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Conserved domains on  [gi|486204962|ref|WP_001551848|]
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MULTISPECIES: glycosyltransferase [Enterobacteriaceae]

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 ...
19-321 2.32e-102

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


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 302.66  E-value: 2.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  19 DAPELNVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYFADLPTSQ 98
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  99 FWSYATYFRVLSFEYLSESISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDNDST--QAACAKRLNIPEmNGRYFNA 176
Cdd:COG1442   82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRLGLPD-DDGYFNS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 177 GVIYVNLKKWHEANLTPYLLKLLRgeTKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYTLKNELYDRSHRKYQQTITDK 256
Cdd:COG1442  161 GVLLINLKKWREENITEKALEFLK--ENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKN 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486204962 257 TVLIHYTGITKPWHSWAGYPSASYFNIAREQSPWKKYPLKEARTVAEMQKQYKHLfahgEYIKGI 321
Cdd:COG1442  239 PVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGI 299
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
19-321 2.32e-102

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 302.66  E-value: 2.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  19 DAPELNVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYFADLPTSQ 98
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  99 FWSYATYFRVLSFEYLSESISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDNDST--QAACAKRLNIPEmNGRYFNA 176
Cdd:COG1442   82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRLGLPD-DDGYFNS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 177 GVIYVNLKKWHEANLTPYLLKLLRgeTKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYTLKNELYDRSHRKYQQTITDK 256
Cdd:COG1442  161 GVLLINLKKWREENITEKALEFLK--ENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKN 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486204962 257 TVLIHYTGITKPWHSWAGYPSASYFNIAREQSPWKKYPLKEARTVAEMQKQYKHLfahgEYIKGI 321
Cdd:COG1442  239 PVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGI 299
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
3-331 1.75e-96

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 288.96  E-value: 1.75e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962   3 EFIKERFSYlADNKKEDAPELNVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSII 82
Cdd:PRK15171   7 EVINKTIDF-NYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRIN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  83 VYLIDPKYFADLPTSQFWSYATYFRVLSFEYLSESISTLLYLDADVVCKGSLKPLTEIIF-KDEFAAVIPDNDST-QAAC 160
Cdd:PRK15171  86 IYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVAEGDAEwWSKR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 161 AKRLNIPEMNGRYFNAGVIYVNLKKWHEANLTPYLLKLLRGETKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYTLKNE 240
Cdd:PRK15171 166 AQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNYE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 241 LYDrshrKYQQTITDKTVLIHYTGITKPWHSWAGYPSASYFNIAREQSPWKKYPLKEARTVAEMQKQYKHLFAHGEYIKG 320
Cdd:PRK15171 246 LKD----SVINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYING 321
                        330
                 ....*....|.
gi 486204962 321 ITSLIKYKLKK 331
Cdd:PRK15171 322 IMNYIKYFKEK 332
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
24-273 1.92e-81

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: 247.62  E-value: 1.92e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962   24 NVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYF-----ADLPTSQ 98
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFeyfskLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962   99 FWSYATYFRVLSFEYLsESISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDN---DSTQAACAKRLNIPEMNGRYFN 175
Cdd:pfam01501  81 YWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNyfqRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  176 AGVIYVNLKKWHEANLTPYLLKLLRGETKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYtlkneLYDRSHRKYQQTITD 255
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLG-----LGYYNKKKSLNEITE 234
                         250
                  ....*....|....*...
gi 486204962  256 KTVLIHYTGITKPWHSWA 273
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
23-271 2.50e-73

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: 226.71  E-value: 2.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  23 LNVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYFADLP-TSQFWS 101
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 102 YATYFRVLSFEYLSEsISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDNDSTQAACAKRLNIPEMNGRYFNAGVIYV 181
Cdd:cd04194   81 YATYYRLLIPDLLPD-YDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 182 NLKKWHEANLTPYLLKLLrgETKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYTLKNELYDRSHRKYQ-QTITDKTVLI 260
Cdd:cd04194  160 NLKKWREENITEKLLELI--KEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKSKEEQElEEARKNPVII 237
                        250
                 ....*....|.
gi 486204962 261 HYTGITKPWHS 271
Cdd:cd04194  238 HYTGSDKPWNK 248
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
19-321 2.32e-102

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 302.66  E-value: 2.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  19 DAPELNVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYFADLPTSQ 98
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  99 FWSYATYFRVLSFEYLSESISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDNDST--QAACAKRLNIPEmNGRYFNA 176
Cdd:COG1442   82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRLGLPD-DDGYFNS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 177 GVIYVNLKKWHEANLTPYLLKLLRgeTKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYTLKNELYDRSHRKYQQTITDK 256
Cdd:COG1442  161 GVLLINLKKWREENITEKALEFLK--ENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKN 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 486204962 257 TVLIHYTGITKPWHSWAGYPSASYFNIAREQSPWKKYPLKEARTVAEMQKQYKHLfahgEYIKGI 321
Cdd:COG1442  239 PVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGI 299
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
3-331 1.75e-96

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 288.96  E-value: 1.75e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962   3 EFIKERFSYlADNKKEDAPELNVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSII 82
Cdd:PRK15171   7 EVINKTIDF-NYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRIN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  83 VYLIDPKYFADLPTSQFWSYATYFRVLSFEYLSESISTLLYLDADVVCKGSLKPLTEIIF-KDEFAAVIPDNDST-QAAC 160
Cdd:PRK15171  86 IYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVAEGDAEwWSKR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 161 AKRLNIPEMNGRYFNAGVIYVNLKKWHEANLTPYLLKLLRGETKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYTLKNE 240
Cdd:PRK15171 166 AQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNYE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 241 LYDrshrKYQQTITDKTVLIHYTGITKPWHSWAGYPSASYFNIAREQSPWKKYPLKEARTVAEMQKQYKHLFAHGEYIKG 320
Cdd:PRK15171 246 LKD----SVINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYING 321
                        330
                 ....*....|.
gi 486204962 321 ITSLIKYKLKK 331
Cdd:PRK15171 322 IMNYIKYFKEK 332
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
24-273 1.92e-81

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: 247.62  E-value: 1.92e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962   24 NVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYF-----ADLPTSQ 98
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFeyfskLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962   99 FWSYATYFRVLSFEYLsESISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDN---DSTQAACAKRLNIPEMNGRYFN 175
Cdd:pfam01501  81 YWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNyfqRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  176 AGVIYVNLKKWHEANLTPYLLKLLRGETKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYtlkneLYDRSHRKYQQTITD 255
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLG-----LGYYNKKKSLNEITE 234
                         250
                  ....*....|....*...
gi 486204962  256 KTVLIHYTGITKPWHSWA 273
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
23-271 2.50e-73

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: 226.71  E-value: 2.50e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  23 LNVSYGIDKNFLYGAGVSISSVLINNSDINFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYFADLP-TSQFWS 101
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 102 YATYFRVLSFEYLSEsISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDNDSTQAACAKRLNIPEMNGRYFNAGVIYV 181
Cdd:cd04194   81 YATYYRLLIPDLLPD-YDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 182 NLKKWHEANLTPYLLKLLrgETKYGSLKYLDQDALNIAFNMNNIYLAKDFDTIYTLKNELYDRSHRKYQ-QTITDKTVLI 260
Cdd:cd04194  160 NLKKWREENITEKLLELI--KEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKSKEEQElEEARKNPVII 237
                        250
                 ....*....|.
gi 486204962 261 HYTGITKPWHS 271
Cdd:cd04194  238 HYTGSDKPWNK 248
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
25-270 2.23e-22

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: 94.05  E-value: 2.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  25 VSYGIDKNFLYGAGVSISSVLINNSDiNFVFHVFTDYVDDDYLKSFNETAKQFNTSIIVYLIDPKYF--ADLPTSQFWSY 102
Cdd:cd00505    4 VIVATGDEYLRGAIVLMKSVLRHRTK-PLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSvdSEHLKRPIKIV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 103 aTYFRVLSFEYLSEsISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDNDSTQAACAKRLNIPEM-NGRYFNAGVIYV 181
Cdd:cd00505   83 -TLTKLHLPNLVPD-YDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREGKYYRQKRSHLaGPDYFNSGVFVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 182 NLKKWHEANLTPYLLKllRGETKYGSLKYLDQDALNIAFNmNNIYLAKDFDTIYTLKNELYDRSHRKYQQTITDKTVlIH 261
Cdd:cd00505  161 NLSKERRNQLLKVALE--KWLQSLSSLSGGDQDLLNTFFK-QVPFIVKSLPCIWNVRLTGCYRSLNCFKAFVKNAKV-IH 236

                 ....*....
gi 486204962 262 YTGITKPWH 270
Cdd:cd00505  237 FNGPTKPWN 245
Glyco_transf_8C pfam08437
Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: ...
276-327 4.45e-19

Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: PF01501 domain in bacterial glucosyltransferase and galactosyltransferase proteins.


Pssm-ID: 429997 [Multi-domain]  Cd Length: 54  Bit Score: 79.27  E-value: 4.45e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 486204962  276 PSASYFNIAREQSPWKKYPLKEARTVAEMQKQYKHLFAHGEYIKGITSLIKY 327
Cdd:pfam08437   1 PSAKYFLKAYEASPWKDVPLLPPRTSKEMKKKAKHLFKQGKYISGIIWYIKY 52
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
31-269 1.08e-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: 52.01  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  31 KNFLYGAGVSISSVlINNSDI-NFVFHVFTDYVDDDYLKS-FNETAKQFNTSIIVYL----------IDPKYF---ADLP 95
Cdd:cd06429    8 DNRLAAAVVINSSI-SNNKDPsNLVFHIVTDNQNYGAMRSwFDLNPLKIATVKVLNFddfkllgkvkVDSLMQlesEADT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  96 TSQFWSYATYFRVLSFE--YLSE---SISTLLYLDADVVCKGSLKPLTEIIFKDEFAAVIPDNdstqaacakrlnipemn 170
Cdd:cd06429   87 SNLKQRKPEYISLLNFArfYLPElfpKLEKVIYLDDDVVVQKDLTELWNTDLGGGVAGAVETS----------------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 171 gryFNAGVIYVNLKKWHEANLTPYLLKLL-RGETKYGSLKYL-DQDALNIAFnmnniylakdFDTIYTLkNELYDRSHRK 248
Cdd:cd06429  150 ---WNPGVNVVNLTEWRRQNVTETYEKWMeLNQEEEVTLWKLiTLPPGLIVF----------YGLTSPL-DPSWHVRGLG 215
                        250       260
                 ....*....|....*....|....*
gi 486204962 249 Y----QQTITDKTVLIHYTGITKPW 269
Cdd:cd06429  216 YnygiRPQDIKAAAVLHFNGNMKPW 240
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
75-272 2.91e-06

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: 47.64  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962  75 KQFNTSIIVYLIDPKYFADLPTSQFWSYA-TYFRVLSF-EYlsesiSTLLYLDADVVCkgsLKPLTEII-FKDEFAAViP 151
Cdd:cd02537   50 EVGWIVREVEPIDPPDSANLLKRPRFKDTyTKLRLWNLtEY-----DKVVFLDADTLV---LRNIDELFdLPGEFAAA-P 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486204962 152 DNDSTqaacakrlnipemngRYFNAGVIYvnlkkwheanLTPYLL---KLLRGETKYGSLKYLDQDALNIAFNMNNIYLA 228
Cdd:cd02537  121 DCGWP---------------DLFNSGVFV----------LKPSEEtfnDLLDALQDTPSFDGGDQGLLNSYFSDRGIWKR 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 486204962 229 KDFdtIY-TLKNELYDRSHRKYQQtitDKTVLIHYTGITKPWHSW 272
Cdd:cd02537  176 LPF--TYnALKPLRYLHPEALWFG---DEIKVVHFIGGDKPWSWW 215
 
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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