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Conserved domains on  [gi|488332000|ref|WP_002401385|]
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MULTISPECIES: glycosyltransferase family 8 protein [Enterococcus]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 11444513)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
4-274 4.30e-93

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


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 277.24  E-value: 4.30e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   4 NQKIVPIVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETVSSNsqNATVEFLTADKEVYQNFL 83
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLEN-NPDRPYDFHILTDGLSDENKERLEALAAKY--NVSIEFIDVDDELLKDLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  84 VSDHITTTAYLRISLPSLLQKySYKKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPG----QAYALKRLGIHSADYY 159
Cdd:COG1442   79 VSKHISKATYYRLLIPELLPD-DYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTvtgsQKKRAKRLGLPDDDGY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 160 FNSGVMMIDIDRWNEKAITQKTIQYLEENGDRIVYHDQDALNAVLYEDWLALEPRWNMQTSLVfnrHEAPNEAYQKLYTA 239
Cdd:COG1442  158 FNSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLY---YELKDKSNKKELLE 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488332000 240 GNQEPAIIHFTGHDKPWNTLENHPYTALYLNKLKK 274
Cdd:COG1442  235 ARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
4-274 4.30e-93

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 277.24  E-value: 4.30e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   4 NQKIVPIVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETVSSNsqNATVEFLTADKEVYQNFL 83
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLEN-NPDRPYDFHILTDGLSDENKERLEALAAKY--NVSIEFIDVDDELLKDLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  84 VSDHITTTAYLRISLPSLLQKySYKKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPG----QAYALKRLGIHSADYY 159
Cdd:COG1442   79 VSKHISKATYYRLLIPELLPD-DYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTvtgsQKKRAKRLGLPDDDGY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 160 FNSGVMMIDIDRWNEKAITQKTIQYLEENGDRIVYHDQDALNAVLYEDWLALEPRWNMQTSLVfnrHEAPNEAYQKLYTA 239
Cdd:COG1442  158 FNSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLY---YELKDKSNKKELLE 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488332000 240 GNQEPAIIHFTGHDKPWNTLENHPYTALYLNKLKK 274
Cdd:COG1442  235 ARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
8-258 1.07e-81

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: 246.36  E-value: 1.07e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   8 VPIVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETVSSNsqNATVEFLTADKEVYQNFL-VSD 86
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILAN-NSKRDYDFYILNDDISEENKKKLKELLKKY--NSSIEFIKIDNDDFKFFPaTTD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  87 HITTTAYLRISLPSLLQkySYKKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQAYALKR---LGIHSADYYFNSG 163
Cdd:cd04194   78 HISYATYYRLLIPDLLP--DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRkrrLGGYDDGSYFNSG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 164 VMMIDIDRWNEKAITQKTIQYLEENGDRIVYHDQDALNAVLYEDWLALEPRWNMQTSLVFNRHEAPNEAYQklYTAGNQE 243
Cdd:cd04194  156 VLLINLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKSKEEQE--LEEARKN 233
                        250
                 ....*....|....*
gi 488332000 244 PAIIHFTGHDKPWNT 258
Cdd:cd04194  234 PVIIHYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
9-257 1.24e-49

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: 164.42  E-value: 1.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000    9 PIVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETVSSNSQNATVEFLTADKEVYQNFLVSD-- 86
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKN-NSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEYFSKLKLRsp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   87 -HITTTAYLRISLPSLLQKYSykKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQAYALKRLGIHSAD------YY 159
Cdd:pfam01501  80 kYWSLLNYLRLYLPDLFPKLD--KILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYFQRYPNFSEPIILEnfgppaCY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  160 FNSGVMMIDIDRWNEKAITQKTIQYLEENGDR--IVYHDQDALNAVLYEDWLALEPRWNMQTSLvfnrheapNEAYQKLY 237
Cdd:pfam01501 158 FNAGMLLFDLDAWRKENITERYIKWLNLNENRtlWKLGDQDPLNIVFYGKVKPLDPRWNVLGLG--------YYNKKKSL 229
                         250       260
                  ....*....|....*....|
gi 488332000  238 TAGNQEPAIIHFTGHDKPWN 257
Cdd:pfam01501 230 NEITENAAVIHYNGPTKPWL 249
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
10-269 1.74e-18

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 83.65  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  10 IVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETvsSNSQNATVEFLTADKEVYQNFLVSDHIT 89
Cdd:PRK15171  28 IAYGIDKNFLFGCGVSIASVLLN-NPDKSLVFHVFTDYISDADKQRFSAL--AKQYNTRINIYLINCERLKSLPSTKNWT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  90 TTAYLRIslpsLLQKYSYK---KVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQ-------AYALKRLGIHSAdyY 159
Cdd:PRK15171 105 YATYFRF----IIADYFIDktdKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDaewwskrAQSLQTPGLASG--Y 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 160 FNSGVMMIDIDRWNEKAITQKTIQYLEENG--DRIVYHDQDALNAVLYEDWLALEPRWNMQTSLVFnrheapnEAYQKLY 237
Cdd:PRK15171 179 FNSGFLLINIPAWAQENISAKAIEMLADPEivSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNY-------ELKDSVI 251
                        250       260       270
                 ....*....|....*....|....*....|..
gi 488332000 238 TAGNQEPAIIHFTGHDKPWNTLENHPYTALYL 269
Cdd:PRK15171 252 NPVNDETVFIHYIGPTKPWHSWADYPVSQYFL 283
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
4-274 4.30e-93

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 277.24  E-value: 4.30e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   4 NQKIVPIVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETVSSNsqNATVEFLTADKEVYQNFL 83
Cdd:COG1442    2 NKNTINIVFAIDDNYLPGLGVSIASLLEN-NPDRPYDFHILTDGLSDENKERLEALAAKY--NVSIEFIDVDDELLKDLP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  84 VSDHITTTAYLRISLPSLLQKySYKKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPG----QAYALKRLGIHSADYY 159
Cdd:COG1442   79 VSKHISKATYYRLLIPELLPD-DYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTvtgsQKKRAKRLGLPDDDGY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 160 FNSGVMMIDIDRWNEKAITQKTIQYLEENGDRIVYHDQDALNAVLYEDWLALEPRWNMQTSLVfnrHEAPNEAYQKLYTA 239
Cdd:COG1442  158 FNSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKVKFLPPRYNYQYSLY---YELKDKSNKKELLE 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488332000 240 GNQEPAIIHFTGHDKPWNTLENHPYTALYLNKLKK 274
Cdd:COG1442  235 ARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKK 269
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
8-258 1.07e-81

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: 246.36  E-value: 1.07e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   8 VPIVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETVSSNsqNATVEFLTADKEVYQNFL-VSD 86
Cdd:cd04194    1 MNIVFAIDDNYAPYLAVTIKSILAN-NSKRDYDFYILNDDISEENKKKLKELLKKY--NSSIEFIKIDNDDFKFFPaTTD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  87 HITTTAYLRISLPSLLQkySYKKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQAYALKR---LGIHSADYYFNSG 163
Cdd:cd04194   78 HISYATYYRLLIPDLLP--DYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAVRDPFIEQEKKRkrrLGGYDDGSYFNSG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 164 VMMIDIDRWNEKAITQKTIQYLEENGDRIVYHDQDALNAVLYEDWLALEPRWNMQTSLVFNRHEAPNEAYQklYTAGNQE 243
Cdd:cd04194  156 VLLINLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKSKEEQE--LEEARKN 233
                        250
                 ....*....|....*
gi 488332000 244 PAIIHFTGHDKPWNT 258
Cdd:cd04194  234 PVIIHYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
9-257 1.24e-49

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: 164.42  E-value: 1.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000    9 PIVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETVSSNSQNATVEFLTADKEVYQNFLVSD-- 86
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKN-NSDFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEYFSKLKLRsp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   87 -HITTTAYLRISLPSLLQKYSykKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQAYALKRLGIHSAD------YY 159
Cdd:pfam01501  80 kYWSLLNYLRLYLPDLFPKLD--KILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYFQRYPNFSEPIILEnfgppaCY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  160 FNSGVMMIDIDRWNEKAITQKTIQYLEENGDR--IVYHDQDALNAVLYEDWLALEPRWNMQTSLvfnrheapNEAYQKLY 237
Cdd:pfam01501 158 FNAGMLLFDLDAWRKENITERYIKWLNLNENRtlWKLGDQDPLNIVFYGKVKPLDPRWNVLGLG--------YYNKKKSL 229
                         250       260
                  ....*....|....*....|
gi 488332000  238 TAGNQEPAIIHFTGHDKPWN 257
Cdd:pfam01501 230 NEITENAAVIHYNGPTKPWL 249
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
10-257 1.53e-32

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: 119.85  E-value: 1.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  10 IVTASDENYAPYLNVMMTTVLEncHAERSVHFYVIDDGLSLSSKKALQETvsSNSQNATVEFLTADKEVYQNF-LVSDHI 88
Cdd:cd00505    4 VIVATGDEYLRGAIVLMKSVLR--HRTKPLRFHVLTNPLSDTFKAALDNL--RKLYNFNYELIPVDILDSVDSeHLKRPI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  89 TTTAYLRISLPSLLQKYSykKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQAYA--LKRLGIHSAD--YYFNSGV 164
Cdd:cd00505   80 KIVTLTKLHLPNLVPDYD--KILYVDADILVLTDIDELWDTPLGGQELAAAPDPGDRREgkYYRQKRSHLAgpDYFNSGV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 165 MMIDIDRWNEKAITQKTIQYLEENGDRIVYHDQDALNAVlYEDWLA----LEPRWNMQTSlvfnrheapNEAYQKLYTAG 240
Cdd:cd00505  158 FVVNLSKERRNQLLKVALEKWLQSLSSLSGGDQDLLNTF-FKQVPFivksLPCIWNVRLT---------GCYRSLNCFKA 227
                        250
                 ....*....|....*...
gi 488332000 241 NQEPA-IIHFTGHDKPWN 257
Cdd:cd00505  228 FVKNAkVIHFNGPTKPWN 245
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
8-268 6.45e-21

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: 88.99  E-value: 6.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000   8 VPIVTASDENYAPyLNVMMTTVLENCHAERsVHFYVIDDGlslSSKKALQETVSSNS-QNATVEFLTADKEVYQNFLVSD 86
Cdd:cd06429    1 IHVVIFSDNRLAA-AVVINSSISNNKDPSN-LVFHIVTDN---QNYGAMRSWFDLNPlKIATVKVLNFDDFKLLGKVKVD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  87 H--------------------ITTTAYLRISLPSLLQKYsyKKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPgqay 146
Cdd:cd06429   76 SlmqleseadtsnlkqrkpeyISLLNFARFYLPELFPKL--EKVIYLDDDVVVQKDLTELWNTDLGGGVAGAVETS---- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 147 alkrlgihsadyyFNSGVMMIDIDRWNEKAITQKTIQYLEENGDRIV-YHDQDALNA---VLYEDWLALEPRWNMqtslv 222
Cdd:cd06429  150 -------------WNPGVNVVNLTEWRRQNVTETYEKWMELNQEEEVtLWKLITLPPgliVFYGLTSPLDPSWHV----- 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488332000 223 fnRHEAPNEA--YQKLYTAgnqepAIIHFTGHDKPWNTLENHPYTALY 268
Cdd:cd06429  212 --RGLGYNYGirPQDIKAA-----AVLHFNGNMKPWLRTAIPSYKELW 252
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
10-269 1.74e-18

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 83.65  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  10 IVTASDENYAPYLNVMMTTVLENcHAERSVHFYVIDDGLSLSSKKALQETvsSNSQNATVEFLTADKEVYQNFLVSDHIT 89
Cdd:PRK15171  28 IAYGIDKNFLFGCGVSIASVLLN-NPDKSLVFHVFTDYISDADKQRFSAL--AKQYNTRINIYLINCERLKSLPSTKNWT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  90 TTAYLRIslpsLLQKYSYK---KVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQ-------AYALKRLGIHSAdyY 159
Cdd:PRK15171 105 YATYFRF----IIADYFIDktdKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDaewwskrAQSLQTPGLASG--Y 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 160 FNSGVMMIDIDRWNEKAITQKTIQYLEENG--DRIVYHDQDALNAVLYEDWLALEPRWNMQTSLVFnrheapnEAYQKLY 237
Cdd:PRK15171 179 FNSGFLLINIPAWAQENISAKAIEMLADPEivSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNY-------ELKDSVI 251
                        250       260       270
                 ....*....|....*....|....*....|..
gi 488332000 238 TAGNQEPAIIHFTGHDKPWNTLENHPYTALYL 269
Cdd:PRK15171 252 NPVNDETVFIHYIGPTKPWHSWADYPVSQYFL 283
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
107-257 8.51e-14

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: 69.21  E-value: 8.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 107 YKKVLYLDADTLVLDDIVQLYDTPlvnQTIGAVIDPGqayalkrlgihsADYYFNSGVMMI--DIDRWNekaitqKTIQY 184
Cdd:cd02537   90 YDKVVFLDADTLVLRNIDELFDLP---GEFAAAPDCG------------WPDLFNSGVFVLkpSEETFN------DLLDA 148
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488332000 185 LEENGDrIVYHDQDALNAVlYED---WLALEPRWNMQtslvfnrheAPNEAYQKLYTAGNQEPAIIHFTGHDKPWN 257
Cdd:cd02537  149 LQDTPS-FDGGDQGLLNSY-FSDrgiWKRLPFTYNAL---------KPLRYLHPEALWFGDEIKVVHFIGGDKPWS 213
PLN02867 PLN02867
Probable galacturonosyltransferase
93-256 1.47e-06

Probable galacturonosyltransferase


Pssm-ID: 178458 [Multi-domain]  Cd Length: 535  Bit Score: 49.13  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  93 YLRISLPSLLQKYSykKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVID--------PGQAY--------ALKRLGIHSA 156
Cdd:PLN02867 333 HLRIYIPELFPDLN--KIVFLDDDVVVQHDLSSLWELDLNGKVVGAVVDswcgdnccPGRKYkdylnfshPLISSNLDQE 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 157 DYYFNSGVMMIDIDRWNEKAITQKTIQYLEENgdrivyhdqdaLNAVLyEDWL--ALEPrwnmqTSLVFNRHEAPNEAYQ 234
Cdd:PLN02867 411 RCAWLYGMNVFDLKAWRRTNITEAYHKWLKLS-----------LNSGL-QLWQpgALPP-----ALLAFKGHVHPIDPSW 473
                        170       180       190
                 ....*....|....*....|....*....|..
gi 488332000 235 KLYTAGNQEP----------AIIHFTGHDKPW 256
Cdd:PLN02867 474 HVAGLGSRPPevpreilesaAVLHFSGPAKPW 505
PLN02769 PLN02769
Probable galacturonosyltransferase
98-264 4.73e-05

Probable galacturonosyltransferase


Pssm-ID: 215412 [Multi-domain]  Cd Length: 629  Bit Score: 44.69  E-value: 4.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  98 LPSLLQKYsyKKVLYLDADTLVLDDIVQLYDTPLVNQTIGAV----IDPGQayaLKRLgIHSADYYFN-----SGVMMID 168
Cdd:PLN02769 445 LPEIFKKL--KKVVVLDDDVVVQRDLSFLWNLDMGGKVNGAVqfcgVRLGQ---LKNY-LGDTNFDTNscawmSGLNVID 518
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 169 IDRWNEKAITQKTIQYLEEngdriVYHDQD------ALNAVL--YEDWL-ALEPRWnMQTSLVFNRHeapneayqkLYTA 239
Cdd:PLN02769 519 LDKWRELDVTETYLKLLQK-----FSKDGEeslraaALPASLltFQDLIyPLDDRW-VLSGLGHDYG---------IDEQ 583
                        170       180
                 ....*....|....*....|....*
gi 488332000 240 GNQEPAIIHFTGHDKPWNTLENHPY 264
Cdd:PLN02769 584 AIKKAAVLHYNGNMKPWLELGIPKY 608
PLN02829 PLN02829
Probable galacturonosyltransferase
93-256 3.59e-04

Probable galacturonosyltransferase


Pssm-ID: 215443 [Multi-domain]  Cd Length: 639  Bit Score: 41.76  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000  93 YLRISLPSLLQKYSykKVLYLDADTLVLDDIVQLYDTPLVNQTIGAVIDPGQAYalkrlgiHSADYYFN----------- 161
Cdd:PLN02829 445 HLRFYLPEIFPKLN--KVLFLDDDIVVQKDLTGLWSIDLKGNVNGAVETCGESF-------HRFDRYLNfsnplisknfd 515
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488332000 162 -------SGVMMIDIDRWNEKAITQKTIQYLEENGDRIVYhDQDALNAVLYEDW---LALEPRWNMqTSLVFNRHEAPNE 231
Cdd:PLN02829 516 phacgwaYGMNVFDLDEWKRQNITEVYHSWQKLNHDRQLW-KLGTLPPGLITFWkrtYPLDRSWHV-LGLGYNPNVNQRD 593
                        170       180
                 ....*....|....*....|....*
gi 488332000 232 AyqklytagnQEPAIIHFTGHDKPW 256
Cdd:PLN02829 594 I---------ERAAVIHYNGNMKPW 609
 
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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