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Conserved domains on  [gi|2017835089|ref|XP_040186601|]
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glycogenin-1-like isoform X1 [Rana temporaria]

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 ...
83-332 4.03e-104

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: 309.96  E-value: 4.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  83 QAFVTLGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRGILREVFDEVVEVDVLDSADSVrlSLLKRPELGVT 162
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSA--NLLKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 163 FTKIRCWTLTQYTKCVFMDADTIALCNIDELFDRE-EFSAAPDSGWPDCFNSGVFVFRPSLETFGRLLKYAEDHGSFDGG 241
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 242 DQGLLNSFFGNWAtadISKHLPFIYNLSISSIYTYSPAfKQFGSEAKVVHFIGTPKPWNCKYNPQTKGIVEEEplsgnqt 321
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDDYN------- 227
                         250
                  ....*....|.
gi 2017835089 322 lPLLVLWWQTY 332
Cdd:cd02537   228 -ELHQWWWDIY 237
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
83-332 4.03e-104

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: 309.96  E-value: 4.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  83 QAFVTLGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRGILREVFDEVVEVDVLDSADSVrlSLLKRPELGVT 162
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSA--NLLKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 163 FTKIRCWTLTQYTKCVFMDADTIALCNIDELFDRE-EFSAAPDSGWPDCFNSGVFVFRPSLETFGRLLKYAEDHGSFDGG 241
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 242 DQGLLNSFFGNWAtadISKHLPFIYNLSISSIYTYSPAfKQFGSEAKVVHFIGTPKPWNCKYNPQTKGIVEEEplsgnqt 321
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDDYN------- 227
                         250
                  ....*....|.
gi 2017835089 322 lPLLVLWWQTY 332
Cdd:cd02537   228 -ELHQWWWDIY 237
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
74-341 1.89e-27

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 110.98  E-value: 1.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  74 HPCRMPVTAQAFVTLGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRGILREVFDEVVEVDVLDSADSVRLSL 153
Cdd:COG5597     5 HPDGPAGSRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDAFNARH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 154 LKRPELGVT----------------FTKIRCWTLTQYTKCVFMDADTIALCNIDELFDREEFSAAPD--SGWPDC--FNS 213
Cdd:COG5597    85 ARGRLHGAApftkgrkpafhtpldnFCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNvyESLADFhrLNS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 214 GVFVFRPSLETFGRLLKYAEDHGSF-DGGDQGLLNSFFGNWatadiskH-LPFIYNLsISSIYTYSPAFKQFGSeAKVVH 291
Cdd:COG5597   165 GVFTARPSQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNM-LQYVWFNLPELWDWPS-IRVLH 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017835089 292 FiGTPKPWnckynpqtkgivEEEPLSGNQTLPLLVLWWQTYISDVLPLLT 341
Cdd:COG5597   236 Y-QYEKPW------------QKDHAKADRLRPLIDLWHAYAGGGPIPDLA 272
PLN00176 PLN00176
galactinol synthase
64-382 4.94e-18

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 85.13  E-value: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  64 TIDSKPRLTQHPCRMPVTAQAFVT-LGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRGILRevfdevvevdv 142
Cdd:PLN00176    4 ELTVKKIAASPKALAKPAKRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILV----------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 143 lDSADSVR-LSLLKRPELGVTF---------TKIRCWTLTQYTKCVFMDADTIALCNIDELFDREE--FSAAPDS----- 205
Cdd:PLN00176   73 -SQGCIVReIEPVYPPENQTQFamayyvinySKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDgyFYAVMDCfcekt 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 206 -------------------GWPD--------CFNSGVFVFRPSLETFGRLLK---------YAEdhgsfdggdQGLLNSF 249
Cdd:PLN00176  152 wshtpqykigycqqcpdkvTWPAelgpppplYFNAGMFVFEPSLSTYEDLLEtlkitpptpFAE---------QDFLNMF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 250 FGnwataDISKHLPFIYNLSISSIYTYSPAFKQfgSEAKVVHFIGT-PKPWncKYNpqtkgivEEEPLSGNQTLPLLVL- 327
Cdd:PLN00176  223 FR-----DIYKPIPPVYNLVLAMLWRHPENVEL--DKVKVVHYCAAgSKPW--RYT-------GKEENMDREDIKMLVKk 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2017835089 328 WWQTYisdvlpllteqqvpngsenkvgriefqikNDPSIDSVEEVPAGNPDSTLP 382
Cdd:PLN00176  287 WWDIY-----------------------------NDESLDYKNFVPADEEEVKLQ 312
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
86-300 1.60e-14

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: 73.12  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  86 VTLGTNDLYCQGALVLGKSLRNHK-----TSHQLVVIVTSEVTGRMRGI---LREVFDEVVEVDVLDSADSVRLSLLKRP 157
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNsdfalNFHIFTDDIPVENLDILNWLassYKPVLPLLESDIKIFEYFSKLKLRSPKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 158 ELGVTFTKIRCWTLT-QYTKCVFMDADTIALCNIDELFD----------------------REEFSAAPDSGWPDCFNSG 214
Cdd:pfam01501  82 WSLLNYLRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 215 VFVFRPSL-------ETFGRLLKYAEDHGSFDGGDQGLLNSFF-GNWATADISkhlpfiYNLSISSIYTYSPAFKQFGSE 286
Cdd:pfam01501 162 MLLFDLDAwrkenitERYIKWLNLNENRTLWKLGDQDPLNIVFyGKVKPLDPR------WNVLGLGYYNKKKSLNEITEN 235
                         250
                  ....*....|....
gi 2017835089 287 AKVVHFIGTPKPWN 300
Cdd:pfam01501 236 AAVIHYNGPTKPWL 249
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
83-332 4.03e-104

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: 309.96  E-value: 4.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  83 QAFVTLGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRGILREVFDEVVEVDVLDSADSVrlSLLKRPELGVT 162
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSA--NLLKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 163 FTKIRCWTLTQYTKCVFMDADTIALCNIDELFDRE-EFSAAPDSGWPDCFNSGVFVFRPSLETFGRLLKYAEDHGSFDGG 241
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPgEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 242 DQGLLNSFFGNWAtadISKHLPFIYNLSISSIYTYSPAfKQFGSEAKVVHFIGTPKPWNCKYNPQTKGIVEEEplsgnqt 321
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDDYN------- 227
                         250
                  ....*....|.
gi 2017835089 322 lPLLVLWWQTY 332
Cdd:cd02537   228 -ELHQWWWDIY 237
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
83-300 5.55e-46

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: 159.91  E-value: 5.55e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  83 QAFVTLGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRG---ILREVFDEVVEVDVLDSADSVRLSLLKRPEL 159
Cdd:cd00505     1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAaldNLRKLYNFNYELIPVDILDSVDSEHLKRPIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 160 GVTFTKIRCWTLTQ-YTKCVFMDADTIALCNIDELFDR----EEFSAAPDSGWP----------------DCFNSGVFVF 218
Cdd:cd00505    81 IVTLTKLHLPNLVPdYDKILYVDADILVLTDIDELWDTplggQELAAAPDPGDRregkyyrqkrshlagpDYFNSGVFVV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 219 RPSLETFGRLLKYAEDHGSF-----DGGDQGLLNSFFGNWAtaDISKHLPFIYNLSISSIYTYSPAFKQFGSEAKVVHFI 293
Cdd:cd00505   161 NLSKERRNQLLKVALEKWLQslsslSGGDQDLLNTFFKQVP--FIVKSLPCIWNVRLTGCYRSLNCFKAFVKNAKVIHFN 238

                  ....*..
gi 2017835089 294 GTPKPWN 300
Cdd:cd00505   239 GPTKPWN 245
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
74-341 1.89e-27

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 110.98  E-value: 1.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  74 HPCRMPVTAQAFVTLGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRGILREVFDEVVEVDVLDSADSVRLSL 153
Cdd:COG5597     5 HPDGPAGSRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDAFNARH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 154 LKRPELGVT----------------FTKIRCWTLTQYTKCVFMDADTIALCNIDELFDREEFSAAPD--SGWPDC--FNS 213
Cdd:COG5597    85 ARGRLHGAApftkgrkpafhtpldnFCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNvyESLADFhrLNS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 214 GVFVFRPSLETFGRLLKYAEDHGSF-DGGDQGLLNSFFGNWatadiskH-LPFIYNLsISSIYTYSPAFKQFGSeAKVVH 291
Cdd:COG5597   165 GVFTARPSQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNM-LQYVWFNLPELWDWPS-IRVLH 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2017835089 292 FiGTPKPWnckynpqtkgivEEEPLSGNQTLPLLVLWWQTYISDVLPLLT 341
Cdd:COG5597   236 Y-QYEKPW------------QKDHAKADRLRPLIDLWHAYAGGGPIPDLA 272
PLN00176 PLN00176
galactinol synthase
64-382 4.94e-18

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 85.13  E-value: 4.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  64 TIDSKPRLTQHPCRMPVTAQAFVT-LGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRMRGILRevfdevvevdv 142
Cdd:PLN00176    4 ELTVKKIAASPKALAKPAKRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILV----------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 143 lDSADSVR-LSLLKRPELGVTF---------TKIRCWTLTQYTKCVFMDADTIALCNIDELFDREE--FSAAPDS----- 205
Cdd:PLN00176   73 -SQGCIVReIEPVYPPENQTQFamayyvinySKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDgyFYAVMDCfcekt 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 206 -------------------GWPD--------CFNSGVFVFRPSLETFGRLLK---------YAEdhgsfdggdQGLLNSF 249
Cdd:PLN00176  152 wshtpqykigycqqcpdkvTWPAelgpppplYFNAGMFVFEPSLSTYEDLLEtlkitpptpFAE---------QDFLNMF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 250 FGnwataDISKHLPFIYNLSISSIYTYSPAFKQfgSEAKVVHFIGT-PKPWncKYNpqtkgivEEEPLSGNQTLPLLVL- 327
Cdd:PLN00176  223 FR-----DIYKPIPPVYNLVLAMLWRHPENVEL--DKVKVVHYCAAgSKPW--RYT-------GKEENMDREDIKMLVKk 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2017835089 328 WWQTYisdvlpllteqqvpngsenkvgriefqikNDPSIDSVEEVPAGNPDSTLP 382
Cdd:PLN00176  287 WWDIY-----------------------------NDESLDYKNFVPADEEEVKLQ 312
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
171-300 9.02e-15

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: 73.79  E-value: 9.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 171 LTQYTKCVFMDADTIALCNIDELFDRE----EFSAAPDSGWPDC---------------FNSGVFVF-----RpSLETFG 226
Cdd:cd04194    93 LPDYDKVLYLDADIIVLGDLSELFDIDlgdnLLAAVRDPFIEQEkkrkrrlggyddgsyFNSGVLLInlkkwR-EENITE 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 227 RLLKYAEDHGSFDG-GDQGLLN-SFFGNWatadisKHLPFIYNL--SISSIYTYSPAFKQFGSEA----KVVHFIGTPKP 298
Cdd:cd04194   172 KLLELIKEYGGRLIyPDQDILNaVLKDKI------LYLPPRYNFqtGFYYLLKKKSKEEQELEEArknpVIIHYTGSDKP 245

                  ..
gi 2017835089 299 WN 300
Cdd:cd04194   246 WN 247
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
86-300 1.60e-14

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: 73.12  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  86 VTLGTNDLYCQGALVLGKSLRNHK-----TSHQLVVIVTSEVTGRMRGI---LREVFDEVVEVDVLDSADSVRLSLLKRP 157
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNsdfalNFHIFTDDIPVENLDILNWLassYKPVLPLLESDIKIFEYFSKLKLRSPKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 158 ELGVTFTKIRCWTLT-QYTKCVFMDADTIALCNIDELFD----------------------REEFSAAPDSGWPDCFNSG 214
Cdd:pfam01501  82 WSLLNYLRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 215 VFVFRPSL-------ETFGRLLKYAEDHGSFDGGDQGLLNSFF-GNWATADISkhlpfiYNLSISSIYTYSPAFKQFGSE 286
Cdd:pfam01501 162 MLLFDLDAwrkenitERYIKWLNLNENRTLWKLGDQDPLNIVFyGKVKPLDPR------WNVLGLGYYNKKKSLNEITEN 235
                         250
                  ....*....|....
gi 2017835089 287 AKVVHFIGTPKPWN 300
Cdd:pfam01501 236 AAVIHYNGPTKPWL 249
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
86-304 3.24e-14

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 73.08  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  86 VTLGTNDLYCQGALVLGKSL-RNHKTSHQLVVIVTSEVTGRMRGILRevfdevvevdvldsadsvrlSLLKRPELGVTFT 164
Cdd:COG1442     8 IVFAIDDNYLPGLGVSIASLlENNPDRPYDFHILTDGLSDENKERLE--------------------ALAAKYNVSIEFI 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 165 KIRC-----------WTLTQYTKCV-------------FMDADTIALCNIDELFDRE----EFSAAPDSGWP-------- 208
Cdd:COG1442    68 DVDDellkdlpvskhISKATYYRLLipellpddydkvlYLDADTLVLGDLSELWDIDlggnLLAAVRDGTVTgsqkkrak 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 209 --------DCFNSGVFVFrpSLE------TFGRLLKYAEDHGS-FDGGDQGLLNSFF-GNWatadisKHLPFIYNLSISS 272
Cdd:COG1442   148 rlglpdddGYFNSGVLLI--NLKkwreenITEKALEFLKENPDkLKYPDQDILNIVLgGKV------KFLPPRYNYQYSL 219
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2017835089 273 IYTYSPAFKQFG-----SEAKVVHFIGTPKPWNCKYN 304
Cdd:COG1442   220 YYELKDKSNKKEllearKNPVIIHYTGPTKPWHKWCT 256
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
84-332 7.04e-14

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: 71.69  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089  84 AFVTLGTNDLYCQGALVLGKSLRNHKTSHQLVVIVTSEVTGRmrgilreVFDEVVEVDVLDSADSVRLSLLKRPELGVT- 162
Cdd:cd06914     2 AYVNYATNADYLCNALILFEQLRRLGSKAKLVLLVPETLLDR-------NLDDFVRRDLLLARDKVIVKLIPVIIASGGd 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 163 ------FTKIRCWTLTQYTKCVFMDADTIALCNIDELF---DREEFsAAPDSGWPdcFNSGVFVFRPSLETFGRLLKYAE 233
Cdd:cd06914    75 aywaksLTKLRAFNQTEYDRIIYFDSDSIIRHPMDELFflpNYIKF-AAPRAYWK--FASHLMVIKPSKEAFKELMTEIL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017835089 234 DHGSFDGG--DQGLLNSFFGNWATADISKH--LPF-IYNL---SISSIYTYSPAFKQFGS-----------EAKVVHFIG 294
Cdd:cd06914   152 PAYLNKKNeyDMDLINEEFYNSKQLFKPSVlvLPHrQYGLltgEFREKLHKSFLSNAQHLyekwdpddvfkESKVIHFSD 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2017835089 295 TP--KPWNCKYN-------PQTKGIVEEEPLSGNQTlplLVLWWQTY 332
Cdd:cd06914   232 SPlpKPWNYNNLediycieKIYCKMVKPRLEDDCRA---CDLWNSLY 275
 
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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