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Conserved domains on  [gi|2273501573|ref|WP_254772084|]
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glycosyltransferase family 4 protein [Pseudoalteromonas sp. DSM 26666]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 1-309 2.17e-35

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: 131.51  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   1 MIGGIETHIIELHKLLNKNRVNCSVL--FYKNHGNNEFYRLLDKQSIQYDFLQGSFMSLI--MRFRSYDHN-TVIHTHGY 75
Cdd:cd03801    12 PVGGAERHVRELARALAARGHDVTVLtpADPGEPPEELEDGVIVPLLPSLAALLRARRLLreLRPLLRLRKfDVVHAHGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  76 KAGILGRLACKLINKHCVSTYHAGEAGT------GKMWLYNKLDLWLSWLSTNFAVSEKISKTIK--------NAQLLEN 141
Cdd:cd03801    92 LAALLAALLALLLGAPLVVTLHGAEPGRlllllaAERRLLARAEALLRRADAVIAVSEALRDELRalggippeKIVVIPN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 142 FIAITEPPSTNFAQPVLK-----IGFVGRLSYEKGPDIFY-ALAQNMLINQQVEFHLFG-DGPMRNAIPQI-----NNLH 209
Cdd:cd03801   172 GVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRKGVDLLLeALAKLLRRGPDVRLVIVGgDGPLRAELEELelglgDRVR 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 210 YHG---LTNRDAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALL 286
Cdd:cd03801   252 FLGfvpDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLL 331

                         330       340
                  ....*....|....*....|...
gi 2273501573 287 AlSTTQKSEMAHSAYAMLEERFS 309
Cdd:cd03801   332 A-DPELRARLGRAARERVAERFS 353
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 1-309 2.17e-35

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: 131.51  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   1 MIGGIETHIIELHKLLNKNRVNCSVL--FYKNHGNNEFYRLLDKQSIQYDFLQGSFMSLI--MRFRSYDHN-TVIHTHGY 75
Cdd:cd03801    12 PVGGAERHVRELARALAARGHDVTVLtpADPGEPPEELEDGVIVPLLPSLAALLRARRLLreLRPLLRLRKfDVVHAHGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  76 KAGILGRLACKLINKHCVSTYHAGEAGT------GKMWLYNKLDLWLSWLSTNFAVSEKISKTIK--------NAQLLEN 141
Cdd:cd03801    92 LAALLAALLALLLGAPLVVTLHGAEPGRlllllaAERRLLARAEALLRRADAVIAVSEALRDELRalggippeKIVVIPN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 142 FIAITEPPSTNFAQPVLK-----IGFVGRLSYEKGPDIFY-ALAQNMLINQQVEFHLFG-DGPMRNAIPQI-----NNLH 209
Cdd:cd03801   172 GVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRKGVDLLLeALAKLLRRGPDVRLVIVGgDGPLRAELEELelglgDRVR 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 210 YHG---LTNRDAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALL 286
Cdd:cd03801   252 FLGfvpDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLL 331

                         330       340
                  ....*....|....*....|...
gi 2273501573 287 AlSTTQKSEMAHSAYAMLEERFS 309
Cdd:cd03801   332 A-DPELRARLGRAARERVAERFS 353
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 159-275 6.05e-19

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: 82.32  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 159 KIGFVGRLSYEKGPDIFY-ALAQNMLINQQVEFHLFGDGPMRN-------AIPQINNLHYHGLTNRDAIW---QHVDALL 227
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIkAFALLKEKNPNLKLVIAGDGEEEKrlkklaeKLGLGDNVIFLGFVSDEDLPellKIADVFV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2273501573 228 ICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANA 275
Cdd:pfam00534  84 LPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNA 131
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 217-321 1.80e-17

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 77.34  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 217 DAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALLAlSTTQKSEM 296
Cdd:COG0438    15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE-DPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 2273501573 297 AHSAYAMLEERFSGKKQFALLQTAY 321
Cdd:COG0438    94 GEAARERAEERFSWEAIAERLLALY 118
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
162-282 4.16e-11

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 63.19  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 162 FVGRLSYEKGP---DIFYALAQnmlINQQVEFHLFGDGPMRNAIPQI-------NNLHYHGLTNrdAIWQ-------HVD 224
Cdd:PRK09922  185 YVGRLKFEGQKnvkELFDGLSQ---TTGEWQLHIIGDGSDFEKCKAYsrelgieQRIIWHGWQS--QPWEvvqqkikNVS 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2273501573 225 ALLICSREEGLPMTLLESMSNHKIVISSPVGAIPS-IINNGVNGFLMKSANALECQQSI 282
Cdd:PRK09922  260 ALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRdIIKPGLNGELYTPGNIDEFVGKL 318
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 1-309 2.17e-35

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: 131.51  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   1 MIGGIETHIIELHKLLNKNRVNCSVL--FYKNHGNNEFYRLLDKQSIQYDFLQGSFMSLI--MRFRSYDHN-TVIHTHGY 75
Cdd:cd03801    12 PVGGAERHVRELARALAARGHDVTVLtpADPGEPPEELEDGVIVPLLPSLAALLRARRLLreLRPLLRLRKfDVVHAHGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  76 KAGILGRLACKLINKHCVSTYHAGEAGT------GKMWLYNKLDLWLSWLSTNFAVSEKISKTIK--------NAQLLEN 141
Cdd:cd03801    92 LAALLAALLALLLGAPLVVTLHGAEPGRlllllaAERRLLARAEALLRRADAVIAVSEALRDELRalggippeKIVVIPN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 142 FIAITEPPSTNFAQPVLK-----IGFVGRLSYEKGPDIFY-ALAQNMLINQQVEFHLFG-DGPMRNAIPQI-----NNLH 209
Cdd:cd03801   172 GVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRKGVDLLLeALAKLLRRGPDVRLVIVGgDGPLRAELEELelglgDRVR 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 210 YHG---LTNRDAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALL 286
Cdd:cd03801   252 FLGfvpDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLL 331

                         330       340
                  ....*....|....*....|...
gi 2273501573 287 AlSTTQKSEMAHSAYAMLEERFS 309
Cdd:cd03801   332 A-DPELRARLGRAARERVAERFS 353
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 2-309 4.83e-35

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: 130.41  E-value: 4.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   2 IGGIETHIIELHKLLNKNrvNCSV-LFYKNHGNNEFY-RLLDKQSIQYDFLQGS---------FMSL--IMRFRSYDhnt 68
Cdd:cd03808     9 DGGFQSFRLPLIKALVKK--GYEVhVIAPDGDKLSDElKELGVKVIDIPILRRGinplkdlkaLFKLykLLKKEKPD--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  69 VIHTHGYKAGILGRLACKLI-NKHCVSTYH----AGEAGTGKMWLYNKLDLWLS-WLSTNFAVSE--------KISKTIK 134
Cdd:cd03808    84 IVHCHTPKPGILGRLAARLAgVPKVIYTVHglgfVFTEGKLLRLLYLLLEKLALlFTDKVIFVNEddrdlaikKGIIKKK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 135 NAQLLE-NFIAITEPP--STNFAQPVLKIGFVGRLSYEKGPDIFYALAQNM-LINQQVEFHLFGDGPMRNAI-PQINNLH 209
Cdd:cd03808   164 KTVLIPgSGVDLDRFQysPESLPSEKVVFLFVARLLKDKGIDELIEAAKILkKKGPNVRFLLVGDGELENPSeILIEKLG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 210 YHGL-------TNRDAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSI 282
Cdd:cd03808   244 LEGRieflgfrSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDVEALADAI 323

                         330       340
                  ....*....|....*....|....*..
gi 2273501573 283 EALLaLSTTQKSEMAHSAYAMLEERFS 309
Cdd:cd03808   324 EKLI-EDPELRKEMGEAARKRVEEKFD 349
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 3-293 1.53e-27

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: 110.14  E-value: 1.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   3 GGIETHIIELHKLLNKNRVNCSVLFYKNHGNNEFYRLLDKQSIQYDFLQGSFMS-----LIMRFRSYDHNT---VIHTHG 74
Cdd:cd03811    12 GGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKlgllkAILKLKRILKRAkpdVVISFL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  75 YKAGILGRLACKLINKhCVSTYH--AGEAGTGKMW------LYNKLDLWLS-------WLSTNFAVSEKISKTIKNAQLL 139
Cdd:cd03811    92 GFATYIVAKLAAARSK-VIAWIHssLSKLYYLKKKlllklkLYKKADKIVCvskgikeDLIRLGPSPPEKIEVIYNPIDI 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 140 ENFIAITEPPSTNFAQPVLKIGFVGRLSYEKGPD-IFYALAQnmLINQQVEFHLF--GDGPMRNAI-PQINNL------H 209
Cdd:cd03811   171 DRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDlLIEAFAK--LRKKYPDVKLVilGDGPLREELeKLAKELglaervI 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 210 YHGL-TNRDAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALLAL 288
Cdd:cd03811   249 FLGFqSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQK 328


                  ....*
gi 2273501573 289 STTQK 293
Cdd:cd03811   329 KLDAA 333
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 2-309 5.81e-24

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: 100.12  E-value: 5.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   2 IGGIETHIIELHKLLNKNrvNCSVLFYKNhGNNEFYRLLdkqsiQYDflQGSFMSLIMRFRSYDHNT------------V 69
Cdd:cd03819    10 IGGAETYILDLARALAER--GHRVLVVTA-GGPLLPRLR-----QIG--IGLPGLKVPLLRALLGNVrlarlirreridL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  70 IHTHGYKAGILGRLACKLINKHCVSTYHageagtGKMWLYNKLDLWLSWLSTN----FAVSEKISKTIKNA--------Q 137
Cdd:cd03819    80 IHAHSRAPAWLGWLASRLTGVPLVTTVH------GSYLATYHPKDFALAVRARgdrvIAVSELVRDHLIEAlgvdperiR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 138 LLENFIAITEPPSTNFAQP---------VLKIGFVGRLSYEKGPDIFYALAQnmLINQQVEFHLF--GDGP----MRNAI 202
Cdd:cd03819   154 VIPNGVDTDRFPPEAEAEEraqlglpegKPVVGYVGRLSPEKGWLLLVDAAA--ELKDEPDFRLLvaGDGPerdeIRRLV 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 203 PQinnlhyHGLTNR----------DAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKS 272
Cdd:cd03819   232 ER------LGLRDRvtftgfredvPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPP 305

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2273501573 273 ANALECQQSIEALLALSTTQKSEMAHSA-YAMLEERFS 309
Cdd:cd03819   306 GDAEALADAIRAAKLLPEAREKLQAAAAlTEAVRELLL 343
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 3-309 8.23e-23

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: 97.39  E-value: 8.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   3 GGIETHIIELHKLLNKNRVNCSVLFYKNHGnnEFYRLLDKQSIQYDFLQGSFMSLI---------MRFRSYDhntVIHTH 73
Cdd:cd03807    12 GGAETMLLRLLEHMDKSRFEHVVISLTGDG--VLGEELLAAGVPVVCLGLSSGKDPgvllrlaklIRKRNPD---VVHTW 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  74 GYKAGILGRLACKLINKHCV--STYHAGEAGTGKMWLyNKLDLWLS-WLSTNFAVSEKI-------------SKTIKNAQ 137
Cdd:cd03807    87 MYHADLIGGLAAKLAGGVKViwSVRSSNIPQRLTRLV-RKLCLLLSkFSPATVANSSAVaefhqeqgyaknkIVVIYNGI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 138 LLENFiAITEPPSTNFAQP------VLKIGFVGRLSYEKG-PDIFYALAQNMLINQQVEFHLFGDGPMR-NAIPQINNLH 209
Cdd:cd03807   166 DLFKL-SPDDASRARARRRlglaedRRVIGIVGRLHPVKDhSDLLRAAALLVETHPDLRLLLVGRGPERpNLERLLLELG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 210 Y----HGLTNRD---AIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVnGFLM--KSANALecQQ 280
Cdd:cd03807   245 LedrvHLLGERSdvpALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGT-GFLVpaGDPQAL--AD 321

                         330       340
                  ....*....|....*....|....*....
gi 2273501573 281 SIEALLALSTTQKsEMAHSAYAMLEERFS 309
Cdd:cd03807   322 AIRALLEDPEKRA-RLGRAARERIANEFS 349
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 159-275 6.05e-19

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: 82.32  E-value: 6.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 159 KIGFVGRLSYEKGPDIFY-ALAQNMLINQQVEFHLFGDGPMRN-------AIPQINNLHYHGLTNRDAIW---QHVDALL 227
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIkAFALLKEKNPNLKLVIAGDGEEEKrlkklaeKLGLGDNVIFLGFVSDEDLPellKIADVFV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2273501573 228 ICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANA 275
Cdd:pfam00534  84 LPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNA 131
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
159-287 6.45e-19

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 81.40  E-value: 6.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 159 KIGFVGRLS-YEKGPDIFY-ALAQnmLINQQ--VEFHLFGDGPMRNAIPQINNL----HYHG-LTNRDAIWQHVDALLIC 229
Cdd:pfam13692   3 VILFVGRLHpNVKGVDYLLeAVPL--LRKRDndVRLVIVGDGPEEELEELAAGLedrvIFTGfVEDLAELLAAADVFVLP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2273501573 230 SREEGLPMTLLESMSNHKIVISSPVGAIPSIInNGVNGFLMKSANALECQQSIEALLA 287
Cdd:pfam13692  81 SLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILRLLE 137
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 217-321 1.80e-17

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 77.34  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 217 DAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALLAlSTTQKSEM 296
Cdd:COG0438    15 EALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLE-DPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 2273501573 297 AHSAYAMLEERFSGKKQFALLQTAY 321
Cdd:COG0438    94 GEAARERAEERFSWEAIAERLLALY 118
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 3-269 3.19e-17

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: 79.37  E-value: 3.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   3 GGIETHIIELHKLLNKNRVNCSVLFYKNHGNNEFYRLLDKQSIQydflqgsfmslimrfrsydhntVIHTHGYKAGILGR 82
Cdd:cd01635    13 GGLELHVRALARALAALGHEVTVLALLLLALRRILKKLLELKPD----------------------VVHAHSPHAAALAA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  83 -LACKLINKHCVSTYHAgeagtgkmwlynkLDLWLSWLSTNFAVSEKISKTIKNAQLlenfiaiteppstnfaqpvlkig 161
Cdd:cd01635    71 lLAARLLGIPIVVTVHG-------------PDSLESTRSELLALARLLVSLPLADKV----------------------- 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 162 FVGRLSYEKGPDIF---YALAQNMLINqqVEFHLFGDGPMRNAIPQ-----------INNLHYHGLTNRDAIWQHVDALL 227
Cdd:cd01635   115 SVGRLVPEKGIDLLleaLALLKARLPD--LVLVLVGGGGEREEEEAlaaalgllervVIIGGLVDDEVLELLLAAADVFV 192

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2273501573 228 ICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFL 269
Cdd:cd01635   193 LPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 57-321 6.82e-17

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: 80.50  E-value: 6.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  57 LIMRFRSYDHNtVIHTHG-YKAGILGRLACKLINKHCVSTYHAGEAGTGKMWLYNKLDL--------WLSWLST------ 121
Cdd:cd03798    87 LLKRRRRGPPD-LIHAHFaYPAGFAAALLARLYGVPYVVTEHGSDINVFPPRSLLRKLLrwalrraaRVIAVSKalaeel 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 122 -NFAVSEKISKTIKNAQLLENFIAITEPPSTNFAQPVlkIGFVGRLSYEKGPDIFY-ALAQNMLINQQVEFHLFGDGPMR 199
Cdd:cd03798   166 vALGVPRDRVDVIPNGVDPARFQPEDRGLGLPLDAFV--ILFVGRLIPRKGIDLLLeAFARLAKARPDVVLLIVGDGPLR 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 200 NAIPQI-------NNLHYHGLTNRDAIWQHV---DALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFL 269
Cdd:cd03798   244 EALRALaedlglgDRVTFTGRLPHEQVPAYYracDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLL 323

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2273501573 270 MKSANAlecqQSIEALL--ALSTTQKSEMAHSAYAMLEERFSGKKQFALLQTAY 321
Cdd:cd03798   324 VPPGDA----DALAAALrrALAEPYLRELGEAARARVAERFSWVKAADRIAAAY 373
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 2-309 3.35e-14

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: 72.27  E-value: 3.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   2 IGGIETHIIELHKLLNKNRVNCSVL---------FYKNHGNNEFYRLLD----KQSIQYDFLQgSFMSLIMRFRSYDHNT 68
Cdd:cd03820    12 AGGAERVAINLANHLAKKGYDVTIIsldsaekppFYELDDNIKIKNLGDrkysHFKLLLKYFK-KVRRLRKYLKNNKPDV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  69 VIHTHGykaGILGRLACKLINKHCVSTYH--------AGEAGTGKMWLYNKLD----LwlswlsTNFAVSEKISKTIKNA 136
Cdd:cd03820    91 VISFRT---SLLTFLALIGLKSKLIVWEHnnyeaynkGLRRLLLRRLLYKRADkivvL------TEADKLKKYKQPNSNV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 137 QLLENFIaiTEPPSTNFAQPVLK-IGFVGRLSYEKGPDifyalaqnMLI-------NQQVEF--HLFGDGPMRNAIP-QI 205
Cdd:cd03820   162 VVIPNPL--SFPSEEPSTNLKSKrILAVGRLTYQKGFD--------LLIeawaliaKKHPDWklRIYGDGPEREELEkLI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 206 NNL------HYHGLTNrdAIWQHV--DALLIC-SREEGLPMTLLESMSNHKIVISS--PVGaiPS-IINNGVNGFLMKSA 273
Cdd:cd03820   232 DKLgledrvKLLGPTK--NIAEEYanSSIFVLsSRYEGFPMVLLEAMAYGLPIISFdcPTG--PSeIIEDGENGLLVPNG 307

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2273501573 274 NALECQQSIEALLAlSTTQKSEMAHSAYAMLeERFS 309
Cdd:cd03820   308 DVDALAEALLRLME-DEELRKKMGKNARKNA-ERFS 341
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 148-315 5.12e-14

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: 71.98  E-value: 5.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 148 PPSTNFAQPVLKIGFVGRLSYEKGPDIFYALAQNmLINQQVEFHLFGDGPMrNAIPQINN---LHYHGLTNRDAI---WQ 221
Cdd:cd03823   182 PPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKR-LPREDIELVIAGHGPL-SDERQIEGgrrIAFLGRVPTDDIkdfYE 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 222 HVDALLICSR-EEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMK--SANALECqqsieALLALSTtqKSEMAH 298
Cdd:cd03823   260 KIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFApgDAEDLAA-----AMRRLLT--DPALLE 332

                         170
                  ....*....|....*..
gi 2273501573 299 SAYAMLEERFSGKKQFA 315
Cdd:cd03823   333 RLRAGAEPPRSTESQAE 349
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 49-272 1.30e-12

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: 67.69  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  49 FLQGSFMSLIMRFRSYDhntVIHTHG-YKAGILGRLACKLINKHCVSTYH-AGEAGTGKMWLYNKLDLW-LSWLSTNF-- 123
Cdd:cd03817    70 FPFKKAVIDRIKELGPD---IIHTHTpFSLGKLGLRIARKLKIPIVHTYHtMYEDYLHYIPKGKLLVKAvVRKLVRRFyn 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 124 ------AVSEKISKTIKNAQLLENFIAI--------TEPPST-------NFAQPVLKIGFVGRLSYEKGPD-IFYALAQn 181
Cdd:cd03817   147 htdaviAPSEKIKDTLREYGVKGPIEVIpngidldkFEKPLNteerrklGLPPDEPILLYVGRLAKEKNIDfLLRAFAE- 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 182 MLINQQVEFHLFGDGPMRNAIPQI-------NNLHYHGLTNRD---AIWQHVDALLICSREEGLPMTLLESMSnhkivIS 251
Cdd:cd03817   226 LKKEPNIKLVIVGDGPEREELKELarelglaDKVIFTGFVPREelpEYYKAADLFVFASTTETQGLVYLEAMA-----AG 300

                         250       260
                  ....*....|....*....|....*.
gi 2273501573 252 SPV-----GAIPSIINNGVNGFLMKS 272
Cdd:cd03817   301 LPVvaakdPAASELVEDGENGFLFEP 326
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 160-321 2.44e-11

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: 63.85  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 160 IGFVGRLSYEKGPDIFYALAQNMLINQQVEFHLFGDGPMRNAIPQIN-NLHYHGLTNRDAIWQHV---DALLICSREEGL 235
Cdd:cd03814   201 LLYVGRLAPEKNLEALLDADLPLAASPPVRLVVVGDGPARAELEARGpDVIFTGFLTGEELARAYasaDVFVFPSRTETF 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 236 PMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALLALSTTQKsEMAHSAYAMLeERFSGKKQFA 315
Cdd:cd03814   281 GLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRR-RMAARARAEA-ERYSWEAFLD 358


                  ....*.
gi 2273501573 316 LLQTAY 321
Cdd:cd03814   359 NLLDYY 364
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
162-282 4.16e-11

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 63.19  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 162 FVGRLSYEKGP---DIFYALAQnmlINQQVEFHLFGDGPMRNAIPQI-------NNLHYHGLTNrdAIWQ-------HVD 224
Cdd:PRK09922  185 YVGRLKFEGQKnvkELFDGLSQ---TTGEWQLHIIGDGSDFEKCKAYsrelgieQRIIWHGWQS--QPWEvvqqkikNVS 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2273501573 225 ALLICSREEGLPMTLLESMSNHKIVISSPVGAIPS-IINNGVNGFLMKSANALECQQSI 282
Cdd:PRK09922  260 ALLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRdIIKPGLNGELYTPGNIDEFVGKL 318
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 125-312 1.59e-10

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. 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: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 61.16  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 125 VSEKISKTIKNAQLLENFIAITEPPSTNFAQPVLKIGFVGRLSYEKGPD-IFYALAQNMLINQQVEFHLFGDGPMRNAIP 203
Cdd:cd04949   128 LSERFNKYPPIFTIPVGYVDQLDTAESNHERKSNKIITISRLAPEKQLDhLIEAVAKAVKKVPEITLDIYGYGEEREKLK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 204 -QINNLH---------YHglTNRDAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPS-IINNGVNGFLMKS 272
Cdd:cd04949   208 kLIEELHlednvflkgYH--SNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYGPSeLIEDGENGYLIEK 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2273501573 273 ANALECQQSIEALLALSTTQKsEMAHSAYAMlEERFSGKK 312
Cdd:cd04949   286 NNIDALADKIIELLNDPEKLQ-QFSEESYKI-AEKYSTEN 323
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 104-313 9.17e-10

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: 59.27  E-value: 9.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 104 GKMWLYNKLDLWL----SWLSTNFAVSEKISKtiKNAQLLENFIAITE---------PPSTNFAQPVlKIGFVGRLSYE- 169
Cdd:cd03825   129 RKREALAKKRLTIvapsRWLADMVRRSPLLKG--LPVVVIPNGIDTEIfapvdkakaRKRLGIPQDK-KVILFGAESVTk 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 170 --KGPDIFYALAQNMLINQQVEFHLFGDGPMRNAIPQINnLHYHGLTNRDA----IWQHVDALLICSREEGLPMTLLESM 243
Cdd:cd03825   206 prKGFDELIEALKLLATKDDLLLVVFGKNDPQIVILPFD-IISLGYIDDDEqlvdIYSAADLFVHPSLADNLPNTLLEAM 284

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 244 SNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALLAlSTTQKSEMAHSAYAMLEERFSGKKQ 313
Cdd:cd03825   285 ACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLA-NPKERESLGERARALAENHFDQRVQ 353
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 2-252 1.12e-09

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: 58.84  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   2 IGGIETHIIELHKLLNKNRVNCSVLFY-----------KNHGNNEFYRLLDKQSIqYDFLQGSFMslIMRFRSYDhntVI 70
Cdd:cd03812    11 VGGIETFLMNLYRKLDKSKIEFDFLATsddkgeydeelEELGGKIFYIPPKKKNI-IKYFIKLLK--LIKKEKYD---IV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  71 HTHG-YKAGILGRLACKLINKHCVSTYHAGEAGTGKMW--LYNKLDLWLSWLSTN-FAVSEKISK------TIKNAQLLE 140
Cdd:cd03812    85 HVHGsSSNGIILLLAAKAGVPVRIAHSHNTKDSSIKLRkiRKNVLKKLIERLSTKyLACSEDAGEwlfgevENGKFKVIP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 141 NFIAITEPpstNFAQPV-------------LKIGFVGRLSYEKGP----DIFYALaqnmlINQQVEFHLF--GDGPMRNA 201
Cdd:cd03812   165 NGIDIEKY---KFNKEKrrkrrklliledkLVLGHVGRFNEQKNHsfliDIFEEL-----KKKNPNVKLVlvGEGELKEK 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2273501573 202 IPQ-------INNLHYHGLTNRDAIW-QHVDALLICSREEGLPMTLLESMSNHKIVISS 252
Cdd:cd03812   237 IKEkvkelglEDKVIFLGFRNDVSEIlSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLS 295
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 126-309 7.90e-09

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: 56.20  E-value: 7.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 126 SEKISkTIKNAQLLENFIAI--TEPPSTNFAQPVLKIGFVGRLSYEKGPDIFYALAQNMLINQQVEFHLFGDGPMRNAIP 203
Cdd:cd03794   185 KEKII-VIPNWADLEEFKPPpkDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAERLKRRPDIRFLFVGDGDEKERLK 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 204 Q------INNLHYHGLTNRDAIWQHV---DALLIC-----SREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFL 269
Cdd:cd03794   264 ElakargLDNVTFLGRVPKEEVPELLsaaDVGLVPlkdnpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLV 343

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2273501573 270 MKSANALECQQSIEALLAlSTTQKSEMAHSAYAMLEERFS 309
Cdd:cd03794   344 VEPGDPEALADAILELLD-DPELRRAMGENGRELAEEKFS 382
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 2-309 1.45e-08

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: 55.36  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   2 IGGIETHIIELHKLLNKNRVNCSVL--------FYKNHGNNEFYRLldKQSIQYdFLQGSFMSLIMRFR----SYDhntV 69
Cdd:cd03795    13 IGGIEQVIYDLAEGLKKKGIEVDVLcfskeketPEKEENGIRIHRV--KSFLNV-ASTPFSPSYIKRFKklakEYD---I 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  70 IHTH-GYKAGILGRLACKlINKHCVSTYHAG---EAGTgkMWLYNKLDLWLswL---------STNFAVSEKISKTIKN- 135
Cdd:cd03795    87 IHYHfPNPLADLLLFFSG-AKKPVVVHWHSDivkQKKL--LKLYKPLMTRF--LrradriiatSPNYVETSPTLREFKNk 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 136 AQLLENFIAITEPPSTNFAQPVLK--------IGFVGRLSYEKGPDIfyalaqnmLIN--QQVEFHLF--GDGPMRNAIP 203
Cdd:cd03795   162 VRVIPLGIDKNVYNIPRVDFENIKrekkgkkiFLFIGRLVYYKGLDY--------LIEaaQYLNYPIVigGEGPLKPDLE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 204 Q------INNLHYHGLTNRDaiwQHVDALLIC--------SREEGLPMTLLESMSNHKIVISSPVG-AIPSIINNGVNGF 268
Cdd:cd03795   234 AqielnlLDNVKFLGRVDDE---EKVIYLHLCdvfvfpsvLRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGL 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2273501573 269 LMKSANALECQQSIEALLAlSTTQKSEMAHSAYAMLEERFS 309
Cdd:cd03795   311 VVPPKDPDALAEAIDKLLS-DEELRESYGENAKKRFEELFT 350
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 2-263 1.80e-08

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: 55.14  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   2 IGGIETHIIELHKLLNK--NRVNCSVLfyknHGNNEFYRLLDKQSIQYDFLQGSFMSLIM------RFRSYDHNTVIHTH 73
Cdd:cd04951    11 LGGAEKQTVLLADQMFIrgHDVNIVYL----TGEVEVKPLNNNIIIYNLGMDKNPRSLLKallklkKIISAFKPDVVHSH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  74 GYKAGILGRLACKLINKH-CVSTYHA-GEAGTGKMWLYNKLDlWLSWLSTNF---AVSEKISK--TIKN-AQLLENFIAI 145
Cdd:cd04951    87 MFHANIFARFLRMLYPIPlLICTAHNkNEGGRIRMFIYRLTD-FLCDITTNVsreALDEFIAKkaFSKNkSVPVYNGIDL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 146 TEPPSTNFAQPVLKIGF-----------VGRLSYEKG-PDIFYALAQNMLINQQVEFHLFGDGPMRNAIPQ-INNLHyhg 212
Cdd:cd04951   166 NKFKKDINVRLKIRNKLnlkndefvilnVGRLTEAKDyPNLLLAISELILSKNDFKLLIAGDGPLRNELERlICNLN--- 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273501573 213 LTNR----------DAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINN 263
Cdd:cd04951   243 LVDRvillgqisniSEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD 303
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 160-285 2.42e-08

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 55.43  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 160 IGFVGRLSYEKGPDIFYALAQNMLINQ-QVEFHLFGDGPMRNAIPQI-------NNLHYHGLTNRDAIW-QHVDALLICS 230
Cdd:PRK15179  520 VGTVMRVDDNKRPFLWVEAAQRFAASHpKVRFIMVGGGPLLESVREFaqrlgmgERILFTGLSRRVGYWlTQFNAFLLLS 599

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2273501573 231 REEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMkSANALECQQSIEAL 285
Cdd:PRK15179  600 RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTL-PADTVTAPDVAEAL 653
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 158-308 8.47e-08

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: 53.22  E-value: 8.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 158 LKIGFVGRLSYEKGpdIFYALAQNMLINQQ---VEFHLFGDGPMRNAIPQI-------NNLHYHGLTNRDAIWQHVD--- 224
Cdd:cd03799   175 IRILTVGRLTEKKG--LEYAIEAVAKLAQKypnIEYQIIGDGDLKEQLQQLiqelnigDCVKLLGWKPQEEIIEILDead 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 225 ---ALLICSR---EEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANAlecQQSIEALLALSTTQK--SEM 296
Cdd:cd03799   253 ifiAPSVTAAdgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDA---EAIAEKLTYLIEHPAiwPEM 329

                         170
                  ....*....|..
gi 2273501573 297 AHSAYAMLEERF 308
Cdd:cd03799   330 GKAGRARVEEEY 341
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 160-318 1.97e-07

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: 52.07  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 160 IGFVGRLSYEKGPDI----FYALAQNMlinQQVEFHLFGDGPMRNAI----PQINNLHYHGLTNRDAIWQHVD-ALLIC- 229
Cdd:cd05844   192 ILFVGRLVEKKGCDVlieaFRRLAARH---PTARLVIAGDGPLRPALqalaAALGRVRFLGALPHAEVQDWMRrAEIFCl 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 230 -------SREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSIEALLAlSTTQKSEMAHSAYA 302
Cdd:cd05844   269 psvtaasGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLA-DRALADRMGGAARA 347

                         170
                  ....*....|....*.
gi 2273501573 303 MLEERFSGKKQFALLQ 318
Cdd:cd05844   348 FVCEQFDIRVQTAKLE 363
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
89-309 4.09e-07

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 51.24  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573  89 NKHCVSTYHAGeagtgkmwlynkldlWLSWLSTNFAV--------SEKISKTIKNaQLLENFIAITEPPSTNfaqpvlkI 160
Cdd:PRK15490  345 NNHCVTRHYAD---------------WLKLEAKHFQVvyngvlppSTEPSSEVPH-KIWQQFTQKTQDADTT-------I 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 161 GFVGRLSYEKGPDIFYALAQNMLINQ-QVEFHLFGDGPMRNAIPQ-------INNLHYHGLTNRDAIW-QHVDALLICSR 231
Cdd:PRK15490  402 GGVFRFVGDKNPFAWIDFAARYLQHHpATRFVLVGDGDLRAEAQKraeqlgiLERILFVGASRDVGYWlQKMNVFILFSR 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 232 EEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLMKSANALECQQSI---EALLALSTTqKSEMAHSAYAMLEERF 308
Cdd:PRK15490  482 YEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGVSGFILDDAQTVNLDQACryaEKLVNLWRS-RTGICQQTQSFLQERF 560


                  .
gi 2273501573 309 S 309
Cdd:PRK15490  561 T 561
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 192-321 4.46e-07

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: 50.81  E-value: 4.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 192 LFGDGPMR-NAIPQINNLhyhGLTNR----------DAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSI 260
Cdd:cd04962   231 LVGDGPERvPAEELAREL---GVEDRvlflgkqddvEELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEV 307

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273501573 261 INNGVNGFLMKSANALECQQSIEALLALSTTQKsEMAHSAYAMLEERFSGKKQFALLQTAY 321
Cdd:cd04962   308 VKHGETGFLSDVGDVDAMAKSALSILEDDELYN-RMGRAARKRAAERFDPERIVPQYEAYY 367
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 160-306 5.44e-07

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 50.86  E-value: 5.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 160 IGFVGRLSYEKGPDifyALAQNMLINQQVEFHLFGDGPMRNAIPQI---NNLHYHGLTNRD---AIWQHVDALLICSREE 233
Cdd:PLN02871  266 IVYVGRLGAEKNLD---FLKRVMERLPGARLAFVGDGPYREELEKMfagTPTVFTGMLQGDelsQAYASGDVFVMPSESE 342

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2273501573 234 GLPMTLLESMSNHKIVISSPVGAIPSIINN---GVNGFLMKSANALECQQSIEALLAlSTTQKSEMAHSAYAMLEE 306
Cdd:PLN02871  343 TLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGDVDDCVEKLETLLA-DPELRERMGAAAREEVEK 417
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
3-129 5.92e-06

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 45.99  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573   3 GGIETHIIELHKLLNKNRVNCSVLFYKNHGNNEF----------YRLLDKQSIQYDFLQGSFMSLIMRFRSYDhntVIHT 72
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEevvrvvrvprVPLPLPPRLLRSLAFLRRLRRLLRRERPD---VVHA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2273501573  73 HGYKAGILGRLACKLI-NKHCVSTYHAGEAGT----GKMWLYNKLDLWLSWLSTN-----FAVSEKI 129
Cdd:pfam13439  78 HSPFPLGLAALAARLRlGIPLVVTYHGLFPDYkrlgARLSPLRRLLRRLERRLLRradrvIAVSEAV 144
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 218-278 2.20e-05

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: 45.77  E-value: 2.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2273501573 218 AIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFLmksANALEC 278
Cdd:cd03792   275 ALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFL---VNSVEG 332
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 162-269 1.24e-04

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: 43.38  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 162 FVGRLSYEKGPDIFY-ALAQNMLINQQVEFHLFG----DGPMRNAIPQINNLHYHGLT---------NRD---AIWQHVD 224
Cdd:cd03800   225 ALGRLDPRKGIDTLVrAFAQLPELRELANLVLVGgpsdDPLSMDREELAELAEELGLIdrvrfpgrvSRDdlpELYRAAD 304

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2273501573 225 ALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGVNGFL 269
Cdd:cd03800   305 VFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLL 349
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 187-314 1.47e-04

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 43.22  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 187 QVEFHLFGDGPMRNAIPQI-----NNLHYH---GLTNRDAI---WQH-VDALLICSREEGLPMTLLESMSNHKIVISSPV 254
Cdd:cd04946   257 CISWTHIGGGPLKERLEKLaenklENVKVNftgEVSNKEVKqlyKENdVDVFVNVSESEGIPVSIMEAISFGIPVIATNV 336

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2273501573 255 GAIPSIINNGVNGFLMKSANALEcqQSIEAL--LALSTTQKSEMAHSAYAMLEERFSGKKQF 314
Cdd:cd04946   337 GGTREIVENETNGLLLDKDPTPN--EIVSSImkFYLDGGDYKTMKISARECWEERFNAEVNY 396
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
69-127 2.68e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 40.85  E-value: 2.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2273501573  69 VIHTHGYKAGILGRLACKLINKHCVSTYHAGEAGTGKMWLYNKLDLWLSWLSTN----FAVSE 127
Cdd:pfam13579  74 VVHAHSPTAGLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARALERRLLRRadavVVVSE 136
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 124-286 4.18e-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: 41.94  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 124 AVSEKIsKTIKNAQLLENFIAITEPPSTnfaQPVLKIGFVGRLSYEKgpDI---FYALAQNMLINQQVEFHLFG---DGP 197
Cdd:cd03813   264 ADPDKT-RVIPNGIDIQRFAPAREERPE---KEPPVVGLVGRVVPIK--DVktfIRAFKLVRRAMPDAEGWLIGpedEDP 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 198 M-----RNAIPQ---INNLHYHGLTNRDAIWQHVDALLICSREEGLPMTLLESMSNHKIVISSPVGAIPSII-----NNG 264
Cdd:cd03813   338 EyaqecKRLVASlglENKVKFLGFQNIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIygaddALG 417

                         170       180
                  ....*....|....*....|..
gi 2273501573 265 VNGFLMKSANALECQQSIEALL 286
Cdd:cd03813   418 QAGLVVPPADPEALAEALIKLL 439
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 162-312 4.20e-04

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: 41.59  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 162 FVGRLSYEKGPDIFyALAQNMLINQQVEFHLFGDGPMRNAIPQI-NNLHYHGLTNR------------DAIWQHVDALLI 228
Cdd:cd03821   209 FLGRIHPKKGLDLL-IRAARKLAEQGRDWHLVIAGPDDGAYPAFlQLQSSLGLGDRvtftgplygeakWALYASADLFVL 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2273501573 229 CSREEGLPMTLLESMSNHKIVISSPVGAIPSIINNGvNGFLMKSaNALECQQSIEALLALSTTQKS--EMAHsAYAMLEE 306
Cdd:cd03821   288 PSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRDPADRKRlgEMAR-RARQVEE 364


                  ....*.
gi 2273501573 307 RFSGKK 312
Cdd:cd03821   365 NFSWEA 370
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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