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Conserved domains on  [gi|1063695079|ref|NP_001320304|]
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UDP-Glycosyltransferase superfamily protein [Arabidopsis thaliana]

Protein Classification

glycosyltransferase( domain architecture ID 13876812)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_trans_4_5 pfam16994
Glycosyl-transferase family 4;
1-159 4.41e-66

Glycosyl-transferase family 4;


:

Pssm-ID: 465332  Cd Length: 172  Bit Score: 206.98  E-value: 4.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079   1 MELAFLLRGVGADVVWITNQKPLEddevvysLEHKMLDRGVQVISAKGQKAVDTSLKADLIVLNTAVAGKWLDAVLKENV 80
Cdd:pfam16994  22 MELATELRSCGATVVVVVLSKGGG-------LEQELLRRGIKVLPDKGRLSFRTALKADLVIANTAVCASWIDQYLKEHV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079  81 VKVLPKILWWIHEMRGHYF-----NADLVKHLPFvagamiDSHATAGYWKNRTQARLGIKMPKTYVVHLGNSKELMEVAE 155
Cdd:pfam16994  95 AGVLPKVLWWIHENRRHYFdraksMLDYVKHLPF------LSHSQAEQWLTWTEEELIILMPQTYVVHLSNNDELYFVAE 168

                  ....
gi 1063695079 156 DSVA 159
Cdd:pfam16994 169 ISVS 172
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
1-366 9.78e-41

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: 147.30  E-value: 9.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079   1 MELAFLLRGVGADVVWITNQKPLEDDEVVYSLEHKMLDRGVQVISAKGQ-----KAVDTSLKADLIVLNTAVAGKWLDAV 75
Cdd:cd03801    21 RELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelRPLLRLRKFDVVHAHGLLAALLAALL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079  76 LKENVVKvlpkILWWIHEMRGHYFNADLVKHLPFVAGAMIDSH------ATAGYWKNRTQARLGIKMPKTYVVHLGnske 149
Cdd:cd03801   101 ALLLGAP----LVVTLHGAEPGRLLLLLAAERRLLARAEALLRradaviAVSEALRDELRALGGIPPEKIVVIPNG---- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 150 lmevaedsVAKRVLREHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIkekklqvPTMHAVVVGSDmskqT 229
Cdd:cd03801   173 --------VDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRG-------PDVRLVIVGGD----G 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 230 KFETELRNfvREKKLENFVHFVNKTL--TVAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNG 307
Cdd:cd03801   234 PLRAELEE--LELGLGDRVRFLGFVPdeELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDG 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063695079 308 TTGLLHSAGKegVIPLAKNIVKLATQVELRLRMGKNGYERVKEMFLEHHMSHRIASVLK 366
Cdd:cd03801   310 EGGLVVPPDD--VEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
Glyco_trans_4_5 pfam16994
Glycosyl-transferase family 4;
1-159 4.41e-66

Glycosyl-transferase family 4;


Pssm-ID: 465332  Cd Length: 172  Bit Score: 206.98  E-value: 4.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079   1 MELAFLLRGVGADVVWITNQKPLEddevvysLEHKMLDRGVQVISAKGQKAVDTSLKADLIVLNTAVAGKWLDAVLKENV 80
Cdd:pfam16994  22 MELATELRSCGATVVVVVLSKGGG-------LEQELLRRGIKVLPDKGRLSFRTALKADLVIANTAVCASWIDQYLKEHV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079  81 VKVLPKILWWIHEMRGHYF-----NADLVKHLPFvagamiDSHATAGYWKNRTQARLGIKMPKTYVVHLGNSKELMEVAE 155
Cdd:pfam16994  95 AGVLPKVLWWIHENRRHYFdraksMLDYVKHLPF------LSHSQAEQWLTWTEEELIILMPQTYVVHLSNNDELYFVAE 168

                  ....
gi 1063695079 156 DSVA 159
Cdd:pfam16994 169 ISVS 172
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
1-366 9.78e-41

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: 147.30  E-value: 9.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079   1 MELAFLLRGVGADVVWITNQKPLEDDEVVYSLEHKMLDRGVQVISAKGQ-----KAVDTSLKADLIVLNTAVAGKWLDAV 75
Cdd:cd03801    21 RELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelRPLLRLRKFDVVHAHGLLAALLAALL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079  76 LKENVVKvlpkILWWIHEMRGHYFNADLVKHLPFVAGAMIDSH------ATAGYWKNRTQARLGIKMPKTYVVHLGnske 149
Cdd:cd03801   101 ALLLGAP----LVVTLHGAEPGRLLLLLAAERRLLARAEALLRradaviAVSEALRDELRALGGIPPEKIVVIPNG---- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 150 lmevaedsVAKRVLREHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIkekklqvPTMHAVVVGSDmskqT 229
Cdd:cd03801   173 --------VDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRG-------PDVRLVIVGGD----G 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 230 KFETELRNfvREKKLENFVHFVNKTL--TVAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNG 307
Cdd:cd03801   234 PLRAELEE--LELGLGDRVRFLGFVPdeELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDG 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063695079 308 TTGLLHSAGKegVIPLAKNIVKLATQVELRLRMGKNGYERVKEMFLEHHMSHRIASVLK 366
Cdd:cd03801   310 EGGLVVPPDD--VEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
260-370 5.24e-18

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 79.26  E-value: 5.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 260 YIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGkeGVIPLAKNIVKLATQVELRLR 339
Cdd:COG0438    17 LLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPG--DPEALAEAILRLLEDPELRRR 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063695079 340 MGKNGYERVKEMFLEHHMSHRIASVLKEVLQ 370
Cdd:COG0438    93 LGEAARERAEERFSWEAIAERLLALYEELLA 123
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
176-347 4.09e-15

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: 72.31  E-value: 4.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 176 EDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKLqvptmhaVVVGsdmskQTKFETELRNFVREKKLENFVHFVNKTL 255
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKL-------VIAG-----DGEEEKRLKKLAEKLGLGDNVIFLGFVS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 256 TVAP--YIAAIDVLVQNSQArgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLhsagkegVIP-----LAKNIV 328
Cdd:pfam00534  69 DEDLpeLLKIADVFVLPSRY--EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFL-------VKPnnaeaLAEAID 139
                         170
                  ....*....|....*....
gi 1063695079 329 KLATQVELRLRMGKNGYER 347
Cdd:pfam00534 140 KLLEDEELRERLGENARKR 158
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
160-366 1.37e-07

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 52.87  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 160 KRVLREHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKLqvptmhaVVVGSDMSKQTKFETELRNFV 239
Cdd:PRK15484  176 QSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKL-------VVVGDPTASSKGEKAAYQKKV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 240 RE--KKLENFVHFVNktlTVAP-----YIAAIDVLVQNSQARgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGlL 312
Cdd:PRK15484  249 LEaaKRIGDRCIMLG---GQPPekmhnYYPLADLVVVPSQVE-EAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITG-Y 323
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063695079 313 HSAGKEGVIPLAKNIVKLATQVElRLRMGKNGYERVKEMFLEHHMSHRIASVLK 366
Cdd:PRK15484  324 HLAEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWEGVTQRFEEQIH 376
 
Name Accession Description Interval E-value
Glyco_trans_4_5 pfam16994
Glycosyl-transferase family 4;
1-159 4.41e-66

Glycosyl-transferase family 4;


Pssm-ID: 465332  Cd Length: 172  Bit Score: 206.98  E-value: 4.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079   1 MELAFLLRGVGADVVWITNQKPLEddevvysLEHKMLDRGVQVISAKGQKAVDTSLKADLIVLNTAVAGKWLDAVLKENV 80
Cdd:pfam16994  22 MELATELRSCGATVVVVVLSKGGG-------LEQELLRRGIKVLPDKGRLSFRTALKADLVIANTAVCASWIDQYLKEHV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079  81 VKVLPKILWWIHEMRGHYF-----NADLVKHLPFvagamiDSHATAGYWKNRTQARLGIKMPKTYVVHLGNSKELMEVAE 155
Cdd:pfam16994  95 AGVLPKVLWWIHENRRHYFdraksMLDYVKHLPF------LSHSQAEQWLTWTEEELIILMPQTYVVHLSNNDELYFVAE 168

                  ....
gi 1063695079 156 DSVA 159
Cdd:pfam16994 169 ISVS 172
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
1-366 9.78e-41

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: 147.30  E-value: 9.78e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079   1 MELAFLLRGVGADVVWITNQKPLEDDEVVYSLEHKMLDRGVQVISAKGQ-----KAVDTSLKADLIVLNTAVAGKWLDAV 75
Cdd:cd03801    21 RELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelRPLLRLRKFDVVHAHGLLAALLAALL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079  76 LKENVVKvlpkILWWIHEMRGHYFNADLVKHLPFVAGAMIDSH------ATAGYWKNRTQARLGIKMPKTYVVHLGnske 149
Cdd:cd03801   101 ALLLGAP----LVVTLHGAEPGRLLLLLAAERRLLARAEALLRradaviAVSEALRDELRALGGIPPEKIVVIPNG---- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 150 lmevaedsVAKRVLREHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIkekklqvPTMHAVVVGSDmskqT 229
Cdd:cd03801   173 --------VDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRG-------PDVRLVIVGGD----G 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 230 KFETELRNfvREKKLENFVHFVNKTL--TVAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNG 307
Cdd:cd03801   234 PLRAELEE--LELGLGDRVRFLGFVPdeELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDG 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063695079 308 TTGLLHSAGKegVIPLAKNIVKLATQVELRLRMGKNGYERVKEMFLEHHMSHRIASVLK 366
Cdd:cd03801   310 EGGLVVPPDD--VEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
131-361 4.85e-23

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: 98.82  E-value: 4.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 131 RLGIKMPKTYVVHLGNSKELMEvaedsvakrvlREHVRESLgvRNEDLLFGIINSVSRGKGQDLFLRAFheslERIKEKK 210
Cdd:cd03808   156 KKGIIKKKKTVLIPGSGVDLDR-----------FQYSPESL--PSEKVVFLFVARLLKDKGIDELIEAA----KILKKKG 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 211 LQVptmHAVVVGSdmskqtkFETELRNFVREKKL--ENFVHFVNKTLTVAPYIAAIDVLVQNSqaRGECFGRITIEAMAF 288
Cdd:cd03808   219 PNV---RFLLVGD-------GELENPSEILIEKLglEGRIEFLGFRSDVPELLAESDVFVLPS--YREGLPRSLLEAMAA 286
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063695079 289 KLPVLGTAAGGTMEIVVNGTTGLLhsAGKEGVIPLAKNIVKLATQVELRLRMGKNGYERVKEMFLEHHMSHRI 361
Cdd:cd03808   287 GRPVITTDVPGCRELVIDGVNGFL--VPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
168-353 2.61e-19

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: 87.80  E-value: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 168 RESLGVRNEDLLFGIINSVSRGKGQDLFLRAfhesLERIKEKklqvPTMHAVVVGSDMSkqtkfETELRNFVREKKLENF 247
Cdd:cd03819   173 RAQLGLPEGKPVVGYVGRLSPEKGWLLLVDA----AAELKDE----PDFRLLVAGDGPE-----RDEIRRLVERLGLRDR 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 248 VHFVNKTLTVAPYIAAIDVLVqnSQARGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGkeGVIPLAKNI 327
Cdd:cd03819   240 VTFTGFREDVPAALAASDVVV--LPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPG--DAEALADAI 315
                         170       180
                  ....*....|....*....|....*...
gi 1063695079 328 VKLATQVELRLRMGKNGY--ERVKEMFL 353
Cdd:cd03819   316 RAAKLLPEAREKLQAAAAltEAVRELLL 343
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
260-370 5.24e-18

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 79.26  E-value: 5.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 260 YIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGkeGVIPLAKNIVKLATQVELRLR 339
Cdd:COG0438    17 LLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPG--DPEALAEAILRLLEDPELRRR 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063695079 340 MGKNGYERVKEMFLEHHMSHRIASVLKEVLQ 370
Cdd:COG0438    93 LGEAARERAEERFSWEAIAERLLALYEELLA 123
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
187-343 6.27e-16

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: 78.17  E-value: 6.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 187 SRGKGQDLFLRAFHESLERIKEKKLqvptmHAVVVGSDmskqtkfETELRNFVREKKLENFVHFVNKTLTVAPYIAAIDV 266
Cdd:cd03811   198 DPQKGHDLLIEAFAKLRKKYPDVKL-----VILGDGPL-------REELEKLAKELGLAERVIFLGFQSNPYPYLKKADL 265
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063695079 267 LVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAG-KEGVIPLAKNIVKLATQVELRLRMGKN 343
Cdd:cd03811   266 FVLSS--RYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGdAAALAGILAALLQKKLDAALRERLAKA 341
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
168-366 7.93e-16

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: 77.74  E-value: 7.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 168 RESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIkekklqvPTMHAVVVGSDMSKQtkfetELRNFVREKKLENF 247
Cdd:cd03807   181 RRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETH-------PDLRLLLVGRGPERP-----NLERLLLELGLEDR 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 248 VHFVNKTLTVAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGtTGLLHSAGKegVIPLAKNI 327
Cdd:cd03807   249 VHLLGERSDVPALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGD--PQALADAI 323
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063695079 328 VKLATQVELRLRMGKNGYERVKEMFLEHHMSHRIASVLK 366
Cdd:cd03807   324 RALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
176-347 4.09e-15

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: 72.31  E-value: 4.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 176 EDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKLqvptmhaVVVGsdmskQTKFETELRNFVREKKLENFVHFVNKTL 255
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKL-------VIAG-----DGEEEKRLKKLAEKLGLGDNVIFLGFVS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 256 TVAP--YIAAIDVLVQNSQArgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLhsagkegVIP-----LAKNIV 328
Cdd:pfam00534  69 DEDLpeLLKIADVFVLPSRY--EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFL-------VKPnnaeaLAEAID 139
                         170
                  ....*....|....*....
gi 1063695079 329 KLATQVELRLRMGKNGYER 347
Cdd:pfam00534 140 KLLEDEELRERLGENARKR 158
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
190-352 2.03e-14

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: 73.81  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 190 KGQDLFLRAFHESLERIKEKKLqvptmhAVVVGSDMSKQTKFETELRNFVREKKLE---NFVHFVNKTlTVAPYIAAIDV 266
Cdd:cd03800   233 KGIDTLVRAFAQLPELRELANL------VLVGGPSDDPLSMDREELAELAEELGLIdrvRFPGRVSRD-DLPELYRAADV 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 267 LVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLL---HSAGKegvipLAKNIVKLATQVELRLRMGKN 343
Cdd:cd03800   306 FVVPS--LYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLvdpHDPEA-----LAAALRRLLDDPALWQRLSRA 378

                  ....*....
gi 1063695079 344 GYERVKEMF 352
Cdd:cd03800   379 GLERARAHY 387
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
190-312 2.25e-14

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 69.46  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 190 KGQDLFLRAFHesleRIKEKKLQVptmHAVVVGSDMSKqtkfetELRNfvREKKLENFVHFVNKTLTVAPYIAAIDVLVQ 269
Cdd:pfam13692  15 KGVDYLLEAVP----LLRKRDNDV---RLVIVGDGPEE------ELEE--LAAGLEDRVIFTGFVEDLAELLAAADVFVL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063695079 270 NSQARGecFGRITIEAMAFKLPVLGTAAGGTMEIvVNGTTGLL 312
Cdd:pfam13692  80 PSLYEG--FGLKLLEAMAAGLPVVATDVGGIPEL-VDGENGLL 119
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
190-350 2.51e-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: 73.43  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 190 KGQDLFLRAFHESLERIKEKKLqvptmHAVVVGSDmskqtkfETELRNFVREKKLENFVHFVNKTLTVAPYIAAIDVLVQ 269
Cdd:cd03820   194 KGFDLLIEAWALIAKKHPDWKL-----RIYGDGPE-------REELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVL 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 270 NSqaRGECFGRITIEAMAFKLPVLGTAA-GGTMEIVVNGTTGLLHSAGKegVIPLAKNIVKLATQVELRLRMGKNGYERV 348
Cdd:cd03820   262 SS--RYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENGLLVPNGD--VDALAEALLRLMEDEELRKKMGKNARKNA 337

                  ..
gi 1063695079 349 KE 350
Cdd:cd03820   338 ER 339
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
155-368 3.51e-13

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: 70.00  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 155 EDSVAKRVLREHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERikekklqvPTMHAVVVGSDmskqtKFETE 234
Cdd:cd03817   179 DLDKFEKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE--------PNIKLVIVGDG-----PEREE 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 235 LRNFVREKKLE---NFVHFVNKTLTVAPYIAAiDVLVQNSQArgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGL 311
Cdd:cd03817   246 LKELARELGLAdkvIFTGFVPREELPEYYKAA-DLFVFASTT--ETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGF 322
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063695079 312 LHsagKEGVIPLAKNIVKLATQVELRLRMGKNGYERVkemfLEHHMSHRIASVLKEV 368
Cdd:cd03817   323 LF---EPNDETLAEKLLHLRENLELLRKLSKNAEISA----REFAFAKSVEKLYEEV 372
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
169-312 1.06e-12

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: 68.56  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 169 ESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHeSLERikekklQVPTMHAVVVGSDMSKQTkfeteLRNFVREKKLENFV 248
Cdd:cd03798   192 RGLGLPLDAFVILFVGRLIPRKGIDLLLEAFA-RLAK------ARPDVVLLIVGDGPLREA-----LRALAEDLGLGDRV 259
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063695079 249 HFVNkTLT---VAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLL 312
Cdd:cd03798   260 TFTG-RLPheqVPAYYRACDVFVLPS--RHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLL 323
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
155-352 1.78e-12

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: 67.76  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 155 EDSVAKRVLREHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKLQVPTmhavvvGSDMSkqtkfetE 234
Cdd:cd04962   174 DEDVFKRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPAKLLLVGD------GPERV-------P 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 235 LRNFVREKKLENFVHFVNKTLTVAPYIAAIDVLVQNSQArgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHS 314
Cdd:cd04962   241 AEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEK--ESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSD 318
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063695079 315 AGKegVIPLAKNIVKLATQVELRLRMGKNGYERVKEMF 352
Cdd:cd04962   319 VGD--VDAMAKSALSILEDDELYNRMGRAARKRAAERF 354
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
120-357 5.97e-12

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 66.59  E-value: 5.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 120 TAGYWKNRT-QARLGIKMPKTYVVHLGnskelMEVAEDSVAKRVLREHvreslgvrnEDLLFGIINSVSRGKGQDLFLRA 198
Cdd:cd03813   249 ISLYEGNRRrQIRLGADPDKTRVIPNG-----IDIQRFAPAREERPEK---------EPPVVGLVGRVVPIKDVKTFIRA 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 199 FHESLERIKEKKLQVptmhavvVGSDMSKQtKFETELRNFVREKKLEN---FVHFVNktltVAPYIAAIDVLVQNSQARG 275
Cdd:cd03813   315 FKLVRRAMPDAEGWL-------IGPEDEDP-EYAQECKRLVASLGLENkvkFLGFQN----IKEYYPKLGLLVLTSISEG 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 276 ecFGRITIEAMAFKLPVLGTAAGGTMEIVvNGTTGLLHSAGKegVIP------LAKNIVKLATQVELRLRMGKNGYERVK 349
Cdd:cd03813   383 --QPLVILEAMASGVPVVATDVGSCRELI-YGADDALGQAGL--VVPpadpeaLAEALIKLLRDPELRQAFGEAGRKRVE 457

                  ....*...
gi 1063695079 350 EMFLEHHM 357
Cdd:cd03813   458 KYYTLEGM 465
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
189-362 7.65e-12

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: 66.21  E-value: 7.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 189 GKGQDLflRAFHESLERIKEKklqvPTMHAVVVGSDMSKQtkfetELRNFVREKKLENFVHF--VNKTlTVAPYIAAIDV 266
Cdd:cd03794   227 GKAQGL--ETLLEAAERLKRR----PDIRFLFVGDGDEKE-----RLKELAKARGLDNVTFLgrVPKE-EVPELLSAADV 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 267 LVQnSQARGECFGRI----TIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGKEGVipLAKNIVKLATQVELRLRMGK 342
Cdd:cd03794   295 GLV-PLKDNPANRGSspskLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEA--LADAILELLDDPELRRAMGE 371
                         170       180
                  ....*....|....*....|
gi 1063695079 343 NGYERVKEMFLEHHMSHRIA 362
Cdd:cd03794   372 NGRELAEEKFSREKLADRLL 391
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
234-358 1.70e-11

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 64.99  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 234 ELRNFVREKKLEN--FVHFVNKTLTVAPYIAAiDVLVQNSQARGECFGRITIEAMAFKLPVLGTA-AGGTMEIVVNGTTG 310
Cdd:cd03795   231 DLEAQIELNLLDNvkFLGRVDDEEKVIYLHLC-DVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNGETG 309
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063695079 311 LlhsagkegVIP------LAKNIVKLATQVELRLRMGKNGYERVKEMFLEHHMS 358
Cdd:cd03795   310 L--------VVPpkdpdaLAEAIDKLLSDEELRESYGENAKKRFEELFTAEKMK 355
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
183-361 8.09e-11

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 62.99  E-value: 8.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 183 INSVSRGKGQDLFLRAFHESLERIKEKKlqvpTMHAVVVGSDMSKQTK----FEtELRNFVREKK-LENFVHFvnktltv 257
Cdd:cd03805   217 INRFERKKNIALAIEAFAKLKQKLPEFE----NVRLVIAGGYDPRVAEnveyLE-ELQRLAEELLnVEDQVLF------- 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 258 apyIAAI-----DVLVQNSQA-----RGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGKEGvipLAKNI 327
Cdd:cd03805   285 ---LRSIsdsqkEQLLSSALAllytpSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEA---FAEAM 358
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063695079 328 VKLATQVELRLRMGKNGYERVKEMFLEHHMSHRI 361
Cdd:cd03805   359 LKLANDPDLADRMGAAGRKRVKEKFSREAFAERL 392
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
165-351 1.91e-09

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 58.46  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 165 EHVRESLGVrNEDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKlqvptmhaVVVGSDMSKQtkfETELRN----FVR 240
Cdd:cd03814   187 AALRRRLGP-PGRPLLLYVGRLAPEKNLEALLDADLPLAASPPVRL--------VVVGDGPARA---ELEARGpdviFTG 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 241 EKKLEnfvhfvnktlTVAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGKEGV 320
Cdd:cd03814   255 FLTGE----------ELARAYASADVFVFPS--RTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAA 322
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063695079 321 ipLAKNIVKLATQVELRLRMGKNGYERVKEM 351
Cdd:cd03814   323 --FAAALRALLEDPELRRRMAARARAEAERY 351
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
167-349 2.24e-09

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: 58.49  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 167 VRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFheslerikeKKLQVPTMHAVVVGSDMSKQTKFetelrnfvreKKLEN 246
Cdd:cd03823   181 PPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAF---------KRLPREDIELVIAGHGPLSDERQ----------IEGGR 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 247 FVHFVNK--TLTVAPYIAAIDVLVQNSQARgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGKegVIPLA 324
Cdd:cd03823   242 RIAFLGRvpTDDIKDFYEKIDVLVVPSIWP-EPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGD--AEDLA 318
                         170       180
                  ....*....|....*....|....*
gi 1063695079 325 KNIVKLATQVELRLRMGKNGYERVK 349
Cdd:cd03823   319 AAMRRLLTDPALLERLRAGAEPPRS 343
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
120-313 1.80e-08

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: 54.72  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 120 TAGYWKNRTQARLGIKMPktYVVHLGNSKELMevaedsvaKRVLREHVRESLGVRNEDLLFgiINSVSRGKGQDLFLRAF 199
Cdd:cd01635    65 AAALAALLAARLLGIPIV--VTVHGPDSLEST--------RSELLALARLLVSLPLADKVS--VGRLVPEKGIDLLLEAL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 200 HESLERIKEKKLqvptmhaVVVGSDMSKQTKFEtELRNFVREKKLENFVHFVNKTLTVApYIAAIDVLVQNSQARGecFG 279
Cdd:cd01635   133 ALLKARLPDLVL-------VLVGGGGEREEEEA-LAAALGLLERVVIIGGLVDDEVLEL-LLAAADVFVLPSRSEG--FG 201
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063695079 280 RITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLH 313
Cdd:cd01635   202 LVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
164-304 2.37e-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: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 164 REHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKLqvptmhaVVVGSDMSKQtkfetELRNFVREKK 243
Cdd:cd04951   175 RLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKL-------LIAGDGPLRN-----ELERLICNLN 242
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063695079 244 LENFVHFVNKTLTVAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIV 304
Cdd:cd04951   243 LVDRVILLGQISNISEYYNAADLFVLSS--EWEGFGLVVAEAMACERPVVATDAGGVAEVV 301
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
181-353 5.19e-08

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: 54.25  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 181 GIINSVSR---GKGQDLFLRAFHESLERIKEKKLqvptmhaVVVGSDMSKQTKFETELRNFVREKKLENFVHFVN---KT 254
Cdd:cd03792   198 PYILQVARfdpSKDPLGVIDAYKLFKRRAEEPQL-------VICGHGAVDDPEGSVVYEEVMEYAGDDHDIHVLRlppSD 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 255 LTVAPYIAAIDVLVQNSqaRGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGKEgvipLAKNIVKLATQV 334
Cdd:cd03792   271 QEINALQRAATVVLQLS--TREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEG----AAVRILRLLTDP 344
                         170
                  ....*....|....*....
gi 1063695079 335 ELRLRMGKNGYERVKEMFL 353
Cdd:cd03792   345 ELRRKMGLAAREHVRDNFL 363
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
160-366 1.37e-07

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 52.87  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 160 KRVLREHVRESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKLqvptmhaVVVGSDMSKQTKFETELRNFV 239
Cdd:PRK15484  176 QSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKL-------VVVGDPTASSKGEKAAYQKKV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 240 RE--KKLENFVHFVNktlTVAP-----YIAAIDVLVQNSQARgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGlL 312
Cdd:PRK15484  249 LEaaKRIGDRCIMLG---GQPPekmhnYYPLADLVVVPSQVE-EAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITG-Y 323
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063695079 313 HSAGKEGVIPLAKNIVKLATQVElRLRMGKNGYERVKEMFLEHHMSHRIASVLK 366
Cdd:PRK15484  324 HLAEPMTSDSIISDINRTLADPE-LTQIAEQAKDFVFSKYSWEGVTQRFEEQIH 376
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
164-368 1.45e-06

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 49.64  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 164 REHVRESLGVRNED--LLFGIINSVSRGKGQDLFLRAfhesLERI-KEKKLQVptmhaVVVGSDMSKQTKFETELRNFVR 240
Cdd:cd03825   180 KAKARKRLGIPQDKkvILFGAESVTKPRKGFDELIEA----LKLLaTKDDLLL-----VVFGKNDPQIVILPFDIISLGY 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 241 EKklenfvhfvNKTLTVAPYIAAiDVLVQNSQArgECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLhsAGKEGV 320
Cdd:cd03825   251 ID---------DDEQLVDIYSAA-DLFVHPSLA--DNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYL--VPPGDV 316
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1063695079 321 IPLAKNIVKLATQVELRLRMGKNGYERVKEMFLEHHMSHRIASVLKEV 368
Cdd:cd03825   317 QALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
116-349 3.34e-06

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 48.51  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 116 DSHATagywKNRTQARLGIKMPKTYVVHLGnskelmevAEDSVAKRVLREHVRESLGVRNEDLLFgiINSVSRGKGQDLF 195
Cdd:cd03809   145 VSEAT----RDDIIKFYGVPPEKIVVIPLG--------VDPSFFPPESAAVLIAKYLLPEPYFLY--VGTLEPRKNHERL 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 196 LRAFheslERIKEKKLQVPTmhaVVVGSdmsKQTKFEtELRNFVREKKLENFVHFVNktltvapYIAAIDV--LVQNSQA 273
Cdd:cd03809   211 LKAF----ALLKKQGGDLKL---VIVGG---KGWEDE-ELLDLVKKLGLGGRVRFLG-------YVSDEDLpaLYRGARA 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 274 -----RGECFGRITIEAMAFKLPVLGTAAGGTMEIVvnGTTGLLHSAGKegVIPLAKNIVKLATQVELRLRMGKNGYERV 348
Cdd:cd03809   273 fvfpsLYEGFGLPVLEAMACGTPVIASNISVLPEVA--GDAALYFDPLD--PESIADAILRLLEDPSLREELIRKGLERA 348

                  .
gi 1063695079 349 K 349
Cdd:cd03809   349 K 349
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
262-350 3.60e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 48.55  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 262 AAIDVLVQNSQArgECFGRITIEAMAFKLPVLGTAAGGTMEIVVN---GTTGLLHSAGKegVIPLAKNIVKLATQVELRL 338
Cdd:PLN02871  330 ASGDVFVMPSES--ETLGFVVLEAMASGVPVVAARAGGIPDIIPPdqeGKTGFLYTPGD--VDDCVEKLETLLADPELRE 405
                          90
                  ....*....|..
gi 1063695079 339 RMGKNGYERVKE 350
Cdd:PLN02871  406 RMGAAAREEVEK 417
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
274-352 1.84e-05

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: 46.29  E-value: 1.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063695079 274 RGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGKegVIPLAKNIVKLATQVELRLRMGKNGYERVKEMF 352
Cdd:cd05844   277 DSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGD--VDALADALQALLADRALADRMGGAARAFVCEQF 353
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
270-365 8.93e-05

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 41.05  E-value: 8.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 270 NSQARGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLLHSAGKEgvipLAKNIVKLATQVELRLRMGKNGYERVK 349
Cdd:pfam13524   4 NPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEE----LAEKIRYLLEHPEERRAIAAAGRERVL 79
                          90
                  ....*....|....*.
gi 1063695079 350 EmflEHHMSHRIASVL 365
Cdd:pfam13524  80 A---EHTYAHRAEQLL 92
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
168-293 1.64e-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: 43.43  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 168 RESLGVRNEDLLFGIINSVSRGKGQDLFLRAFHESLERIKEKKLqvptmhaVVVGsdmskQTKFETELRNFVREKKLENF 247
Cdd:cd03812   182 RRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKL-------VLVG-----EGELKEKIKEKVKELGLEDK 249
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063695079 248 VHFVNKTLTVAPYIAAIDVLVQNSQARGecFGRITIEAMAFKLPVL 293
Cdd:cd03812   250 VIFLGFRNDVSEILSAMDVFLFPSLYEG--LPLVAVEAQASGLPCL 293
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
276-312 2.85e-04

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: 42.27  E-value: 2.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1063695079 276 ECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLL 312
Cdd:cd03802   251 EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFL 287
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
284-355 8.14e-04

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 40.90  E-value: 8.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063695079 284 EAMAFKLPVLGTAAGGTMEIVVNGTTGLLhsAGKEGVIPLAKNIVKLATQVELRLRMGKNGYERVKEMFLEH 355
Cdd:cd03799   275 EAMAMGLPVISTEHGGIPELVEDGVSGFL--VPERDAEAIAEKLTYLIEHPAIWPEMGKAGRARVEEEYDIN 344
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
241-312 9.85e-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: 40.91  E-value: 9.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063695079 241 EKKLEN----FVHFVNKTLTVAPYIA-AIDVLVQNSQARGEcfgRITI-EAMAFKLPVLGTAAGGTMEIVVNGTTGLL 312
Cdd:cd04946   277 ENKLENvkvnFTGEVSNKEVKQLYKEnDVDVFVNVSESEGI---PVSImEAISFGIPVIATNVGGTREIVENETNGLL 351
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
182-358 1.77e-03

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: 39.98  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 182 IINSVSR---GKGQDLFLRAFHESLERIKEKKLqvptmHAVVVGSDMSKQTKFETELrnfvrekKLENFVHFVNKTLTVA 258
Cdd:cd04949   162 KIITISRlapEKQLDHLIEAVAKAVKKVPEITL-----DIYGYGEEREKLKKLIEEL-------HLEDNVFLKGYHSNLD 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 259 PYIAAIDVLVQNSQARGecFGRITIEAMAFKLPVLGTAAG-GTMEIVVNGTTGLLhsAGKEGVIPLAKNIVKLATQVELR 337
Cdd:cd04949   230 QEYQDAYLSLLTSQMEG--FGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYL--IEKNNIDALADKIIELLNDPEKL 305
                         170       180
                  ....*....|....*....|.
gi 1063695079 338 LRMGKNGYERVKEMFLEHHMS 358
Cdd:cd04949   306 QQFSEESYKIAEKYSTENVME 326
PLN00142 PLN00142
sucrose synthase
260-310 2.82e-03

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 39.96  E-value: 2.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063695079 260 YIA-AIDVLVQnsQARGECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTG 310
Cdd:PLN00142  662 YIAdTKGAFVQ--PALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSG 711
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
130-312 3.33e-03

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 39.19  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 130 ARLGIKMPKTYVVHLGNSKELMEVAEDSVAKRVLREHVRES--------------LGVRNEDLLfgiinSVSR---GKGQ 192
Cdd:cd03804   140 ASLFLHYLRLWDVRTAQRVDLFIANSQFVARRIKKFYGREStviyppvdtdafapAADKEDYYL-----TASRlvpYKRI 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 193 DLFLRAFHESlerikEKKLqvptmhaVVVGS--DMSKqtkfeteLRNFVRekklenfvhfvnKTLTVAPYIAAIDVLVQN 270
Cdd:cd03804   215 DLAVEAFNEL-----PKRL-------VVIGDgpDLDR-------LRAMAS------------PNVEFLGYQPDEVLKELL 263
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1063695079 271 SQARG------ECFGRITIEAMAFKLPVLGTAAGGTMEIVVNGTTGLL 312
Cdd:cd03804   264 SKARAfvfaaeEDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGIL 311
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
190-312 4.06e-03

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 39.13  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063695079 190 KGQDLFLRAFHESLERIKEKKLQVPTMhaVVVGSDMSKQ-TKFETELRNFVREKKLENFVHFVnktlTVAPYiaaIDVLV 268
Cdd:cd03806   250 KNHPLQLRAFAELLKRLPESIRSNPKL--VLIGSCRNEEdKERVEALKLLAKELILEDSVEFV----VDAPY---EELKE 320
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063695079 269 QNSQAR-------GECFGrITI-EAMAFKLPVLGTAAGG-TMEIVVN---GTTGLL 312
Cdd:cd03806   321 LLSTASiglhtmwNEHFG-IGVvEYMAAGLIPLAHASAGpLLDIVVPwdgGPTGFL 375
 
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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