAKPyGLLAGLAARLSGFPPV----VLSAWG--LDVYKFPNKSRLKKLLLKLNLKKATLIISTS 139
|
|
| GT4_CapH-like |
cd03812 |
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ... |
8-310 |
2.91e-10 |
|
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).
Pssm-ID: 340840 [Multi-domain] Cd Length: 357 Bit Score: 61.15 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 8 RILHCF-RSPVGGIFRHVRDLVEEHSKAGHEIGILCDSSTGGEYEDSLfddirpyLSLGLTRV-PIRRSISPsdIATMWD 85
Cdd:cd03812 1 KILHIVgGMNVGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEEL-------EELGGKIFyIPPKKKNI--IKYFIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 86 TYKKIKSLRPDVLHGHGAKGGVLARLAgSALRVNRYRVARLYTAHGGSLHYSRStfsgqFVLRMERLQEYFTDALvFICE 165
Cdd:cd03812 72 LLKLIKKEKYDIVHVHGSSSNGIILLL-AAKAGVPVRIAHSHNTKDSSIKLRKI-----RKNVLKKLIERLSTKY-LACS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 166 YERDIYARKVGRPRtKTRLIYNGIGERDFEPIPTR----------SDAVHFIYVGMLRDLKGPDLFVDAFAKterLLGRP 235
Cdd:cd03812 145 EDAGEWLFGEVENG-KFKVIPNGIDIEKYKFNKEKrrkrrkllilEDKLVLGHVGRFNEQKNHSFLIDIFEE---LKKKN 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586791992 236 LSA--LMIGDGPDRDRYREMMVERGLGKRIGMLPAM-RVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAG-KTIIASRVG 310
Cdd:cd03812 221 PNVklVLVGEGELKEKIKEKVKELGLEDKVIFLGFRnDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGlPCLLSDTIT 299
|
|
| GT4-like |
cd03814 |
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ... |
17-348 |
4.63e-10 |
|
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: 60.39 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 17 VGGIFRHVRDLVEEHSKAGHEIGILcdSSTGGEYEDSLFDDIRPYLSLGLTRVP-IRRSISPsdiatMWDTYKKIKSLRP 95
Cdd:cd03814 13 VNGVVRTLERLVDHLRRRGHEVRVV--APGPFDEAESAEGRVVSVPSFPLPFYPeYRLALPL-----PRRVRRLIKEFQP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 96 DVLHghgakggvLA---RLAGSALRVNRyrvaRLYTAHGGSLH-----YSRSTFSGQFVLRMERLQEYFTDALVFICEYE 167
Cdd:cd03814 86 DIIH--------IAtpgPLGLAALRAAR----RLGLPVVTSYHtdfpeYLSYYTLGPLSWLAWAYLRWFHNPFDTTLVPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 168 RDIYARKVGRPRTKTRLIYNGI-------GERDFEPIPTRS--DAVHFIYVGMLRDLKGPDLFVDAFAKTERLlgRPLSA 238
Cdd:cd03814 154 PSIARELEGHGFERVRLWPRGVdtelfhpSRRDAALRRRLGppGRPLLLYVGRLAPEKNLEALLDADLPLAAS--PPVRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 239 LMIGDGPDRDRYREMMVERGLgkrIGMLPAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGA 318
Cdd:cd03814 232 VVVGDGPARAELEARGPDVIF---TGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRP 308
|
330 340 350
....*....|....*....|....*....|.
gi 1586791992 319 D-SAALVEPGNSDDLARVMAETLSTPDWHAR 348
Cdd:cd03814 309 GgTGALVEPGDAAAFAAALRALLEDPELRRR 339
|
|
| GT4_WbaZ-like |
cd03804 |
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ... |
168-315 |
2.85e-09 |
|
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.
Pssm-ID: 340833 [Multi-domain] Cd Length: 356 Bit Score: 58.07 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 168 RDIYARKvgrprtkTRLIYNGIGERDFEPIPTRSDavHFIYVGMLRDLKGPDLFVDAFAKterlLGRPLsaLMIGDGPDR 247
Cdd:cd03804 173 KKFYGRE-------STVIYPPVDTDAFAPAADKED--YYLTASRLVPYKRIDLAVEAFNE----LPKRL--VVIGDGPDL 237
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586791992 248 DRYREMmvergLGKRI---GMLPAMRVHEAFSMAQNLVVPSRaEAMPYIVLEGLGAGKTIIASRVGGIPEV 315
Cdd:cd03804 238 DRLRAM-----ASPNVeflGYQPDEVLKELLSKARAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALET 302
|
|
| PLN02871 |
PLN02871 |
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase |
207-348 |
8.93e-09 |
|
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
Pssm-ID: 215469 [Multi-domain] Cd Length: 465 Bit Score: 57.03 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 207 IYVGMLRDLKGPDLFVDAFaktERLLGRPLSalMIGDGPDRDRYREMMVerglGKRI---GMLPAMRVHEAFSMAQNLVV 283
Cdd:PLN02871 267 VYVGRLGAEKNLDFLKRVM---ERLPGARLA--FVGDGPYREELEKMFA----GTPTvftGMLQGDELSQAYASGDVFVM 337
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586791992 284 PSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGADSAA----LVEPGNSDDLARVMAETLSTPDWHAR 348
Cdd:PLN02871 338 PSESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDQEGktgfLYTPGDVDDCVEKLETLLADPELRER 406
|
|
| GT4_AviGT4-like |
cd03802 |
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ... |
185-373 |
1.36e-08 |
|
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.
Pssm-ID: 340832 [Multi-domain] Cd Length: 333 Bit Score: 55.76 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 185 IYNGIGERDFEPIPTRSDAVHFiyVGMLRDLKGPDLFVDAFAKterlLGRPLsaLMIGDGPDRDRYReMMVERGLGKRI- 263
Cdd:cd03802 153 VHNGLDPADYRFQPDPEDYLAF--LGRIAPEKGLEDAIRVARR----AGLPL--KIAGKVRDEDYFY-YLQEPLPGPRIe 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 264 --GMLPAMRVHEAFSMAQNLVVPSR-AEAMPYIVLEGLGAGKTIIASRVGGIPEVLGADSAA-LVEPGnsDDLARVMAET 339
Cdd:cd03802 224 fiGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGfLVDSV--EEMAEAIANI 301
|
170 180 190
....*....|....*....|....*....|....
gi 1586791992 340 LSTPDWHARtmpkpEAVKAVFSSAVMARDVLKLY 373
Cdd:cd03802 302 DRIDRAACR-----RYAEDRFSAARMADRYEALY 330
|
|
| PRK15484 |
PRK15484 |
lipopolysaccharide N-acetylglucosaminyltransferase; |
165-347 |
5.70e-08 |
|
lipopolysaccharide N-acetylglucosaminyltransferase;
Pssm-ID: 185381 [Multi-domain] Cd Length: 380 Bit Score: 54.03 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 165 EYERDIYARKVgrPRTKTRLIYNGIG----ERDFEPIPTR-----SDAVHFIYVGMLRDLKGPDLFVDAFAKTERLlGRP 235
Cdd:PRK15484 148 QFLKKFYEERL--PNADISIVPNGFCletyQSNPQPNLRQqlnisPDETVLLYAGRISPDKGILLLMQAFEKLATA-HSN 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 236 LSALMIGD-----GPDRDRYREMMVErgLGKRIG----ML---PAMRVHEAFSMAQNLVVPSR-AEAMPYIVLEGLGAGK 302
Cdd:PRK15484 225 LKLVVVGDptassKGEKAAYQKKVLE--AAKRIGdrciMLggqPPEKMHNYYPLADLVVVPSQvEEAFCMVAVEAMAAGK 302
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1586791992 303 TIIASRVGGIPEVL--GADSAALVEPGNSDDLARVMAETLSTPDWHA 347
Cdd:PRK15484 303 PVLASTKGGITEFVleGITGYHLAEPMTSDSIISDINRTLADPELTQ 349
|
|
| GT4_AmsK-like |
cd03799 |
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ... |
158-376 |
3.43e-04 |
|
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: 42.44 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 158 DALVFICEYERDiYARKVGRPRTKTRLIYNGIGERDFePIPTRSDA----VHFIYVGMLRDLKGPDLFVDAFAKTERLLG 233
Cdd:cd03799 127 DLFLPNCELFKH-RLIALGCDEKKIIVHRSGIDCNKF-RFKPRYLPldgkIRILTVGRLTEKKGLEYAIEAVAKLAQKYP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 234 RpLSALMIGDGPDRDRYREMMVERGLG---KRIGMLPAMRVHEAFSMAQNLVVPS------RAEAMPYIVLEGLGAGKTI 304
Cdd:cd03799 205 N-IEYQIIGDGDLKEQLQQLIQELNIGdcvKLLGWKPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPV 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586791992 305 IASRVGGIPEVL--GAdSAALVEPGNSDDLARVMAETLSTP-DWhartmpkPEAVKAVFSSAVMARDVLKLYHEL 376
Cdd:cd03799 284 ISTEHGGIPELVedGV-SGFLVPERDAEAIAEKLTYLIEHPaIW-------PEMGKAGRARVEEEYDINKLNDEL 350
|
|
| PRK10307 |
PRK10307 |
colanic acid biosynthesis glycosyltransferase WcaI; |
172-367 |
5.75e-04 |
|
colanic acid biosynthesis glycosyltransferase WcaI;
Pssm-ID: 236670 [Multi-domain] Cd Length: 412 Bit Score: 41.89 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 172 ARKVGRPRTKTRLIYNGIGERDFEPIPTRS------------DAVHFIYVGMLRDLKGPDLFVDAfakTERLLGRP-LSA 238
Cdd:PRK10307 186 AREKGVAAEKVIFFPNWSEVARFQPVADADvdalraqlglpdGKKIVLYSGNIGEKQGLELVIDA---ARRLRDRPdLIF 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 239 LMIGDGPDRDRYREMMVERGLG--KRIGMLPAMRVHEAFSMAQNLVVPSRAEA----MPYIVLEGLGAGKTIIA-SRVG- 310
Cdd:PRK10307 263 VICGQGGGKARLEKMAQCRGLPnvHFLPLQPYDRLPALLKMADCHLLPQKAGAadlvLPSKLTNMLASGRNVVAtAEPGt 342
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586791992 311 GIPEVLgADSAALVEPGNSDDLARVMAETLSTPDW----------HARTMPKPEAVKAVFSSAVMAR 367
Cdd:PRK10307 343 ELGQLV-EGIGVCVEPESVEALVAAIAALARQALLrpklgtvareYAERTLDKENVLRQFIADIRGL 408
|
|
| PRK15179 |
PRK15179 |
Vi polysaccharide biosynthesis protein TviE; Provisional |
171-337 |
8.72e-04 |
|
Vi polysaccharide biosynthesis protein TviE; Provisional
Pssm-ID: 185101 [Multi-domain] Cd Length: 694 Bit Score: 41.56 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 171 YARKVGRPRTKTRLIYNGIGERDFEPIP----------TRSDAVHFIYVGMLR--DLKGPDLFVDAFAKTerLLGRP-LS 237
Cdd:PRK15179 473 YADWLGVDERRIPVVYNGLAPLKSVQDDactammaqfdARTSDARFTVGTVMRvdDNKRPFLWVEAAQRF--AASHPkVR 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 238 ALMIGDGPDRDRYREMMVERGLGKRIgMLPAMRVHEAFSMAQ--NLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEV 315
Cdd:PRK15179 551 FIMVGGGPLLESVREFAQRLGMGERI-LFTGLSRRVGYWLTQfnAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEA 629
|
170 180
....*....|....*....|....*
gi 1586791992 316 LGADSAALVEPGNS---DDLARVMA 337
Cdd:PRK15179 630 VQEGVTGLTLPADTvtaPDVAEALA 654
|
|
| GT4_mannosyltransferase-like |
cd03822 |
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ... |
207-344 |
1.17e-03 |
|
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.
Pssm-ID: 340849 [Multi-domain] Cd Length: 370 Bit Score: 40.83 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 207 IYVGMLRDLKGPDLFVDAF----AKTERL----LGRPlsalmiGDGPDR---DRYREMMVER-GLGKRIGM----LPAMR 270
Cdd:cd03822 191 LTFGFIGPGKGLEILLEALpelkAEFPDVrlviAGEL------HPSLARyegERYRKAAIEElGLQDHVDFhnnfLPEEE 264
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1586791992 271 VHEAFSMAQNLVVP--SRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGADSAALVEPGNSDDLARVMAETLSTPD 344
Cdd:cd03822 265 VPRYISAADVVVLPylNTEQSSSGTLSYAIACGKPVISTPLRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDE 340
|
|
| PRK09922 |
PRK09922 |
lipopolysaccharide 1,6-galactosyltransferase; |
176-334 |
1.85e-03 |
|
lipopolysaccharide 1,6-galactosyltransferase;
Pssm-ID: 182148 [Multi-domain] Cd Length: 359 Bit Score: 40.08 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 176 GRPRTKTRLIYNGIGERDFE-PIPTRSDAVHFIYVGML-----RDLKgpDLFvDAFAKTErllgRPLSALMIGDGPDRDR 249
Cdd:PRK09922 152 GISAQRISVIYNPVEIKTIIiPPPERDKPAVFLYVGRLkfegqKNVK--ELF-DGLSQTT----GEWQLHIIGDGSDFEK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 250 YREMMVERGLGKRIGML-----PAMRVHEAFSMAQNLVVPSRAEAMPYIVLEGLGAGKTIIASRVGGIPEVLGADSA--A 322
Cdd:PRK09922 225 CKAYSRELGIEQRIIWHgwqsqPWEVVQQKIKNVSALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRDIIKPGLngE 304
|
170
....*....|..
gi 1586791992 323 LVEPGNSDDLAR 334
Cdd:PRK09922 305 LYTPGNIDEFVG 316
|
|
| GT4_trehalose_phosphorylase |
cd03792 |
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ... |
189-313 |
1.90e-03 |
|
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.
Pssm-ID: 340823 [Multi-domain] Cd Length: 378 Bit Score: 40.00 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586791992 189 IGERDFEPIPTRSdavHFIYVGMLRDLKGPDLFVDAFAKTERLLGRPLSALMIG---DGPDRDR-YREMMVERGLGKRIG 264
Cdd:cd03792 186 YLEKPFVIDPERP---YILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHgavDDPEGSVvYEEVMEYAGDDHDIH 262
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1586791992 265 ML---PAMRVHEAFSMAQNLVVP-SRAEAMPYIVLEGLGAGKTIIASRVGGIP 313
Cdd:cd03792 263 VLrlpPSDQEINALQRAATVVLQlSTREGFGLTVSEALWKGKPVIATPAGGIP 315
|
|
| |
