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Conserved domains on  [gi|446236146|ref|WP_000314001|]
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lipopolysaccharide 3-alpha-galactosyltransferase, partial [Escherichia coli]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15171 super family cl33095
lipopolysaccharide 3-alpha-galactosyltransferase;
1-253 2.47e-176

lipopolysaccharide 3-alpha-galactosyltransferase;


The actual alignment was detected with superfamily member PRK15171:

Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 488.11  E-value: 2.47e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   1 SRINIYVINCDKLKSLPSTKNWTYATYFRFIIADYFYHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVVAERDVEW 80
Cdd:PRK15171  82 TRINIYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDAEW 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  81 WQNRASVLTTPQLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPDWVSKITHLDQDVLNVLLNGKVKFISEKYNTRYS 160
Cdd:PRK15171 162 WSKRAQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFS 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146 161 INYELKDKVDNPVNDDTVFIHYVGPTKPWHEWADYPVSRSFLIAKAASPWSKEDLLKPVNSNQYRYCAKHKFKQKHYMAG 240
Cdd:PRK15171 242 LNYELKDSVINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYING 321
                        250
                 ....*....|...
gi 446236146 241 IFNYLKYYKEKCF 253
Cdd:PRK15171 322 IMNYIKYFKEKIF 334
 
Name Accession Description Interval E-value
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
1-253 2.47e-176

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 488.11  E-value: 2.47e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   1 SRINIYVINCDKLKSLPSTKNWTYATYFRFIIADYFYHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVVAERDVEW 80
Cdd:PRK15171  82 TRINIYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDAEW 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  81 WQNRASVLTTPQLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPDWVSKITHLDQDVLNVLLNGKVKFISEKYNTRYS 160
Cdd:PRK15171 162 WSKRAQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFS 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146 161 INYELKDKVDNPVNDDTVFIHYVGPTKPWHEWADYPVSRSFLIAKAASPWSKEDLLKPVNSNQYRYCAKHKFKQKHYMAG 240
Cdd:PRK15171 242 LNYELKDSVINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYING 321
                        250
                 ....*....|...
gi 446236146 241 IFNYLKYYKEKCF 253
Cdd:PRK15171 322 IMNYIKYFKEKIF 334
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-243 5.60e-79

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 239.88  E-value: 5.60e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   1 SRINIYVINCDKLKSLPSTKNWTYATYFRFIIADYFYHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVVAERDVEW 80
Cdd:COG1442   62 VSIEFIDVDDELLKDLPVSKHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  81 WQNRASVLTTPqLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPdwVSKITHLDQDVLNVLLNGKVKFISEKYNTRYS 160
Cdd:COG1442  142 QKKRAKRLGLP-DDDGYFNSGVLLINLKKWREENITEKALEFLKEN--PDKLKYPDQDILNIVLGGKVKFLPPRYNYQYS 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146 161 INYELKDKVD----NPVNDDTVFIHYVGPTKPWHEWADYPVSRSFLIAKAASPWSKEDLLKPVNSNQYRYCAKHkfkqKH 236
Cdd:COG1442  219 LYYELKDKSNkkelLEARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKH----LR 294

                 ....*..
gi 446236146 237 YMAGIFN 243
Cdd:COG1442  295 YLKGIKN 301
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
3-193 2.05e-53

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: 173.28  E-value: 2.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146    3 INIYVINCDKLKSLPSTKNWTYATYFRFIIADYFyHKHEKILYLDADIACKGSIKELLDYQFsTNEIAAVVAER--DVEW 80
Cdd:pfam01501  63 SDIKIFEYFSKLKLRSPKYWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDL-GGKVLAAVEDNyfQRYP 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   81 WQNRASVLTTPQLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPDWVSKITHLDQDVLNVLLNGKVKFISEKYNTRYS 160
Cdd:pfam01501 141 NFSEPIILENFGPPACYFNAGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGL 220
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446236146  161 INYeLKDKVDNPVNDDTVFIHYVGPTKPWHEWA 193
Cdd:pfam01501 221 GYY-NKKKSLNEITENAAVIHYNGPTKPWLDIA 252
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
1-190 1.10e-49

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: 163.54  E-value: 1.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   1 SRINIYVINCDKLKSLP-STKNWTYATYFRFIIADYFyHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVvaeRD-V 78
Cdd:cd04194   57 SSIEFIKIDNDDFKFFPaTTDHISYATYYRLLIPDLL-PDYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAV---RDpF 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  79 EWWQNRASVLTTPQLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPDwvSKITHLDQDVLNVLLNGKVKFISEKYNTR 158
Cdd:cd04194  133 IEQEKKRKRRLGGYDDGSYFNSGVLLINLKKWREENITEKLLELIKEYG--GRLIYPDQDILNAVLKDKILYLPPRYNFQ 210
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446236146 159 YSINYELKDK-----VDNPVNDDTVFIHYVGPTKPWH 190
Cdd:cd04194  211 TGFYYLLKKKskeeqELEEARKNPVIIHYTGSDKPWN 247
 
Name Accession Description Interval E-value
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
1-253 2.47e-176

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 488.11  E-value: 2.47e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   1 SRINIYVINCDKLKSLPSTKNWTYATYFRFIIADYFYHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVVAERDVEW 80
Cdd:PRK15171  82 TRINIYLINCERLKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDFAENEIAAVVAEGDAEW 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  81 WQNRASVLTTPQLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPDWVSKITHLDQDVLNVLLNGKVKFISEKYNTRYS 160
Cdd:PRK15171 162 WSKRAQSLQTPGLASGYFNSGFLLINIPAWAQENISAKAIEMLADPEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFS 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146 161 INYELKDKVDNPVNDDTVFIHYVGPTKPWHEWADYPVSRSFLIAKAASPWSKEDLLKPVNSNQYRYCAKHKFKQKHYMAG 240
Cdd:PRK15171 242 LNYELKDSVINPVNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNEALLKPVNSNQLRYCAKHMFKQKHYING 321
                        250
                 ....*....|...
gi 446236146 241 IFNYLKYYKEKCF 253
Cdd:PRK15171 322 IMNYIKYFKEKIF 334
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-243 5.60e-79

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 239.88  E-value: 5.60e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   1 SRINIYVINCDKLKSLPSTKNWTYATYFRFIIADYFYHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVVAERDVEW 80
Cdd:COG1442   62 VSIEFIDVDDELLKDLPVSKHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDLGGNLLAAVRDGTVTGS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  81 WQNRASVLTTPqLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPdwVSKITHLDQDVLNVLLNGKVKFISEKYNTRYS 160
Cdd:COG1442  142 QKKRAKRLGLP-DDDGYFNSGVLLINLKKWREENITEKALEFLKEN--PDKLKYPDQDILNIVLGGKVKFLPPRYNYQYS 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146 161 INYELKDKVD----NPVNDDTVFIHYVGPTKPWHEWADYPVSRSFLIAKAASPWSKEDLLKPVNSNQYRYCAKHkfkqKH 236
Cdd:COG1442  219 LYYELKDKSNkkelLEARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKH----LR 294

                 ....*..
gi 446236146 237 YMAGIFN 243
Cdd:COG1442  295 YLKGIKN 301
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
3-193 2.05e-53

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: 173.28  E-value: 2.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146    3 INIYVINCDKLKSLPSTKNWTYATYFRFIIADYFyHKHEKILYLDADIACKGSIKELLDYQFsTNEIAAVVAER--DVEW 80
Cdd:pfam01501  63 SDIKIFEYFSKLKLRSPKYWSLLNYLRLYLPDLF-PKLDKILYLDADIVVQGDLSPLWDIDL-GGKVLAAVEDNyfQRYP 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   81 WQNRASVLTTPQLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPDWVSKITHLDQDVLNVLLNGKVKFISEKYNTRYS 160
Cdd:pfam01501 141 NFSEPIILENFGPPACYFNAGMLLFDLDAWRKENITERYIKWLNLNENRTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGL 220
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446236146  161 INYeLKDKVDNPVNDDTVFIHYVGPTKPWHEWA 193
Cdd:pfam01501 221 GYY-NKKKSLNEITENAAVIHYNGPTKPWLDIA 252
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
1-190 1.10e-49

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: 163.54  E-value: 1.10e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146   1 SRINIYVINCDKLKSLP-STKNWTYATYFRFIIADYFyHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVvaeRD-V 78
Cdd:cd04194   57 SSIEFIKIDNDDFKFFPaTTDHISYATYYRLLIPDLL-PDYDKVLYLDADIIVLGDLSELFDIDLGDNLLAAV---RDpF 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  79 EWWQNRASVLTTPQLASGYFNAGFLLINIDEWNLNNISSKAIEMLRDPDwvSKITHLDQDVLNVLLNGKVKFISEKYNTR 158
Cdd:cd04194  133 IEQEKKRKRRLGGYDDGSYFNSGVLLINLKKWREENITEKLLELIKEYG--GRLIYPDQDILNAVLKDKILYLPPRYNFQ 210
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446236146 159 YSINYELKDK-----VDNPVNDDTVFIHYVGPTKPWH 190
Cdd:cd04194  211 TGFYYLLKKKskeeqELEEARKNPVIIHYTGSDKPWN 247
Glyco_transf_8C pfam08437
Glycosyl transferase family 8 C-terminal; This domain is found at the C-terminus of the Pfam: ...
196-249 4.74e-17

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: 72.73  E-value: 4.74e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446236146  196 PVSRSFLIAKAASPWSKEDLLKPVNSNQYRYCAKHKFKQKHYMAGIFNYLKYYK 249
Cdd:pfam08437   1 PSAKYFLKAYEASPWKDVPLLPPRTSKEMKKKAKHLFKQGKYISGIIWYIKYLY 54
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
18-190 8.61e-14

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: 68.62  E-value: 8.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  18 STKNWTYATYFRF-IIADYfyhkhEKILYLDADIACKGSIKELLDYQFSTNEIAAvvAERDVEWWQNRASVLTTPQLASG 96
Cdd:cd00505   78 PIKIVTLTKLHLPnLVPDY-----DKILYVDADILVLTDIDELWDTPLGGQELAA--APDPGDRREGKYYRQKRSHLAGP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  97 -YFNAGFLLINIDEWNLNNISSKAIEmlRDPDWVSKITHLDQDVLNVLLNG---KVKFISEKYNTR-----YSINYELKD 167
Cdd:cd00505  151 dYFNSGVFVVNLSKERRNQLLKVALE--KWLQSLSSLSGGDQDLLNTFFKQvpfIVKSLPCIWNVRltgcyRSLNCFKAF 228
                        170       180
                 ....*....|....*....|...
gi 446236146 168 KVDNPVnddtvfIHYVGPTKPWH 190
Cdd:cd00505  229 VKNAKV------IHFNGPTKPWN 245
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
41-195 1.38e-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: 56.89  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  41 EKILYLDADIACKGSIKELLDYQFstnEIAAVVaerDVEWwqnrasvlttpqlaSGYFNAGFLLI--NIDEWNlnnissK 118
Cdd:cd02537   91 DKVVFLDADTLVLRNIDELFDLPG---EFAAAP---DCGW--------------PDLFNSGVFVLkpSEETFN------D 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146 119 AIEMLRDPdwvSKITHLDQDVLNVLLNGKVKF--ISEKYN-TRYSINYELKDKVDNpvnDDTVFIHYVGPTKPWHEWADY 195
Cdd:cd02537  145 LLDALQDT---PSFDGGDQGLLNSYFSDRGIWkrLPFTYNaLKPLRYLHPEALWFG---DEIKVVHFIGGDKPWSWWRDP 218
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
26-193 1.74e-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: 38.91  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146  26 TYFRFIIADyFYHKHEKILYLDADIACKGSIKELLDYQFSTNEIAAVvaerdvewwqnrasvlttpqlaSGYFNAGFLLI 105
Cdd:cd06429  101 NFARFYLPE-LFPKLEKVIYLDDDVVVQKDLTELWNTDLGGGVAGAV----------------------ETSWNPGVNVV 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446236146 106 NIDEWNLNNISSkAIEMLRDPDWVSKITHLDQDVLNVLL---NGKVKFISEKYNTR-----YSINYELkdkVDNpvnddT 177
Cdd:cd06429  158 NLTEWRRQNVTE-TYEKWMELNQEEEVTLWKLITLPPGLivfYGLTSPLDPSWHVRglgynYGIRPQD---IKA-----A 228
                        170
                 ....*....|....*.
gi 446236146 178 VFIHYVGPTKPWHEWA 193
Cdd:cd06429  229 AVLHFNGNMKPWLRTA 244
 
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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