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Conserved domains on  [gi|1242013580|ref|NP_001342190|]
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glycogenin-1 isoform 1 [Mus musculus]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 10118608)

glycosyltransferase family 8 protein similar to vertebrate glycogenin, which catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached to internal tyrosine residues

CATH:  3.90.550.10
Gene Ontology:  GO:0016757|GO:0005978
PubMed:  10508766|12691742

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
4-254 1.00e-113

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: 329.99  E-value: 1.00e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   4 QAFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETVFDDVIMVDVLDSGDSAHLtlMKRPELGIT 83
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  84 LTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFERE-ELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGG 162
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 163 DQGLLNTYFSGWAttdITKHLPFVYNLSSISIYSYLPAfKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVNCdsqdptvsH 242
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDD--------Y 226
                         250
                  ....*....|..
gi 1242013580 243 PEFLNLWWDTFT 254
Cdd:cd02537   227 NELHQWWWDIYD 238
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
4-254 1.00e-113

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: 329.99  E-value: 1.00e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   4 QAFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETVFDDVIMVDVLDSGDSAHLtlMKRPELGIT 83
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  84 LTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFERE-ELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGG 162
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 163 DQGLLNTYFSGWAttdITKHLPFVYNLSSISIYSYLPAfKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVNCdsqdptvsH 242
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDD--------Y 226
                         250
                  ....*....|..
gi 1242013580 243 PEFLNLWWDTFT 254
Cdd:cd02537   227 NELHQWWWDIYD 238
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
2-189 6.91e-28

N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 110.21  E-value: 6.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   2 TDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETVFDDVIMVDVLDSGDS------------ 69
Cdd:COG5597    12 SRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDAfnarhargrlhg 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  70 -AHLTLMKRPELGITL---TKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREELSAAPD--PGWPDC--FNSGVFVYQP 141
Cdd:COG5597    92 aAPFTKGRKPAFHTPLdnfCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNvyESLADFhrLNSGVFTARP 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1242013580 142 SIETYNQLLHLASEQGSF-DGGDQGLLNTYFSGWattditkH-LPFVYNL 189
Cdd:COG5597   172 SQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNM 214
PLN00176 PLN00176
galactinol synthase
3-258 1.57e-18

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 85.13  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   3 DQAFVT-LTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETvfDDVIMVDVLDSGDSAHLTLMKRPELG 81
Cdd:PLN00176   22 KRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVS--QGCIVREIEPVYPPENQTQFAMAYYV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  82 ITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREE--LSAAPD---------------------PG---WPD----- 130
Cdd:PLN00176  100 INYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDgyFYAVMDcfcektwshtpqykigycqqcPDkvtWPAelgpp 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 131 ---CFNSGVFVYQPSIETYNQLLHLASEQGSFDGGDQGLLNTYFSgwattDITKHLPFVYNLSSISIYSYlPAFKAFGKn 207
Cdd:PLN00176  180 pplYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFR-----DIYKPIPPVYNLVLAMLWRH-PENVELDK- 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242013580 208 AKVVHFLGR-TKPWNYTynpqTKSVNCDSQDPTvshpEFLNLWWDTFTTNVL 258
Cdd:PLN00176  253 VKVVHYCAAgSKPWRYT----GKEENMDREDIK----MLVKKWWDIYNDESL 296
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-223 7.32e-16

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: 76.21  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   7 VTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTS-----PQVSDSMRKvLETVFDDVIMVDVLDSGDSAHLTLMK----R 77
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALNFHIFtddipVENLDILNW-LASSYKPVLPLLESDIKIFEYFSKLKlrspK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  78 PELGITLTKLHCWSLT-QYSKCVFMDADTLVLSNIDDLFE----------------------REELSAAPDPGWPDCFNS 134
Cdd:pfam01501  81 YWSLLNYLRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 135 GVFVYQP------SI-ETYNQLLHLASEQGSFDGGDQGLLNTYFsgwatTDITKHLPFVYNLSSISIYSYLPAFKAFGKN 207
Cdd:pfam01501 161 GMLLFDLdawrkeNItERYIKWLNLNENRTLWKLGDQDPLNIVF-----YGKVKPLDPRWNVLGLGYYNKKKSLNEITEN 235
                         250
                  ....*....|....*.
gi 1242013580 208 AKVVHFLGRTKPWNYT 223
Cdd:pfam01501 236 AAVIHYNGPTKPWLDI 251
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
4-254 1.00e-113

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: 329.99  E-value: 1.00e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   4 QAFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETVFDDVIMVDVLDSGDSAHLtlMKRPELGIT 83
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  84 LTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFERE-ELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGG 162
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 163 DQGLLNTYFSGWAttdITKHLPFVYNLSSISIYSYLPAfKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVNCdsqdptvsH 242
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDD--------Y 226
                         250
                  ....*....|..
gi 1242013580 243 PEFLNLWWDTFT 254
Cdd:cd02537   227 NELHQWWWDIYD 238
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
4-222 9.68e-66

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: 208.06  E-value: 9.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   4 QAFVTLTTNDAYAKGALVLGSSLKQHRTT-RRMVVLTSPqVSDSMRKVLETVFD------DVIMVDVLDSGDSAHLtlmK 76
Cdd:cd00505     1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKpLRFHVLTNP-LSDTFKAALDNLRKlynfnyELIPVDILDSVDSEHL---K 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  77 RPELGITLTKLHCWSLTQ-YSKCVFMDADTLVLSNIDDLFER----EELSAAPDPGWP----------------DCFNSG 135
Cdd:cd00505    77 RPIKIVTLTKLHLPNLVPdYDKILYVDADILVLTDIDELWDTplggQELAAAPDPGDRregkyyrqkrshlagpDYFNSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 136 VFVYQPSIETYNQLLHLASEQGSF-----DGGDQGLLNTYFSGWAttDITKHLPFVYNLSSISIYSYLPAFKAFGKNAKV 210
Cdd:cd00505   157 VFVVNLSKERRNQLLKVALEKWLQslsslSGGDQDLLNTFFKQVP--FIVKSLPCIWNVRLTGCYRSLNCFKAFVKNAKV 234
                         250
                  ....*....|..
gi 1242013580 211 VHFLGRTKPWNY 222
Cdd:cd00505   235 IHFNGPTKPWNK 246
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
2-189 6.91e-28

N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 110.21  E-value: 6.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   2 TDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETVFDDVIMVDVLDSGDS------------ 69
Cdd:COG5597    12 SRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDAfnarhargrlhg 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  70 -AHLTLMKRPELGITL---TKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREELSAAPD--PGWPDC--FNSGVFVYQP 141
Cdd:COG5597    92 aAPFTKGRKPAFHTPLdnfCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNvyESLADFhrLNSGVFTARP 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1242013580 142 SIETYNQLLHLASEQGSF-DGGDQGLLNTYFSGWattditkH-LPFVYNL 189
Cdd:COG5597   172 SQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNM 214
PLN00176 PLN00176
galactinol synthase
3-258 1.57e-18

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 85.13  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   3 DQAFVT-LTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETvfDDVIMVDVLDSGDSAHLTLMKRPELG 81
Cdd:PLN00176   22 KRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVS--QGCIVREIEPVYPPENQTQFAMAYYV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  82 ITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREE--LSAAPD---------------------PG---WPD----- 130
Cdd:PLN00176  100 INYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDgyFYAVMDcfcektwshtpqykigycqqcPDkvtWPAelgpp 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 131 ---CFNSGVFVYQPSIETYNQLLHLASEQGSFDGGDQGLLNTYFSgwattDITKHLPFVYNLSSISIYSYlPAFKAFGKn 207
Cdd:PLN00176  180 pplYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFR-----DIYKPIPPVYNLVLAMLWRH-PENVELDK- 252
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1242013580 208 AKVVHFLGR-TKPWNYTynpqTKSVNCDSQDPTvshpEFLNLWWDTFTTNVL 258
Cdd:PLN00176  253 VKVVHYCAAgSKPWRYT----GKEENMDREDIK----MLVKKWWDIYNDESL 296
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-225 2.28e-16

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 78.48  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   1 MTDQAF-VTLTTNDAYAKGALVLGSSLKQHRTTR--RMVVLTSpQVSDSMRKVLETVFDD----VIMVDVlDSGDSAHLT 73
Cdd:COG1442     1 MNKNTInIVFAIDDNYLPGLGVSIASLLENNPDRpyDFHILTD-GLSDENKERLEALAAKynvsIEFIDV-DDELLKDLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  74 LMKRpelgITLT---KLHCWSL--TQYSKCVFMDADTLVLSNIDDLFERE----ELSAAPDPGWP--------------- 129
Cdd:COG1442    79 VSKH----ISKAtyyRLLIPELlpDDYDKVLYLDADTLVLGDLSELWDIDlggnLLAAVRDGTVTgsqkkrakrlglpdd 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 130 -DCFNSGVFVY------QPSIEtyNQLLHLASEQGS-FDGGDQGLLNTYFSGWattdiTKHLPFVYN-----LSSISIYS 196
Cdd:COG1442   155 dGYFNSGVLLInlkkwrEENIT--EKALEFLKENPDkLKYPDQDILNIVLGGK-----VKFLPPRYNyqyslYYELKDKS 227
                         250       260
                  ....*....|....*....|....*....
gi 1242013580 197 YLPAFKAFGKNAKVVHFLGRTKPWNYTYN 225
Cdd:COG1442   228 NKKELLEARKNPVIIHYTGPTKPWHKWCT 256
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-223 7.32e-16

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: 76.21  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   7 VTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTS-----PQVSDSMRKvLETVFDDVIMVDVLDSGDSAHLTLMK----R 77
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALNFHIFtddipVENLDILNW-LASSYKPVLPLLESDIKIFEYFSKLKlrspK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  78 PELGITLTKLHCWSLT-QYSKCVFMDADTLVLSNIDDLFE----------------------REELSAAPDPGWPDCFNS 134
Cdd:pfam01501  81 YWSLLNYLRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 135 GVFVYQP------SI-ETYNQLLHLASEQGSFDGGDQGLLNTYFsgwatTDITKHLPFVYNLSSISIYSYLPAFKAFGKN 207
Cdd:pfam01501 161 GMLLFDLdawrkeNItERYIKWLNLNENRTLWKLGDQDPLNIVF-----YGKVKPLDPRWNVLGLGYYNKKKSLNEITEN 235
                         250
                  ....*....|....*.
gi 1242013580 208 AKVVHFLGRTKPWNYT 223
Cdd:pfam01501 236 AAVIHYNGPTKPWLDI 251
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
92-222 1.19e-13

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: 69.94  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  92 LTQYSKCVFMDADTLVLSNIDDLFERE----ELSAAPDPGWPDC---------------FNSGVFVyqpsI--------E 144
Cdd:cd04194    93 LPDYDKVLYLDADIIVLGDLSELFDIDlgdnLLAAVRDPFIEQEkkrkrrlggyddgsyFNSGVLL----InlkkwreeN 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 145 TYNQLLHLASEQGSFDG-GDQGLLNTYFSGwattDItKHLPFVYNLsSISIYSYLPA-------FKAFGKNAKVVHFLGR 216
Cdd:cd04194   169 ITEKLLELIKEYGGRLIyPDQDILNAVLKD----KI-LYLPPRYNF-QTGFYYLLKKkskeeqeLEEARKNPVIIHYTGS 242

                  ....*.
gi 1242013580 217 TKPWNY 222
Cdd:cd04194   243 DKPWNK 248
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
5-250 2.05e-12

GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases.


Pssm-ID: 133064  Cd Length: 278  Bit Score: 66.68  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580   5 AFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQ-----VSDSMRKVLETVFDDVIM--VDVLDSGDSAhltlmkr 77
Cdd:cd06914     2 AYVNYATNADYLCNALILFEQLRRLGSKAKLVLLVPETlldrnLDDFVRRDLLLARDKVIVklIPVIIASGGD------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580  78 PELGITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFE-REELS-AAPDPGWPdcFNSGVFVYQPSIETYNQLLHLASE 155
Cdd:cd06914    75 AYWAKSLTKLRAFNQTEYDRIIYFDSDSIIRHPMDELFFlPNYIKfAAPRAYWK--FASHLMVIKPSKEAFKELMTEILP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242013580 156 QGSFDGG--DQGLLNTYFSGWATTDITKH--LPF-VYNLSSISIYSYLPafKAFGKN----------------AKVVHF- 213
Cdd:cd06914   153 AYLNKKNeyDMDLINEEFYNSKQLFKPSVlvLPHrQYGLLTGEFREKLH--KSFLSNaqhlyekwdpddvfkeSKVIHFs 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1242013580 214 ---LGrtKPWNY-----TYNPQTKSVNCDSQDPTVSHpEFLNLWW 250
Cdd:cd06914   231 dspLP--KPWNYnnledIYCIEKIYCKMVKPRLEDDC-RACDLWN 272
 
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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