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Conserved domains on  [gi|16131497|ref|NP_418083|]
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UDP-glucose:(glucosyl)LPS alpha-1,2-glucosyltransferase [Escherichia coli str. K-12 substr. MG1655]

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 ...
24-325 1.10e-97

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


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 291.11  E-value: 1.10e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  24 TSECLNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDKLQCLPCTQ 103
Cdd:COG1442   2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 104 VWSRAMYFRLFAFQLLGLTLDRLLYLDADVVCKGDISQLLHLGLNGAVAAVVKD--VEPMQEKAVSRLSDPELlGQYFNS 181
Cdd:COG1442  82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDgtVTGSQKKRAKRLGLPDD-DGYFNS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 182 GVVYLDLKKWADAKLTEKALSILMSKDNVYKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDKTHQNYKKLITESTL 261
Cdd:COG1442 161 GVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNPV 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131497 262 LIHYTGATKPWHKWAIYPSVKYYKIALENSPWKDDSPRDAKSIIEFKKRYKHLlvqhHYISGII 325
Cdd:COG1442 241 IIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIK 300
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
24-325 1.10e-97

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 291.11  E-value: 1.10e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  24 TSECLNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDKLQCLPCTQ 103
Cdd:COG1442   2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 104 VWSRAMYFRLFAFQLLGLTLDRLLYLDADVVCKGDISQLLHLGLNGAVAAVVKD--VEPMQEKAVSRLSDPELlGQYFNS 181
Cdd:COG1442  82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDgtVTGSQKKRAKRLGLPDD-DGYFNS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 182 GVVYLDLKKWADAKLTEKALSILMSKDNVYKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDKTHQNYKKLITESTL 261
Cdd:COG1442 161 GVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNPV 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131497 262 LIHYTGATKPWHKWAIYPSVKYYKIALENSPWKDDSPRDAKSIIEFKKRYKHLlvqhHYISGII 325
Cdd:COG1442 241 IIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIK 300
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
16-334 2.85e-84

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 258.14  E-value: 2.85e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   16 DFRLANINTSECLNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDK 95
Cdd:PRK15171  14 DFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCER 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   96 LQCLPCTQVWSRAMYFRLFAFQLLGLTLDRLLYLDADVVCKGDISQLLHLGL-NGAVAAVV--KDVEPMQEKAVSrLSDP 172
Cdd:PRK15171  94 LKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVaeGDAEWWSKRAQS-LQTP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  173 ELLGQYFNSGVVYLDLKKWADAKLTEKALSILMSKDNVYK--YPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDKthq 250
Cdd:PRK15171 173 GLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRitHLDQDVLNILLAGKVKFIDAKYNTQFSLNYELKDS--- 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  251 nYKKLITESTLLIHYTGATKPWHKWAIYPSVKYYKIALENSPWKDDSPRDAKSIIEFKKRYKHLLVQHHYISGIIAGVCY 330
Cdd:PRK15171 250 -VINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYINGIMNYIKY 328

                 ....
gi 16131497  331 LCRK 334
Cdd:PRK15171 329 FKEK 332
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
28-274 3.19e-72

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: 224.02  E-value: 3.19e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  28 LNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDKLQCLPC-TQVWS 106
Cdd:cd04194   1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPAtTDHIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 107 RAMYFRLFAFQLLGLTLDRLlYLDADVVCKGDISQLLHLGLNGAVAAVVKDVEPMQEKAVSRLSDPELLGQYFNSGVVYL 186
Cdd:cd04194  81 YATYYRLLIPDLLPDYDKVL-YLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 187 DLKKWADAKLTEKALSILMSKDNVYKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDK-THQNYKKLITESTLLIHY 265
Cdd:cd04194 160 NLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKsKEEQELEEARKNPVIIHY 239

                ....*....
gi 16131497 266 TGATKPWHK 274
Cdd:cd04194 240 TGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
29-276 8.48e-55

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: 179.44  E-value: 8.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497    29 NVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLY-----RINTDKLQCLPCTQ 103
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLesdikIFEYFSKLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   104 VWSRAMYFRLFAFQlLGLTLDRLLYLDADVVCKGDISQLLHLGLNGAVAAVVKD---VEPMQEKAVSRLSDPELLGQYFN 180
Cdd:pfam01501  81 YWSLLNYLRLYLPD-LFPKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDnyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   181 SGVVYLDLKKWADAKLTEKALSILMSKDNV--YKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDkthqnYKKLITE 258
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRtlWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYYNKKK-----SLNEITE 234
                         250
                  ....*....|....*...
gi 16131497   259 STLLIHYTGATKPWHKWA 276
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
24-325 1.10e-97

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 291.11  E-value: 1.10e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  24 TSECLNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDKLQCLPCTQ 103
Cdd:COG1442   2 NKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 104 VWSRAMYFRLFAFQLLGLTLDRLLYLDADVVCKGDISQLLHLGLNGAVAAVVKD--VEPMQEKAVSRLSDPELlGQYFNS 181
Cdd:COG1442  82 HISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDgtVTGSQKKRAKRLGLPDD-DGYFNS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 182 GVVYLDLKKWADAKLTEKALSILMSKDNVYKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDKTHQNYKKLITESTL 261
Cdd:COG1442 161 GVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNPV 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131497 262 LIHYTGATKPWHKWAIYPSVKYYKIALENSPWKDDSPRDAKSIIEFKKRYKHLlvqhHYISGII 325
Cdd:COG1442 241 IIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIK 300
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
16-334 2.85e-84

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 258.14  E-value: 2.85e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   16 DFRLANINTSECLNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDK 95
Cdd:PRK15171  14 DFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCER 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   96 LQCLPCTQVWSRAMYFRLFAFQLLGLTLDRLLYLDADVVCKGDISQLLHLGL-NGAVAAVV--KDVEPMQEKAVSrLSDP 172
Cdd:PRK15171  94 LKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVaeGDAEWWSKRAQS-LQTP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  173 ELLGQYFNSGVVYLDLKKWADAKLTEKALSILMSKDNVYK--YPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDKthq 250
Cdd:PRK15171 173 GLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRitHLDQDVLNILLAGKVKFIDAKYNTQFSLNYELKDS--- 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  251 nYKKLITESTLLIHYTGATKPWHKWAIYPSVKYYKIALENSPWKDDSPRDAKSIIEFKKRYKHLLVQHHYISGIIAGVCY 330
Cdd:PRK15171 250 -VINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYINGIMNYIKY 328

                 ....
gi 16131497  331 LCRK 334
Cdd:PRK15171 329 FKEK 332
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
28-274 3.19e-72

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: 224.02  E-value: 3.19e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  28 LNVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRINTDKLQCLPC-TQVWS 106
Cdd:cd04194   1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPAtTDHIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 107 RAMYFRLFAFQLLGLTLDRLlYLDADVVCKGDISQLLHLGLNGAVAAVVKDVEPMQEKAVSRLSDPELLGQYFNSGVVYL 186
Cdd:cd04194  81 YATYYRLLIPDLLPDYDKVL-YLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 187 DLKKWADAKLTEKALSILMSKDNVYKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDK-THQNYKKLITESTLLIHY 265
Cdd:cd04194 160 NLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKsKEEQELEEARKNPVIIHY 239

                ....*....
gi 16131497 266 TGATKPWHK 274
Cdd:cd04194 240 TGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
29-276 8.48e-55

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: 179.44  E-value: 8.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497    29 NVAYGVDANYLDGVGVSITSIVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLY-----RINTDKLQCLPCTQ 103
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLesdikIFEYFSKLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   104 VWSRAMYFRLFAFQlLGLTLDRLLYLDADVVCKGDISQLLHLGLNGAVAAVVKD---VEPMQEKAVSRLSDPELLGQYFN 180
Cdd:pfam01501  81 YWSLLNYLRLYLPD-LFPKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDnyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497   181 SGVVYLDLKKWADAKLTEKALSILMSKDNV--YKYPDQDVMNVLLKGMTLFLPREYNTIYTIKSELKDkthqnYKKLITE 258
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRtlWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYYNKKK-----SLNEITE 234
                         250
                  ....*....|....*...
gi 16131497   259 STLLIHYTGATKPWHKWA 276
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
Glyco_transf_8C pfam08437
Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: ...
279-332 8.44e-20

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: 81.59  E-value: 8.44e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16131497   279 PSVKYYKIALENSPWKDDSPRDAKSIIEFKKRYKHLLVQHHYISGIIAGVCYLC 332
Cdd:pfam08437   1 PSAKYFLKAYEASPWKDVPLLPPRTSKEMKKKAKHLFKQGKYISGIIWYIKYLY 54
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
30-274 8.99e-11

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: 61.30  E-value: 8.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  30 VAYGVDANYLDGVGVSITSiVLNNRHINLDFYIIADVYNDGFFQKIAKLAEQNQLRITLYRIN--------TDKLQCLPC 101
Cdd:cd00505   4 VIVATGDEYLRGAIVLMKS-VLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDildsvdseHLKRPIKIV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 102 TqvwsramYFRLFAFqLLGLTLDRLLYLDADVVCKGDISQLLHLGLNGAVAAVVKDV-EPMQEKAVSRLSDPELLGQYFN 180
Cdd:cd00505  83 T-------LTKLHLP-NLVPDYDKILYVDADILVLTDIDELWDTPLGGQELAAAPDPgDRREGKYYRQKRSHLAGPDYFN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 181 SGVVYLDLKKWADAKLTEKALSILMSKDNVYKYPDQDVMNVLLKGMTL---FLPREYNTIYT-IKSELkdkthqNYKKLI 256
Cdd:cd00505 155 SGVFVVNLSKERRNQLLKVALEKWLQSLSSLSGGDQDLLNTFFKQVPFivkSLPCIWNVRLTgCYRSL------NCFKAF 228
                       250
                ....*....|....*...
gi 16131497 257 TESTLLIHYTGATKPWHK 274
Cdd:cd00505 229 VKNAKVIHFNGPTKPWNK 246
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
128-277 6.76e-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: 6.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 128 YLDADVVCKGDISQLLHLGLNGAVAAVVKDVepmqekavsrlsdpellgqyFNSGVVYLDLKKWADAKLTEkALSILMSK 207
Cdd:cd06429 119 YLDDDVVVQKDLTELWNTDLGGGVAGAVETS--------------------WNPGVNVVNLTEWRRQNVTE-TYEKWMEL 177
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131497 208 dnvykypDQDVMNVLLKGMTlfLPREYNTIYTIKSELKDKTHQ-----NYKK--LITESTLLIHYTGATKPWHKWAI 277
Cdd:cd06429 178 -------NQEEEVTLWKLIT--LPPGLIVFYGLTSPLDPSWHVrglgyNYGIrpQDIKAAAVLHFNGNMKPWLRTAI 245
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
128-275 2.14e-04

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: 42.25  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497 128 YLDADVVCKGDISQLLHLGlnGAVAAVVKDVEPmqekavsrlsdpellgQYFNSGVVYL--DLKKWADakLTEKalsilM 205
Cdd:cd02537  95 FLDADTLVLRNIDELFDLP--GEFAAAPDCGWP----------------DLFNSGVFVLkpSEETFND--LLDA-----L 149
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131497 206 SKDNVYKYPDQDVMNVLLKGMTLF--LPREYNTI----YTIKSELKDKTHqnykklitesTLLIHYTGATKPWHKW 275
Cdd:cd02537 150 QDTPSFDGGDQGLLNSYFSDRGIWkrLPFTYNALkplrYLHPEALWFGDE----------IKVVHFIGGDKPWSWW 215
PLN02742 PLN02742
Probable galacturonosyltransferase
128-277 5.11e-04

Probable galacturonosyltransferase


Pssm-ID: 215395 [Multi-domain]  Cd Length: 534  Bit Score: 41.68  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  128 YLDADVVCKGDISQLLHLGLNGAV-AAVVKDVEPMQE---------KAVSRLSDPELLGQYFnsGVVYLDLKKWADAKLT 197
Cdd:PLN02742 358 FLDDDVVVQKDLTPLFSIDLHGNVnGAVETCLETFHRyhkylnfshPLISSHFDPDACGWAF--GMNVFDLVAWRKANVT 435
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131497  198 EkalsilmskdnVYKY-PDQDVMNVLLKGMTLflPREYNTIYTIKSELKDKTH-------QNYKKLITESTLLIHYTGAT 269
Cdd:PLN02742 436 A-----------IYHYwQEQNVDRTLWKLGTL--PPGLLTFYGLTEPLDRRWHvlglgydTNIDPRLIESAAVLHFNGNM 502

                 ....*...
gi 16131497  270 KPWHKWAI 277
Cdd:PLN02742 503 KPWLKLAI 510
 
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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