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Conserved domains on  [gi|16131498|ref|NP_418084|]
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UDP-D-glucose:(glucosyl)LPS alpha-1,3-glucosyltransferase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

lipopolysaccharide 3-alpha-galactosyltransferase( domain architecture ID 11487673)

lipopolysaccharide 3-alpha-galactosyltransferase catalyzes the conversion of UDP-galactose and lipopolysaccharide to UDP and 3-alpha-D-galactosyl-[lipopolysaccharide glucose]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
4-338 0e+00

lipopolysaccharide 3-alpha-galactosyltransferase;


:

Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 620.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498    4 VFFQETEFLNSVIDYDHKVETENLCLDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQY 83
Cdd:PRK15171   1 HYFNEEEVINKTIDFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498   84 KTRIKIYLINGDRLRSLPSTKNWTHAIYFRFVIADYFINKAPKVLYLDADIICQGTIEPLINFSFPDDKVAMVVTEGQAD 163
Cdd:PRK15171  81 NTRINIYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  164 WWEKRAHSLGVAGIAKGYFNSGFLLINTAQWAAQQVSARAIAMLNEPEIIKKITHPDQDVLNMLLADKLIFADIKYNTQF 243
Cdd:PRK15171 161 WWSKRAQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  244 SLNYQLKESFINPVTNDTIFIHYIGPTKPWHDWAwDYPVSQAFMEAKNASPWKNTALLKPNNSNQLRYSAKHMLKKHRYL 323
Cdd:PRK15171 241 SLNYELKDSVINPVNDETVFIHYIGPTKPWHSWA-DYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYI 319
                        330
                 ....*....|....*
gi 16131498  324 KGFSNYLFYFIEKIK 338
Cdd:PRK15171 320 NGIMNYIKYFKEKIF 334
 
Name Accession Description Interval E-value
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
4-338 0e+00

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 620.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498    4 VFFQETEFLNSVIDYDHKVETENLCLDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQY 83
Cdd:PRK15171   1 HYFNEEEVINKTIDFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498   84 KTRIKIYLINGDRLRSLPSTKNWTHAIYFRFVIADYFINKAPKVLYLDADIICQGTIEPLINFSFPDDKVAMVVTEGQAD 163
Cdd:PRK15171  81 NTRINIYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  164 WWEKRAHSLGVAGIAKGYFNSGFLLINTAQWAAQQVSARAIAMLNEPEIIKKITHPDQDVLNMLLADKLIFADIKYNTQF 243
Cdd:PRK15171 161 WWSKRAQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  244 SLNYQLKESFINPVTNDTIFIHYIGPTKPWHDWAwDYPVSQAFMEAKNASPWKNTALLKPNNSNQLRYSAKHMLKKHRYL 323
Cdd:PRK15171 241 SLNYELKDSVINPVNDETVFIHYIGPTKPWHSWA-DYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYI 319
                        330
                 ....*....|....*
gi 16131498  324 KGFSNYLFYFIEKIK 338
Cdd:PRK15171 320 NGIMNYIKYFKEKIF 334
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
29-328 2.28e-97

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 290.34  E-value: 2.28e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  29 LDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQYKTRIKIYLINGDRLRSLPSTKNWTH 108
Cdd:COG1442   6 INIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKHISK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 109 AIYFRFVIADYFINKAPKVLYLDADIICQGTIEPLINFSFPDDKVAMVVTEGQADWWEKRAHSLGvAGIAKGYFNSGFLL 188
Cdd:COG1442  86 ATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSQKKRAKRLG-LPDDDGYFNSGVLL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 189 INTAQWAAQQVSARAIAMLNEPeiIKKITHPDQDVLNMLLADKLIFADIKYNTQFSLNYQLKESF----INPVTNDTIFI 264
Cdd:COG1442 165 INLKKWREENITEKALEFLKEN--PDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSnkkeLLEARKNPVII 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131498 265 HYIGPTKPWHDWAwDYPVSQAFMEAKNASPWKNTALLKPNNSNQLRYSAKHMlkkhRYLKGFSN 328
Cdd:COG1442 243 HYTGPTKPWHKWC-THPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIKN 301
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
31-277 1.52e-84

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: 255.71  E-value: 1.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498    31 IAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQYKTRIKIYLINGDRLR-----SLPSTKN 105
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEyfsklKLRSPKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498   106 WTHAIYFRFVIADYFiNKAPKVLYLDADIICQGTIEPLINFSFpDDKVAMVVTEG--QADWWEKRAHSLGVAGIAKGYFN 183
Cdd:pfam01501  82 WSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDL-GGKVLAAVEDNyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498   184 SGFLLINTAQWAAQQVSARAIAMLNEPEIIKKITHPDQDVLNMLLADKLIFADIKYNTQFSLNYQlKESFINPVTNDTIF 263
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYYN-KKKSLNEITENAAV 238
                         250
                  ....*....|....
gi 16131498   264 IHYIGPTKPWHDWA 277
Cdd:pfam01501 239 IHYNGPTKPWLDIA 252
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
29-275 8.40e-71

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: 220.55  E-value: 8.40e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  29 LDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQYKTRIKIYLINGDRLRSLP-STKNWT 107
Cdd:cd04194   1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 108 HAIYFRFVIADYFINkAPKVLYLDADIICQGTIEPLINFSFpDDKVAMVVTEGQADWWEKRAHSLGVaGIAKGYFNSGFL 187
Cdd:cd04194  81 YATYYRLLIPDLLPD-YDKVLYLDADIIVLGDLSELFDIDL-GDNLLAAVRDPFIEQEKKRKRRLGG-YDDGSYFNSGVL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 188 LINTAQWAAQQVSARAIAMLNEPEiiKKITHPDQDVLNMLLADKLIFADIKYNTQFSLNYQLK-----ESFINPVTNDTI 262
Cdd:cd04194 158 LINLKKWREENITEKLLELIKEYG--GRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKkkskeEQELEEARKNPV 235
                       250
                ....*....|...
gi 16131498 263 FIHYIGPTKPWHD 275
Cdd:cd04194 236 IIHYTGSDKPWNK 248
 
Name Accession Description Interval E-value
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
4-338 0e+00

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 620.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498    4 VFFQETEFLNSVIDYDHKVETENLCLDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQY 83
Cdd:PRK15171   1 HYFNEEEVINKTIDFNYQPHASKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDKSLVFHVFTDYISDADKQRFSALAKQY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498   84 KTRIKIYLINGDRLRSLPSTKNWTHAIYFRFVIADYFINKAPKVLYLDADIICQGTIEPLINFSFPDDKVAMVVTEGQAD 163
Cdd:PRK15171  81 NTRINIYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDAE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  164 WWEKRAHSLGVAGIAKGYFNSGFLLINTAQWAAQQVSARAIAMLNEPEIIKKITHPDQDVLNMLLADKLIFADIKYNTQF 243
Cdd:PRK15171 161 WWSKRAQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  244 SLNYQLKESFINPVTNDTIFIHYIGPTKPWHDWAwDYPVSQAFMEAKNASPWKNTALLKPNNSNQLRYSAKHMLKKHRYL 323
Cdd:PRK15171 241 SLNYELKDSVINPVNDETVFIHYIGPTKPWHSWA-DYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYI 319
                        330
                 ....*....|....*
gi 16131498  324 KGFSNYLFYFIEKIK 338
Cdd:PRK15171 320 NGIMNYIKYFKEKIF 334
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
29-328 2.28e-97

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 290.34  E-value: 2.28e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  29 LDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQYKTRIKIYLINGDRLRSLPSTKNWTH 108
Cdd:COG1442   6 INIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTDGLSDENKERLEALAAKYNVSIEFIDVDDELLKDLPVSKHISK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 109 AIYFRFVIADYFINKAPKVLYLDADIICQGTIEPLINFSFPDDKVAMVVTEGQADWWEKRAHSLGvAGIAKGYFNSGFLL 188
Cdd:COG1442  86 ATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGSQKKRAKRLG-LPDDDGYFNSGVLL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 189 INTAQWAAQQVSARAIAMLNEPeiIKKITHPDQDVLNMLLADKLIFADIKYNTQFSLNYQLKESF----INPVTNDTIFI 264
Cdd:COG1442 165 INLKKWREENITEKALEFLKEN--PDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKSnkkeLLEARKNPVII 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131498 265 HYIGPTKPWHDWAwDYPVSQAFMEAKNASPWKNTALLKPNNSNQLRYSAKHMlkkhRYLKGFSN 328
Cdd:COG1442 243 HYTGPTKPWHKWC-THPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHL----RYLKGIKN 301
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
31-277 1.52e-84

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: 255.71  E-value: 1.52e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498    31 IAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQYKTRIKIYLINGDRLR-----SLPSTKN 105
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEyfsklKLRSPKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498   106 WTHAIYFRFVIADYFiNKAPKVLYLDADIICQGTIEPLINFSFpDDKVAMVVTEG--QADWWEKRAHSLGVAGIAKGYFN 183
Cdd:pfam01501  82 WSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDL-GGKVLAAVEDNyfQRYPNFSEPIILENFGPPACYFN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498   184 SGFLLINTAQWAAQQVSARAIAMLNEPEIIKKITHPDQDVLNMLLADKLIFADIKYNTQFSLNYQlKESFINPVTNDTIF 263
Cdd:pfam01501 160 AGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGYYN-KKKSLNEITENAAV 238
                         250
                  ....*....|....
gi 16131498   264 IHYIGPTKPWHDWA 277
Cdd:pfam01501 239 IHYNGPTKPWLDIA 252
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
29-275 8.40e-71

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: 220.55  E-value: 8.40e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  29 LDIAYGTDKNFLFGCGISIASILKYNEGSRLCFHIFTDYFGDDDRKYFDALALQYKTRIKIYLINGDRLRSLP-STKNWT 107
Cdd:cd04194   1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILNDDISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFPaTTDHIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 108 HAIYFRFVIADYFINkAPKVLYLDADIICQGTIEPLINFSFpDDKVAMVVTEGQADWWEKRAHSLGVaGIAKGYFNSGFL 187
Cdd:cd04194  81 YATYYRLLIPDLLPD-YDKVLYLDADIIVLGDLSELFDIDL-GDNLLAAVRDPFIEQEKKRKRRLGG-YDDGSYFNSGVL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 188 LINTAQWAAQQVSARAIAMLNEPEiiKKITHPDQDVLNMLLADKLIFADIKYNTQFSLNYQLK-----ESFINPVTNDTI 262
Cdd:cd04194 158 LINLKKWREENITEKLLELIKEYG--GRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKkkskeEQELEEARKNPV 235
                       250
                ....*....|...
gi 16131498 263 FIHYIGPTKPWHD 275
Cdd:cd04194 236 IIHYTGSDKPWNK 248
Glyco_transf_8C pfam08437
Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: ...
281-334 7.71e-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: 7.71e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16131498   281 PVSQAFMEAKNASPWKNTALLKPNNSNQLRYSAKHMLKKHRYLKGFSNYLFYFI 334
Cdd:pfam08437   1 PSAKYFLKAYEASPWKDVPLLPPRTSKEMKKKAKHLFKQGKYISGIIWYIKYLY 54
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
33-274 1.54e-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: 63.61  E-value: 1.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  33 YGTDKNFLFGCGISIASILKyNEGSRLCFHIFTDYFGDDDRKYFDALAlqYKTRIKIYLINGDRLRSLPS------TKNW 106
Cdd:cd00505   6 VATGDEYLRGAIVLMKSVLR-HRTKPLRFHVLTNPLSDTFKAALDNLR--KLYNFNYELIPVDILDSVDSehlkrpIKIV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 107 THAIYFRFVIadyfINKAPKVLYLDADIICQGTIEPLINFSFPDDKVAMVvtegQADWWE--------KRAHSLGvagia 178
Cdd:cd00505  83 TLTKLHLPNL----VPDYDKILYVDADILVLTDIDELWDTPLGGQELAAA----PDPGDRregkyyrqKRSHLAG----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 179 KGYFNSGFLLINTAQWAAQQvsarAIAMLNEPEIIKK--ITHPDQDVLNMLL---ADKLIFADIKYNTQFSLNYQLKESF 253
Cdd:cd00505 150 PDYFNSGVFVVNLSKERRNQ----LLKVALEKWLQSLssLSGGDQDLLNTFFkqvPFIVKSLPCIWNVRLTGCYRSLNCF 225
                       250       260
                ....*....|....*....|.
gi 16131498 254 INPVTNDTIfIHYIGPTKPWH 274
Cdd:cd00505 226 KAFVKNAKV-IHFNGPTKPWN 245
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
126-283 7.30e-09

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: 55.35  E-value: 7.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 126 KVLYLDADIICQGTIEPLinFSFPDDKVAmvvtegqadwwekrAHSLGVAgiakGYFNSGFLLI--NTAQWAaqqvsara 203
Cdd:cd02537  92 KVVFLDADTLVLRNIDEL--FDLPGEFAA--------------APDCGWP----DLFNSGVFVLkpSEETFN-------- 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 204 iAMLNEPEIIKKITHPDQDVLNMLLADKLIFADI--KYNTQFSLNYQLKESFINPvtNDTIFIHYIGPTKPWHDWAWDYP 281
Cdd:cd02537 144 -DLLDALQDTPSFDGGDQGLLNSYFSDRGIWKRLpfTYNALKPLRYLHPEALWFG--DEIKVVHFIGGDKPWSWWRDPET 220

                ..
gi 16131498 282 VS 283
Cdd:cd02537 221 KE 222
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
47-200 2.69e-06

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: 48.15  E-value: 2.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498  47 IASILKYNEGSRLCFHIFTD---------YFGDDDRK-------YFDALALQYKTRIKIYLINGDRLRSLPSTKNWTHAI 110
Cdd:cd06429  18 NSSISNNKDPSNLVFHIVTDnqnygamrsWFDLNPLKiatvkvlNFDDFKLLGKVKVDSLMQLESEADTSNLKQRKPEYI 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131498 111 ----YFRFVIADYFiNKAPKVLYLDADIICQGTIEPLINFSFpddkvamvvtegqadwwekrahSLGVAGIAKGYFNSGF 186
Cdd:cd06429  98 sllnFARFYLPELF-PKLEKVIYLDDDVVVQKDLTELWNTDL----------------------GGGVAGAVETSWNPGV 154
                       170
                ....*....|....
gi 16131498 187 LLINTAQWAAQQVS 200
Cdd:cd06429 155 NVVNLTEWRRQNVT 168
 
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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