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Conserved domains on  [gi|488277556|ref|WP_002348764|]
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MULTISPECIES: glycosyltransferase family 8 protein [Enterococcus]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 11444513)

glycosyltransferase family 8 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Escherichia coli lipopolysaccharide 1,2-glucosyltransferase, which adds the glucose(II) group on the galactose(I) group of LPS

CATH:  3.90.550.10
CAZY:  GT8
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
4-271 6.43e-78

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 238.33  E-value: 6.43e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556   4 DEQIELLFTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTDYLQFGFEAIKIDGSRWNSAKTEDR 83
Cdd:COG1442    3 KNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  84 YPKEMYFRLLAGEILPKEMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDV-STRVNQMRLDVDHAYYNSGV 162
Cdd:COG1442   83 ISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSqKKRAKRLGLPDDDGYFNSGV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 163 MVIDLDKAREIIKWSDIAQMIEKYNLLLILPDQDILNRLYGKYTKEIPEEiWNYDTRKYMRYFTKSlAQHDIHWVMAHTA 242
Cdd:COG1442  163 LLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPR-YNYQYSLYYELKDKS-NKKELLEARKNPV 240
                        250       260
                 ....*....|....*....|....*....
gi 488277556 243 ILHFCGGPKPWDDKHDNRFTSLYLTYQNQ 271
Cdd:COG1442  241 IIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
4-271 6.43e-78

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 238.33  E-value: 6.43e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556   4 DEQIELLFTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTDYLQFGFEAIKIDGSRWNSAKTEDR 83
Cdd:COG1442    3 KNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  84 YPKEMYFRLLAGEILPKEMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDV-STRVNQMRLDVDHAYYNSGV 162
Cdd:COG1442   83 ISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSqKKRAKRLGLPDDDGYFNSGV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 163 MVIDLDKAREIIKWSDIAQMIEKYNLLLILPDQDILNRLYGKYTKEIPEEiWNYDTRKYMRYFTKSlAQHDIHWVMAHTA 242
Cdd:COG1442  163 LLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPR-YNYQYSLYYELKDKS-NKKELLEARKNPV 240
                        250       260
                 ....*....|....*....|....*....
gi 488277556 243 ILHFCGGPKPWDDKHDNRFTSLYLTYQNQ 271
Cdd:COG1442  241 IIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
9-255 2.21e-66

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 207.07  E-value: 2.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556   9 LLFTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTDYLQFGFEAIKIDGSRWNSAK-TEDRYPKE 87
Cdd:cd04194    3 IVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHISYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  88 MYFRLLAGEILPKEmKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDVSTRVNQMRLDVDHAYYNSGVMVIDL 167
Cdd:cd04194   83 TYYRLLIPDLLPDY-DKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLINL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 168 DKAREIIKWSDIAQMIEKYNLLLILPDQDILNRLYGKYTKEIPEEiWNYDTRKYMRYFTKSLAQHDIHWVMAHTAILHFC 247
Cdd:cd04194  162 KKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPR-YNFQTGFYYLLKKKSKEEQELEEARKNPVIIHYT 240

                 ....*...
gi 488277556 248 GGPKPWDD 255
Cdd:cd04194  241 GSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
9-255 1.31e-30

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 114.73  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556    9 LLFTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTdyLQFG-------FEAIKIDGSRWNSAKTE 81
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLA--SSYKpvlplleSDIKIFEYFSKLKLRSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556   82 DRYPKEMYFRLLAGEILPKeMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDVSTRVNQMRL---DVDHAYY 158
Cdd:pfam01501  80 KYWSLLNYLRLYLPDLFPK-LDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYFQRYPNFSEPIILenfGPPACYF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  159 NSGVMVIDLDKARE------IIKWsdiaQMIEKYNLLLILPDQDILNRLYGKYTKEIPEEiWNydtrkyMRYFTKSLAQH 232
Cdd:pfam01501 159 NAGMLLFDLDAWRKeniterYIKW----LNLNENRTLWKLGDQDPLNIVFYGKVKPLDPR-WN------VLGLGYYNKKK 227
                         250       260
                  ....*....|....*....|...
gi 488277556  233 DIHWVMAHTAILHFCGGPKPWDD 255
Cdd:pfam01501 228 SLNEITENAAVIHYNGPTKPWLD 250
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
11-253 3.97e-11

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 62.46  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  11 FTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTDYLQFGFEAIKIDGSRWNSAKTEDRYPKEMYF 90
Cdd:PRK15171  30 YGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCERLKSLPSTKNWTYATYF 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  91 RLLAGEILPKEMKRVIYLDPDILV---VNPLLDLwqtDLEGYMLAAATHVGLTD------VSTRVNQMrldvDHAYYNSG 161
Cdd:PRK15171 110 RFIIADYFIDKTDKVLYLDADIACkgsIKELIDL---DFAENEIAAVVAEGDAEwwskraQSLQTPGL----ASGYFNSG 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 162 VMVIDLD---------KAREIIKWSDIAQMIEKynlllilPDQDILNRLYGKYTKEIPEeiwNYDTRKYMRYFTKSLAqh 232
Cdd:PRK15171 183 FLLINIPawaqenisaKAIEMLADPEIVSRITH-------LDQDVLNILLAGKVKFIDA---KYNTQFSLNYELKDSV-- 250
                        250       260
                 ....*....|....*....|.
gi 488277556 233 dIHWVMAHTAILHFCGGPKPW 253
Cdd:PRK15171 251 -INPVNDETVFIHYIGPTKPW 270
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
4-271 6.43e-78

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 238.33  E-value: 6.43e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556   4 DEQIELLFTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTDYLQFGFEAIKIDGSRWNSAKTEDR 83
Cdd:COG1442    3 KNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  84 YPKEMYFRLLAGEILPKEMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDV-STRVNQMRLDVDHAYYNSGV 162
Cdd:COG1442   83 ISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSqKKRAKRLGLPDDDGYFNSGV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 163 MVIDLDKAREIIKWSDIAQMIEKYNLLLILPDQDILNRLYGKYTKEIPEEiWNYDTRKYMRYFTKSlAQHDIHWVMAHTA 242
Cdd:COG1442  163 LLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPR-YNYQYSLYYELKDKS-NKKELLEARKNPV 240
                        250       260
                 ....*....|....*....|....*....
gi 488277556 243 ILHFCGGPKPWDDKHDNRFTSLYLTYQNQ 271
Cdd:COG1442  241 IIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
9-255 2.21e-66

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 207.07  E-value: 2.21e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556   9 LLFTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTDYLQFGFEAIKIDGSRWNSAK-TEDRYPKE 87
Cdd:cd04194    3 IVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHISYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  88 MYFRLLAGEILPKEmKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDVSTRVNQMRLDVDHAYYNSGVMVIDL 167
Cdd:cd04194   83 TYYRLLIPDLLPDY-DKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLINL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 168 DKAREIIKWSDIAQMIEKYNLLLILPDQDILNRLYGKYTKEIPEEiWNYDTRKYMRYFTKSLAQHDIHWVMAHTAILHFC 247
Cdd:cd04194  162 KKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPR-YNFQTGFYYLLKKKSKEEQELEEARKNPVIIHYT 240

                 ....*...
gi 488277556 248 GGPKPWDD 255
Cdd:cd04194  241 GSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
9-255 1.31e-30

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 114.73  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556    9 LLFTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTdyLQFG-------FEAIKIDGSRWNSAKTE 81
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLA--SSYKpvlplleSDIKIFEYFSKLKLRSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556   82 DRYPKEMYFRLLAGEILPKeMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDVSTRVNQMRL---DVDHAYY 158
Cdd:pfam01501  80 KYWSLLNYLRLYLPDLFPK-LDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYFQRYPNFSEPIILenfGPPACYF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  159 NSGVMVIDLDKARE------IIKWsdiaQMIEKYNLLLILPDQDILNRLYGKYTKEIPEEiWNydtrkyMRYFTKSLAQH 232
Cdd:pfam01501 159 NAGMLLFDLDAWRKeniterYIKW----LNLNENRTLWKLGDQDPLNIVFYGKVKPLDPR-WN------VLGLGYYNKKK 227
                         250       260
                  ....*....|....*....|...
gi 488277556  233 DIHWVMAHTAILHFCGGPKPWDD 255
Cdd:pfam01501 228 SLNEITENAAVIHYNGPTKPWLD 250
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
14-254 1.57e-19

Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.


Pssm-ID: 132996 [Multi-domain]  Cd Length: 246  Bit Score: 85.19  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  14 DEGYLNPLKVALTSIRQNNPgQAFRIWLIHESIAmHTIRELQKLTDYLQ-FGFEAIKIDGSRWNSAKTEDRYPKEM-YFR 91
Cdd:cd00505    9 GDEYLRGAIVLMKSVLRHRT-KPLRFHVLTNPLS-DTFKAALDNLRKLYnFNYELIPVDILDSVDSEHLKRPIKIVtLTK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  92 LLAGEILPkEMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLTDVSTRVNQMRLDVDHAYY-NSGVMVIDLDKA 170
Cdd:cd00505   87 LHLPNLVP-DYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGKYYRQKRSHLAGPDYfNSGVFVVNLSKE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 171 REIIKWSDIAQMIEKYNLLLILPDQDILNRLYgkytKEIPEEI------WNY---DTRKYMRYFTKSLAQhdihwvmahT 241
Cdd:cd00505  166 RRNQLLKVALEKWLQSLSSLSGGDQDLLNTFF----KQVPFIVkslpciWNVrltGCYRSLNCFKAFVKN---------A 232
                        250
                 ....*....|...
gi 488277556 242 AILHFCGGPKPWD 254
Cdd:cd00505  233 KVIHFNGPTKPWN 245
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
101-254 7.41e-12

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 63.82  E-value: 7.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 101 EMKRVIYLDPDILVVNPLLDLWqtDLEGYmLAAATHVGLTDvstrvnqmrldvdhaYYNSGVMVI--DLDKAREIIkwsD 178
Cdd:cd02537   89 EYDKVVFLDADTLVLRNIDELF--DLPGE-FAAAPDCGWPD---------------LFNSGVFVLkpSEETFNDLL---D 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 179 IAQMIEKYNllliLPDQDILNrlygKYTKEIPeeIWN-----YDTRKYMRYFTKSlaqhdIHWVMAHTAILHFCGGPKPW 253
Cdd:cd02537  148 ALQDTPSFD----GGDQGLLN----SYFSDRG--IWKrlpftYNALKPLRYLHPE-----ALWFGDEIKVVHFIGGDKPW 212

                 .
gi 488277556 254 D 254
Cdd:cd02537  213 S 213
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
11-253 3.97e-11

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 62.46  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  11 FTIDEGYLNPLKVALTSIRQNNPGQAFRIWLIHESIAMHTIRELQKLTDYLQFGFEAIKIDGSRWNSAKTEDRYPKEMYF 90
Cdd:PRK15171  30 YGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCERLKSLPSTKNWTYATYF 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  91 RLLAGEILPKEMKRVIYLDPDILV---VNPLLDLwqtDLEGYMLAAATHVGLTD------VSTRVNQMrldvDHAYYNSG 161
Cdd:PRK15171 110 RFIIADYFIDKTDKVLYLDADIACkgsIKELIDL---DFAENEIAAVVAEGDAEwwskraQSLQTPGL----ASGYFNSG 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 162 VMVIDLD---------KAREIIKWSDIAQMIEKynlllilPDQDILNRLYGKYTKEIPEeiwNYDTRKYMRYFTKSLAqh 232
Cdd:PRK15171 183 FLLINIPawaqenisaKAIEMLADPEIVSRITH-------LDQDVLNILLAGKVKFIDA---KYNTQFSLNYELKDSV-- 250
                        250       260
                 ....*....|....*....|.
gi 488277556 233 dIHWVMAHTAILHFCGGPKPW 253
Cdd:PRK15171 251 -INPVNDETVFIHYIGPTKPW 270
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
89-270 4.52e-07

GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.


Pssm-ID: 133051 [Multi-domain]  Cd Length: 257  Bit Score: 49.69  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  89 YFRLLAGEILPKeMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAathvgltdVSTRvnqmrldvdhayYNSGVMVIDLD 168
Cdd:cd06429  102 FARFYLPELFPK-LEKVIYLDDDVVVQKDLTELWNTDLGGGVAGA--------VETS------------WNPGVNVVNLT 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 169 KAR------EIIKWSDIAQMIEK-YNLLLILPDQDILnrLYGKYTKeiPEEIWN-----YDTRKYMRyFTKSlaqhdihw 236
Cdd:cd06429  161 EWRrqnvteTYEKWMELNQEEEVtLWKLITLPPGLIV--FYGLTSP--LDPSWHvrglgYNYGIRPQ-DIKA-------- 227
                        170       180       190
                 ....*....|....*....|....*....|....
gi 488277556 237 vmahTAILHFCGGPKPWDDKHDNRFTSLYLTYQN 270
Cdd:cd06429  228 ----AAVLHFNGNMKPWLRTAIPSYKELWEKYLS 257
GT8_LARGE_C cd06431
LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in ...
91-274 1.22e-06

LARGE catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis; The catalytic domain of LARGE is a putative glycosyltransferase. Mutations of LARGE in mouse and human cause dystroglycanopathies, a disease associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. LARGE needs to both physically interact with alpha-dystroglycan and function as a glycosyltransferase in order to stimulate alpha-dystroglycan hyperglycosylation. LARGE localizes to the Golgi apparatus and contains three conserved DxD motifs. While two of the motifs are indispensible for glycosylation function, one is important for localization of th eenzyme. LARGE was originally named because it covers approximately large trunck of genomic DNA, more than 600bp long. The predicted protein structure contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, and two putative catalytic domains. This catalytic domain has closest homology to GT8 glycosyltransferase involved in lipooligosaccharide synthesis.


Pssm-ID: 133053  Cd Length: 280  Bit Score: 48.62  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  91 RLLAGEILPKEMKRVIYLDPDILVVNPLLDLWQTdleGYMLAAATHVGLTDVSTRVNQMRLDVDHAY-------YNSGVM 163
Cdd:cd06431   87 KLVLTEALPSDLEKVIVLDTDITFATDIAELWKI---FHKFTGQQVLGLVENQSDWYLGNLWKNHRPwpalgrgFNTGVI 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556 164 VIDLDKAREiIKWSDIAQMIEKYNLLLI----LPDQDILNrlygKYTKEIPEEI------WNY---DTRKYMRYFTKSLA 230
Cdd:cd06431  164 LLDLDKLRK-MKWESMWRLTAERELMSMlstsLADQDIFN----AVIKQNPFLVyqlpcaWNVqlsDHTRSEQCYRDVSD 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 488277556 231 QHDIHWvmahtailhfcGGPKPWD--DKHDNRFTSLYLTYQ----NQLKR 274
Cdd:cd06431  239 LKVIHW-----------NSPKKLRvkNKHVEFFRNLYLTFLeydgNLLRR 277
PLN02769 PLN02769
Probable galacturonosyltransferase
96-172 1.23e-05

Probable galacturonosyltransferase


Pssm-ID: 215412 [Multi-domain]  Cd Length: 629  Bit Score: 46.23  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  96 EILPKeMKRVIYLDPDILVVNPLLDLWQTDLEGYMLAAATHVGLtdvstRVNQMRLDVDHAYYN-------SGVMVIDLD 168
Cdd:PLN02769 447 EIFKK-LKKVVVLDDDVVVQRDLSFLWNLDMGGKVNGAVQFCGV-----RLGQLKNYLGDTNFDtnscawmSGLNVIDLD 520

                 ....
gi 488277556 169 KARE 172
Cdd:PLN02769 521 KWRE 524
GT8_like_2 cd06430
GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of ...
91-216 8.74e-04

GT8_like_2 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.


Pssm-ID: 133052  Cd Length: 304  Bit Score: 40.14  E-value: 8.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488277556  91 RLLAGEILPkEMKRVIYLDPDILVVNPLLDLWQ--TDLEGYMLAA------ATHVGLTDVSTRvnqmrldvdHAYY---- 158
Cdd:cd06430   87 RLFLPSLLP-DVDSLLYVDTDILFLRPVEEIWSflKKFNSTQLAAmapeheEPNIGWYNRFAR---------HPYYgktg 156
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488277556 159 -NSGVMVIDLDKAREI----------IKWSD-IAQMIEKYNLLLILPDQDILNRLYGKYtkeiPEEI------WNY 216
Cdd:cd06430  157 vNSGVMLMNLTRMRRKyfkndmtpvgLRWEEiLMPLYKKYKLKITWGDQDLINIIFHHN----PEMLyvfpchWNY 228
 
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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