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Conserved domains on  [gi|15833756|ref|NP_312529|]
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lipopolysaccharide 1,2-glucosyltransferase WaaR [Escherichia coli O157:H7 str. Sakai]

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 ...
25-324 7.05e-101

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


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 299.20  E-value: 7.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  25 RETFNVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALPQSNI 104
Cdd:COG1442   3 KNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 105 WPVSIYYRLLSFDYFSARLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVIDVDAM--QSKSAERLcNEDFNGSYFNSG 182
Cdd:COG1442  83 ISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRL-GLPDDDGYFNSG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 183 VMYINLREWLKQRLTEKFFDLLSDESiiKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSEFEEKNSEYYTRFINDDT 262
Cdd:COG1442 162 VLLINLKKWREENITEKALEFLKENP--DKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNP 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833756 263 VFIHYTGITKPWHDWANYASADYFRNIYNISPWRNIPYKKAVKKHEYKEKYKHLLYQKKFLD 324
Cdd:COG1442 240 VIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHLRYLKGIKN 301
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
25-324 7.05e-101

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 299.20  E-value: 7.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  25 RETFNVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALPQSNI 104
Cdd:COG1442   3 KNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 105 WPVSIYYRLLSFDYFSARLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVIDVDAM--QSKSAERLcNEDFNGSYFNSG 182
Cdd:COG1442  83 ISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRL-GLPDDDGYFNSG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 183 VMYINLREWLKQRLTEKFFDLLSDESiiKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSEFEEKNSEYYTRFINDDT 262
Cdd:COG1442 162 VLLINLKKWREENITEKALEFLKENP--DKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNP 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833756 263 VFIHYTGITKPWHDWANYASADYFRNIYNISPWRNIPYKKAVKKHEYKEKYKHLLYQKKFLD 324
Cdd:COG1442 240 VIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHLRYLKGIKN 301
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
24-332 5.34e-84

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 257.37  E-value: 5.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756   24 ERETFNVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALPQSN 103
Cdd:PRK15171  22 SKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCERLKSLPSTK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  104 IWPVSIYYRLLSFDYFSARLDSLLYLDADIVCKGSLNELIALEF-KDEYGAVVIDVDA-MQSKSAERLCNEDFNGSYFNS 181
Cdd:PRK15171 102 NWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVAEGDAeWWSKRAQSLQTPGLASGYFNS 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  182 GVMYINLREWLKQRLTEKFFDLLSDESIIKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSEFEEKnseyYTRFINDD 261
Cdd:PRK15171 182 GFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNYELKDS----VINPVNDE 257
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833756  262 TVFIHYTGITKPWHDWANYASADYFRNIYNISPWRNIPYKKAVKKHEYKEKYKHLLYQKKFLDGVFTAIKY 332
Cdd:PRK15171 258 TVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYINGIMNYIKY 328
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
28-276 3.87e-79

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: 241.74  E-value: 3.87e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  28 FNVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALP-QSNIWP 106
Cdd:cd04194   1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 107 VSIYYRLLSFDYFSaRLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVIDVDAMQSKSAERLCNEDFNGSYFNSGVMYI 186
Cdd:cd04194  81 YATYYRLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 187 NLREWLKQRLTEKFFDLLSDESiiKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSE-FEEKNSEYYTRFINDDTVFI 265
Cdd:cd04194 160 NLKKWREENITEKLLELIKEYG--GRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLlKKKSKEEQELEEARKNPVII 237
                       250
                ....*....|.
gi 15833756 266 HYTGITKPWHD 276
Cdd:cd04194 238 HYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
29-278 2.40e-60

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: 193.69  E-value: 2.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756    29 NVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSE-----PLKALPQSN 103
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKifeyfSKLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756   104 IWPVSIYYRLLSFDYFsARLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVID---VDAMQSKSAERLCNEDFNGSYFN 180
Cdd:pfam01501  81 YWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDnyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756   181 SGVMYINLREWLKQRLTEKFFDLLSDESIIKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSefeekNSEYYTRFIND 260
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYY-----NKKKSLNEITE 234
                         250
                  ....*....|....*...
gi 15833756   261 DTVFIHYTGITKPWHDWA 278
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
25-324 7.05e-101

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 299.20  E-value: 7.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  25 RETFNVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALPQSNI 104
Cdd:COG1442   3 KNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 105 WPVSIYYRLLSFDYFSARLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVIDVDAM--QSKSAERLcNEDFNGSYFNSG 182
Cdd:COG1442  83 ISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTgsQKKRAKRL-GLPDDDGYFNSG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 183 VMYINLREWLKQRLTEKFFDLLSDESiiKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSEFEEKNSEYYTRFINDDT 262
Cdd:COG1442 162 VLLINLKKWREENITEKALEFLKENP--DKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSNKKELLEARKNP 239
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833756 263 VFIHYTGITKPWHDWANYASADYFRNIYNISPWRNIPYKKAVKKHEYKEKYKHLLYQKKFLD 324
Cdd:COG1442 240 VIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHLRYLKGIKN 301
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
24-332 5.34e-84

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 257.37  E-value: 5.34e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756   24 ERETFNVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALPQSN 103
Cdd:PRK15171  22 SKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQYNTRINIYLINCERLKSLPSTK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  104 IWPVSIYYRLLSFDYFSARLDSLLYLDADIVCKGSLNELIALEF-KDEYGAVVIDVDA-MQSKSAERLCNEDFNGSYFNS 181
Cdd:PRK15171 102 NWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFaENEIAAVVAEGDAeWWSKRAQSLQTPGLASGYFNS 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  182 GVMYINLREWLKQRLTEKFFDLLSDESIIKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSEFEEKnseyYTRFINDD 261
Cdd:PRK15171 182 GFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNYELKDS----VINPVNDE 257
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833756  262 TVFIHYTGITKPWHDWANYASADYFRNIYNISPWRNIPYKKAVKKHEYKEKYKHLLYQKKFLDGVFTAIKY 332
Cdd:PRK15171 258 TVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYINGIMNYIKY 328
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
28-276 3.87e-79

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: 241.74  E-value: 3.87e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  28 FNVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALP-QSNIWP 106
Cdd:cd04194   1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 107 VSIYYRLLSFDYFSaRLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVIDVDAMQSKSAERLCNEDFNGSYFNSGVMYI 186
Cdd:cd04194  81 YATYYRLLIPDLLP-DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRKRRLGGYDDGSYFNSGVLLI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 187 NLREWLKQRLTEKFFDLLSDESiiKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSE-FEEKNSEYYTRFINDDTVFI 265
Cdd:cd04194 160 NLKKWREENITEKLLELIKEYG--GRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLlKKKSKEEQELEEARKNPVII 237
                       250
                ....*....|.
gi 15833756 266 HYTGITKPWHD 276
Cdd:cd04194 238 HYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
29-278 2.40e-60

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: 193.69  E-value: 2.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756    29 NVSWGIDENYQVGAAISIASILENNKQNKFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDSE-----PLKALPQSN 103
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKifeyfSKLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756   104 IWPVSIYYRLLSFDYFsARLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVID---VDAMQSKSAERLCNEDFNGSYFN 180
Cdd:pfam01501  81 YWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDnyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756   181 SGVMYINLREWLKQRLTEKFFDLLSDESIIKKLKYPDQDILNLMFLHHAKILPRKYNCIYTIKSefeekNSEYYTRFIND 260
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYY-----NKKKSLNEITE 234
                         250
                  ....*....|....*...
gi 15833756   261 DTVFIHYTGITKPWHDWA 278
Cdd:pfam01501 235 NAAVIHYNGPTKPWLDIA 252
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
35-275 6.83e-16

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: 75.94  E-value: 6.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  35 DENYQVGAAISIASILENNKQNkFTFHIIADYLDKEYIELLSQLATKYQTVIKLYHIDsEPLKALPQSNIWPVSI--YYR 112
Cdd:cd00505   9 GDEYLRGAIVLMKSVLRHRTKP-LRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVD-ILDSVDSEHLKRPIKIvtLTK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 113 LLSFDYFSArLDSLLYLDADIVCKGSLNELIALEFKDE-YGAVVIDVDAMQSKSAERLCNEDFNGSYFNSGVMYINLREW 191
Cdd:cd00505  87 LHLPNLVPD-YDKILYVDADILVLTDIDELWDTPLGGQeLAAAPDPGDRREGKYYRQKRSHLAGPDYFNSGVFVVNLSKE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 192 ----LKQRLTEKFFDLLSDESiikklkYPDQDILNLMFLHHA---KILPRKYNciYTIKSEFEEKNseYYTRFINDDTVf 264
Cdd:cd00505 166 rrnqLLKVALEKWLQSLSSLS------GGDQDLLNTFFKQVPfivKSLPCIWN--VRLTGCYRSLN--CFKAFVKNAKV- 234
                       250
                ....*....|.
gi 15833756 265 IHYTGITKPWH 275
Cdd:cd00505 235 IHFNGPTKPWN 245
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
124-277 5.34e-07

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: 49.95  E-value: 5.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 124 DSLLYLDADIVCKGSLNELiaLEFKDEYGAVvIDVDAMQsksaerlcnedfngsYFNSGVMYInlrewlkqRLTEKFFDL 203
Cdd:cd02537  91 DKVVFLDADTLVLRNIDEL--FDLPGEFAAA-PDCGWPD---------------LFNSGVFVL--------KPSEETFND 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 204 LSDEsIIKKLKY--PDQDILNLMF--LHHAKILPRKYNCIYTiksefeekNSEYYTRFINDD--TVFIHYTGITKPWHDW 277
Cdd:cd02537 145 LLDA-LQDTPSFdgGDQGLLNSYFsdRGIWKRLPFTYNALKP--------LRYLHPEALWFGdeIKVVHFIGGDKPWSWW 215
Glyco_transf_8C pfam08437
Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: ...
281-332 9.64e-04

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: 36.90  E-value: 9.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15833756   281 ASADYFRNIYNISPWRNIPYKKAVKKHEYKEKYKHLLYQKKFLDGVFTAIKY 332
Cdd:pfam08437   1 PSAKYFLKAYEASPWKDVPLLPPRTSKEMKKKAKHLFKQGKYISGIIWYIKY 52
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
41-291 6.99e-03

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: 37.75  E-value: 6.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756  41 GAAISIASILENNKQNK-FTFHIIAD---------YLDKEYIELLSQLATKYQTVIKLYHIDSEPLKALPQSNIWPVSI- 109
Cdd:cd06429  12 AAAVVINSSISNNKDPSnLVFHIVTDnqnygamrsWFDLNPLKIATVKVLNFDDFKLLGKVKVDSLMQLESEADTSNLKq 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 110 ----YYRLLSFDYFS-----ARLDSLLYLDADIVCKGSLNELIALEFKDEYGAVVIDVdamqsksaerlcnedfngsyFN 180
Cdd:cd06429  92 rkpeYISLLNFARFYlpelfPKLEKVIYLDDDVVVQKDLTELWNTDLGGGVAGAVETS--------------------WN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833756 181 SGVMYINLREWLKQRLT---EKFFDLL-SDESIIKKLKypDQDILNLMFLHHAKILPRKYNCIYTIKSEFEEknseyyTR 256
Cdd:cd06429 152 PGVNVVNLTEWRRQNVTetyEKWMELNqEEEVTLWKLI--TLPPGLIVFYGLTSPLDPSWHVRGLGYNYGIR------PQ 223
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15833756 257 FInDDTVFIHYTGITKPWHDWANYASADYFRNIYN 291
Cdd:cd06429 224 DI-KAAAVLHFNGNMKPWLRTAIPSYKELWEKYLS 257
 
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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