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Conserved domains on  [gi|1178481222|ref|WP_083003058|]
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glycosyltransferase [Pasteurella multocida]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 5-349 2.25e-16

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.


The actual alignment was detected with superfamily member cd03801:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 366  Bit Score: 79.89  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222   5 NVLIFTGLYLPGVkgGGPIRTIYNLTSRL-KNDINFYIITLDRDLGDPSPYKNIatntWIADENGTNIYYINPNFKVREL 83
Cdd:cd03801     1 KILLLSPELPPPV--GGAERHVRELARALaARGHDVTVLTPADPGEPPEELEDG----VIVPLLPSLAALLRARRLLREL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  84 IKVVNKIDYDVLYLNSFFNFRFTIIPLFLNKfnffkksKPIVLAPRGELSSSALSIKKYKKEIFTKLASWIGLYDQDIVW 163
Cdd:cd03801    75 RPLLRLRKFDVVHAHGLLAALLAALLALLLG-------APLVVTLHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 164 QGSSAHEINDIYtflvknNITYKKIIECRN---LSTPSSLTTSKKGINiQSRLRICFLSRIAKIKNLYFALEILQEI--D 238
Cdd:cd03801   148 SEALRDELRALG------GIPPEKIVVIPNgvdLERFSPPLRRKLGIP-PDRPVLLFVGRLSPRKGVDLLLEALAKLlrR 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 239 FP----VFLGIYGPLEDKkYWNACLSLINKlpshieVKYYGIVENTKVQETISNYDLFFVPTQGENYGHVFIEALSSGTP 314
Cdd:cd03801   221 GPdvrlVIVGGDGPLRAE-LEELELGLGDR------VRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLP 293

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1178481222 315 ILLSDQTPWR-NLKDKGIGWDIPLARKDRFIHALQA 349
Cdd:cd03801   294 VVATDVGGLPeVVEDGEGGLVVPPDDVEALADALLR 329
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 5-349 2.25e-16

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: 79.89  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222   5 NVLIFTGLYLPGVkgGGPIRTIYNLTSRL-KNDINFYIITLDRDLGDPSPYKNIatntWIADENGTNIYYINPNFKVREL 83
Cdd:cd03801     1 KILLLSPELPPPV--GGAERHVRELARALaARGHDVTVLTPADPGEPPEELEDG----VIVPLLPSLAALLRARRLLREL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  84 IKVVNKIDYDVLYLNSFFNFRFTIIPLFLNKfnffkksKPIVLAPRGELSSSALSIKKYKKEIFTKLASWIGLYDQDIVW 163
Cdd:cd03801    75 RPLLRLRKFDVVHAHGLLAALLAALLALLLG-------APLVVTLHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 164 QGSSAHEINDIYtflvknNITYKKIIECRN---LSTPSSLTTSKKGINiQSRLRICFLSRIAKIKNLYFALEILQEI--D 238
Cdd:cd03801   148 SEALRDELRALG------GIPPEKIVVIPNgvdLERFSPPLRRKLGIP-PDRPVLLFVGRLSPRKGVDLLLEALAKLlrR 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 239 FP----VFLGIYGPLEDKkYWNACLSLINKlpshieVKYYGIVENTKVQETISNYDLFFVPTQGENYGHVFIEALSSGTP 314
Cdd:cd03801   221 GPdvrlVIVGGDGPLRAE-LEELELGLGDR------VRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLP 293

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1178481222 315 ILLSDQTPWR-NLKDKGIGWDIPLARKDRFIHALQA 349
Cdd:cd03801   294 VVATDVGGLPeVVEDGEGGLVVPPDDVEALADALLR 329
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
212-319 1.62e-07

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 49.82  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 212 RLRICFLSRIAK-IKNLYFALEILQEI---DFPVFLGIYGPLEDKKYwnacLSLINKLPSHIEVkyYGIVENtkVQETIS 287
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLrkrDNDVRLVIVGDGPEEEL----EELAAGLEDRVIF--TGFVED--LAELLA 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1178481222 288 NYDLFFVPTQGENYGHVFIEALSSGTPILLSD 319
Cdd:pfam13692  73 AADVFVLPSLYEGFGLKLLEAMAAGLPVVATD 104
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 286-390 6.62e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 44.98  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 286 ISNYDLFFVPTQGENYGHVFIEALSSGTPILLSDQTPWRNL-KDKGIGWDIPLARKDRFIHALQAFNHfNVEKRQIIKQK 364
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEViEDGETGLLVPPGDPEALAEAILRLLE-DPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....*.
gi 1178481222 365 CINFADSIINSKEVLDANKNIFLDLV 390
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 5-349 2.25e-16

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: 79.89  E-value: 2.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222   5 NVLIFTGLYLPGVkgGGPIRTIYNLTSRL-KNDINFYIITLDRDLGDPSPYKNIatntWIADENGTNIYYINPNFKVREL 83
Cdd:cd03801     1 KILLLSPELPPPV--GGAERHVRELARALaARGHDVTVLTPADPGEPPEELEDG----VIVPLLPSLAALLRARRLLREL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  84 IKVVNKIDYDVLYLNSFFNFRFTIIPLFLNKfnffkksKPIVLAPRGELSSSALSIKKYKKEIFTKLASWIGLYDQDIVW 163
Cdd:cd03801    75 RPLLRLRKFDVVHAHGLLAALLAALLALLLG-------APLVVTLHGAEPGRLLLLLAAERRLLARAEALLRRADAVIAV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 164 QGSSAHEINDIYtflvknNITYKKIIECRN---LSTPSSLTTSKKGINiQSRLRICFLSRIAKIKNLYFALEILQEI--D 238
Cdd:cd03801   148 SEALRDELRALG------GIPPEKIVVIPNgvdLERFSPPLRRKLGIP-PDRPVLLFVGRLSPRKGVDLLLEALAKLlrR 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 239 FP----VFLGIYGPLEDKkYWNACLSLINKlpshieVKYYGIVENTKVQETISNYDLFFVPTQGENYGHVFIEALSSGTP 314
Cdd:cd03801   221 GPdvrlVIVGGDGPLRAE-LEELELGLGDR------VRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLP 293

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1178481222 315 ILLSDQTPWR-NLKDKGIGWDIPLARKDRFIHALQA 349
Cdd:cd03801   294 VVATDVGGLPeVVEDGEGGLVVPPDDVEALADALLR 329
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 5-333 3.40e-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: 67.01  E-value: 3.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222   5 NVLIFTGLYLPgvKGGGPIRTIYNLTSRLKND-INFYIITLDrDLGDPSPyKNIATNTWIADENGTNIYYINP---NFKV 80
Cdd:cd03821     1 KILHVTPSISP--KAGGPVKVVLRLAAALAALgHEVTIVSTG-DGYESLV-VEENGRYIPPQDGFASIPLLRQgagRTDF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  81 RELIKVV---NKIDYDVLYLNSFFNfRFTIIPLFLNKfnffKKSKPIVLAPRGELSSSALSIKKYKKEIFTKL--ASWIG 155
Cdd:cd03821    77 SPGLPNWlrrNLREYDVVHIHGVWT-YTSLAACKLAR----RRGIPYVVSPHGMLDPWALQQKHWKKRIALHLieRRNLN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 156 LYDQDIVwqgSSAHEINDIYTFLVKNNITykkIIEcRNLSTP---SSLTTSKKGINIQSRLRICFLSRIAKIKNL-YF-- 229
Cdd:cd03821   152 NAALVHF---TSEQEADELRRFGLEPPIA---VIP-NGVDIPefdPGLRDRRKHNGLEDRRIILFLGRIHPKKGLdLLir 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 230 ALEILQEIDFPVFLGIYGPleDKKYWNACLSLINKLPSHIEVKYYGIVENTKVQETISNYDLFFVPTQGENYGHVFIEAL 309
Cdd:cd03821   225 AARKLAEQGRDWHLVIAGP--DDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEAL 302

                         330       340
                  ....*....|....*....|....
gi 1178481222 310 SSGTPILLSDQTPWRNLKDKGIGW 333
Cdd:cd03821   303 ACGLPVVITDKCGLSELVEAGCGV 326
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
212-319 1.62e-07

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 49.82  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 212 RLRICFLSRIAK-IKNLYFALEILQEI---DFPVFLGIYGPLEDKKYwnacLSLINKLPSHIEVkyYGIVENtkVQETIS 287
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLrkrDNDVRLVIVGDGPEEEL----EELAAGLEDRVIF--TGFVED--LAELLA 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1178481222 288 NYDLFFVPTQGENYGHVFIEALSSGTPILLSD 319
Cdd:pfam13692  73 AADVFVLPSLYEGFGLKLLEAMAAGLPVVATD 104
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 215-319 1.82e-07

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: 50.35  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 215 ICFLSRIAKIKNLYFALE---ILQEIDFPVFLGIYGPLEDKKYwnACLSLINKLPSHiEVKYYGIVENTKVQETISNYDL 291
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKafaLLKEKNPNLKLVIAGDGEEEKR--LKKLAEKLGLGD-NVIFLGFVSDEDLPELLKIADV 81

                          90       100
                  ....*....|....*....|....*...
gi 1178481222 292 FFVPTQGENYGHVFIEALSSGTPILLSD 319
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASD 109
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 217-316 5.10e-07

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: 51.13  E-value: 5.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 217 FLSRIAKIKNLYFALEILQEIDFPvfLGIYGPLEDKKYWNaclSLINKLP-SHIEvkYYGIVENTKVQETISN-YDLFFV 294
Cdd:cd03802   174 FLGRIAPEKGLEDAIRVARRAGLP--LKIAGKVRDEDYFY---YLQEPLPgPRIE--FIGEVGHDEKQELLGGaRALLFP 246

                          90       100
                  ....*....|....*....|..
gi 1178481222 295 PTQGENYGHVFIEALSSGTPIL 316
Cdd:cd03802   247 INWDEPFGLVMIEAMACGTPVI 268
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 178-319 3.57e-06

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: 48.48  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 178 LVKNNITYKKIIECRNLSTPSSLTTsKKGINIQSRLRICFLSRIAKIKNLYFALEILQEIDFP----VFLGiYGPLEDKK 253
Cdd:cd03823   158 HEANGLFSARISVIPNAVEPDLAPP-PRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPREdielVIAG-HGPLSDER 235

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1178481222 254 YWNACLSlinklpshieVKYYGIVENTKVQETISNYDLFFVPTQ-GENYGHVFIEALSSGTPILLSD 319
Cdd:cd03823   236 QIEGGRR----------IAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASD 292
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 286-390 6.62e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 44.98  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 286 ISNYDLFFVPTQGENYGHVFIEALSSGTPILLSDQTPWRNL-KDKGIGWDIPLARKDRFIHALQAFNHfNVEKRQIIKQK 364
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEViEDGETGLLVPPGDPEALAEAILRLLE-DPELRRRLGEA 96

                          90       100
                  ....*....|....*....|....*.
gi 1178481222 365 CINFADSIINSKEVLDANKNIFLDLV 390
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 216-319 9.33e-06

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: 46.63  E-value: 9.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 216 CFLSRIAKIKN---LYFALEILQEIDFPVFLGIYGPLEDKKYWNACLslINKLPSHIEVKYYGIVENTKVQETISNYDLF 292
Cdd:cd01635   114 VSVGRLVPEKGidlLLEALALLKARLPDLVLVLVGGGGEREEEEALA--AALGLLERVVIIGGLVDDEVLELLLAAADVF 191

                          90       100
                  ....*....|....*....|....*..
gi 1178481222 293 FVPTQGENYGHVFIEALSSGTPILLSD 319
Cdd:cd01635   192 VLPSRSEGFGLVLLEAMAAGKPVIATD 218
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 214-319 6.84e-05

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: 44.58  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 214 RICFLSRIAKIKNLYFALEILQEIDFP-----VFLGIyGPLED--KKywnaclsLINKLPSHIEVKYYGIVENTKVQETI 286
Cdd:cd03817   203 ILLYVGRLAKEKNIDFLLRAFAELKKEpniklVIVGD-GPEREelKE-------LARELGLADKVIFTGFVPREELPEYY 274

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1178481222 287 SNYDLFFVPTQGENYGHVFIEALSSGTPILLSD 319
Cdd:cd03817   275 KAADLFVFASTTETQGLVYLEAMAAGLPVVAAK 307
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 4-319 4.90e-04

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: 41.84  E-value: 4.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222   4 KNVLIFTGLYlpgvKGGGPIRTIYNLTSRL---KNDInfYIITLDRDlGDPSPY---KNIaTNTWIADENGTNIY-YINP 76
Cdd:cd03820     1 KIAIVIPSIS----NAGGAERVAINLANHLakkGYDV--TIISLDSA-EKPPFYeldDNI-KIKNLGDRKYSHFKlLLKY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  77 NFKVRELIKVVNKIDYDVLYlnsffNFRFTIIpLFLNKFNffKKSKPIVlaprGELSSSaLSIKKYKKEIFTKLASWIGL 156
Cdd:cd03820    73 FKKVRRLRKYLKNNKPDVVI-----SFRTSLL-TFLALIG--LKSKLIV----WEHNNY-EAYNKGLRRLLLRRLLYKRA 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 157 ydqdivwqgssaheinDIYTFLVKNNITYKKIIECRNLST---PSSLTTSKKGINIQSRlRICFLSRIAKIKNLYFALEI 233
Cdd:cd03820   140 ----------------DKIVVLTEADKLKKYKQPNSNVVVipnPLSFPSEEPSTNLKSK-RILAVGRLTYQKGFDLLIEA 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 234 LQEI--DFPVF-LGIYGPLEDKKYWNAclsLINKLpsHIE--VKYYGIVENtkVQETISNYDLFFVPTQGENYGHVFIEA 308
Cdd:cd03820   203 WALIakKHPDWkLRIYGDGPEREELEK---LIDKL--GLEdrVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEA 275

                         330
                  ....*....|.
gi 1178481222 309 LSSGTPILLSD 319
Cdd:cd03820   276 MAYGLPIISFD 286
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 12-319 6.29e-04

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: 41.51  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  12 LYLPGVKGGGPIRT----IYNLTSRLKNDINFYIITLDRDlgdpsPYKNIAtntwiaDENGTNIYYI-----NPNFKVRE 82
Cdd:cd03812     3 LHIVGGMNVGGIETflmnLYRKLDKSKIEFDFLATSDDKG-----EYDEEL------EELGGKIFYIppkkkNIIKYFIK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  83 LIKVVNKIDYDVLYLNSFFNfrfTIIPLFLnkfnFFKKSKPIVLAPrgelSSSALSIKKYKKEIFTKLASWIGLYDQDIV 162
Cdd:cd03812    72 LLKLIKKEKYDIVHVHGSSS---NGIILLL----AAKAGVPVRIAH----SHNTKDSSIKLRKIRKNVLKKLIERLSTKY 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 163 WQ-GSSAHE----INDIYTFLVKNN----ITYKKIIECRNLStpsslttsKKGINIQSRLRICFLSRIAKIKNLYFALEI 233
Cdd:cd03812   141 LAcSEDAGEwlfgEVENGKFKVIPNgidiEKYKFNKEKRRKR--------RKLLILEDKLVLGHVGRFNEQKNHSFLIDI 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 234 LQEIDfpvflgiygpledKKYWNACLSLINKLPSHIEVKYY----GIVENTK-------VQETISNYDLFFVPTQGENYG 302
Cdd:cd03812   213 FEELK-------------KKNPNVKLVLVGEGELKEKIKEKvkelGLEDKVIflgfrndVSEILSAMDVFLFPSLYEGLP 279

                         330
                  ....*....|....*..
gi 1178481222 303 HVFIEALSSGTPILLSD 319
Cdd:cd03812   280 LVAVEAQASGLPCLLSD 296
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 215-319 2.08e-03

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: 40.06  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 215 ICFLSRIAKIKNLYFALEI---LQEIDFPVFLGIYG--PLEDKKYWNA-CLSLINKlpshieVKYYGIVENTKVQETISN 288
Cdd:cd03798   203 ILFVGRLIPRKGIDLLLEAfarLAKARPDVVLLIVGdgPLREALRALAeDLGLGDR------VTFTGRLPHEQVPAYYRA 276

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1178481222 289 YDLFFVPTQGENYGHVFIEALSSGTPILLSD 319
Cdd:cd03798   277 CDVFVLPSRHEGFGLVLLEAMACGLPVVATD 307
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 79-319 2.66e-03

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: 39.65  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222  79 KVRELIKVVNKIDYDVLYLNSFFNFRFTIIPLFLNKF-NFFKKSKPIVLAPRGELSSSALSIKKYKKeifTKLASWIGLY 157
Cdd:cd03811    39 DEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLkRILKRAKPDVVISFLGFATYIVAKLAAAR---SKVIAWIHSS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 158 DQDIVWQGSSAHEINDIYTFL---------VKNNITYKKIIECRNLST-------PSSLTTSKKGINIQS--RLRICFLS 219
Cdd:cd03811   116 LSKLYYLKKKLLLKLKLYKKAdkivcvskgIKEDLIRLGPSPPEKIEViynpidiDRIRALAKEPILNEPedGPVILAVG 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 220 RIAKIKNLYFALEILQEIDF---PVFLGIYGPLEDKkywNACLSLINKLpsHIE--VKYYGIVENtkVQETISNYDLFFV 294
Cdd:cd03811   196 RLDPQKGHDLLIEAFAKLRKkypDVKLVILGDGPLR---EELEKLAKEL--GLAerVIFLGFQSN--PYPYLKKADLFVL 268

                         250       260
                  ....*....|....*....|....*
gi 1178481222 295 PTQGENYGHVFIEALSSGTPILLSD 319
Cdd:cd03811   269 SSRYEGFPNVLLEAMALGTPVVSTD 293
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 177-319 3.39e-03

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: 39.37  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1178481222 177 FLVKNNITYKKIIECRNLSTPSSLTTSKKGINIQsrLRICFLSRIAKIKNLYFALEILQEI-DFPVFLGI------YGPL 249
Cdd:cd04946   191 YLQKCYPAYKEKIFVSRLGVSDKEQYSKVKKEGD--LRLVSCSSIVPVKRIDLIIETLNSLcVAHPSICIswthigGGPL 268

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1178481222 250 EDKkywnaCLSLINKLPSHIEVKYYGIVENTKVQE--TISNYDLFFVPTQGENYGHVFIEALSSGTPILLSD 319
Cdd:cd04946   269 KER-----LEKLAENKLENVKVNFTGEVSNKEVKQlyKENDVDVFVNVSESEGIPVSIMEAISFGIPVIATN 335
 
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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