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Conserved domains on  [gi|2462631488|ref|XP_054184026|]
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glycogenin-2 isoform X2 [Homo sapiens]

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 ...
37-288 2.22e-111

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: 329.61  E-value: 2.22e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  37 QAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLafLKRPELGLT 116
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 117 LTKLHCWTLTHYSKCVFLDADTLVLSNVDELFDR-GEFSAAPDPGWPDCFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGA 195
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLpGEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 196 DQGLLNSFFRNWSttdIHKHLPFIYNLSSNTMYTYSPAfKQFGSSAKVVHFLGSMKPWNYKYNPQSGSVLEQGSVsssqH 275
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDDYNEL----H 230
                         250
                  ....*....|...
gi 2462631488 276 QaaflhLWWTVYQ 288
Cdd:cd02537   231 Q-----WWWDIYD 238
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
37-288 2.22e-111

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: 329.61  E-value: 2.22e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  37 QAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLafLKRPELGLT 116
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 117 LTKLHCWTLTHYSKCVFLDADTLVLSNVDELFDR-GEFSAAPDPGWPDCFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGA 195
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLpGEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 196 DQGLLNSFFRNWSttdIHKHLPFIYNLSSNTMYTYSPAfKQFGSSAKVVHFLGSMKPWNYKYNPQSGSVLEQGSVsssqH 275
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDDYNEL----H 230
                         250
                  ....*....|...
gi 2462631488 276 QaaflhLWWTVYQ 288
Cdd:cd02537   231 Q-----WWWDIYD 238
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
35-222 1.03e-26

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 109.05  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  35 TDQAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSAD---------YIHL 105
Cdd:COG5597    12 SRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDafnarhargRLHG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 106 A--FLK--RPELGLTL---TKLHCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPD--PGWPDC--FNSGVFVFQP 174
Cdd:COG5597    92 AapFTKgrKPAFHTPLdnfCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNvyESLADFhrLNSGVFTARP 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462631488 175 SLHTHKLLLQHAMEHGSF-DGADQGLLNSFFRNWsttdihkH-LPFIYNL 222
Cdd:COG5597   172 SQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNM 214
PLN00176 PLN00176
galactinol synthase
23-255 4.69e-22

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 97.07  E-value: 4.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  23 PTSASQSAGMTVTDQAFVT-LATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSK---VFDEVIEVNLID 98
Cdd:PLN00176    9 KIAASPKALAKPAKRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSqgcIVREIEPVYPPE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  99 SADYIHLAFLKrpelgLTLTKLHCWTLTHYSKCVFLDADTLVLSNVDELFD--RGEFSAAPD------------------ 158
Cdd:PLN00176   89 NQTQFAMAYYV-----INYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDlpDGYFYAVMDcfcektwshtpqykigyc 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 159 ---PG---WPD--------CFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGADQGLLNSFFRnwsttDIHKHLPFIYNLSS 224
Cdd:PLN00176  164 qqcPDkvtWPAelgpppplYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFR-----DIYKPIPPVYNLVL 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462631488 225 nTMYTYSPAFKQFgSSAKVVHFL--GSmKPWNY 255
Cdd:PLN00176  239 -AMLWRHPENVEL-DKVKVVHYCaaGS-KPWRY 268
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
40-255 7.92e-18

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: 83.14  E-value: 7.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  40 VTLATNDIYCQGALVLGQSLRRHRLTRKL-VVLITPQVSSLLRVI---LSKVFDEVIEVNLIDSADYIHLAFLK----RP 111
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALnFHIFTDDIPVENLDIlnwLASSYKPVLPLLESDIKIFEYFSKLKlrspKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 112 ELGLTLTKLHCWTLT-HYSKCVFLDADTLVLSNVDELFD----------------------RGEFSAAPDPGWPDCFNSG 168
Cdd:pfam01501  82 WSLLNYLRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 169 VFVFQPSLHTHKLLLQHAME-------HGSFDGADQGLLNSFFRnwsttDIHKHLPFIYNLSSNTMYTYSPAFKQFGSSA 241
Cdd:pfam01501 162 MLLFDLDAWRKENITERYIKwlnlnenRTLWKLGDQDPLNIVFY-----GKVKPLDPRWNVLGLGYYNKKKSLNEITENA 236
                         250
                  ....*....|....
gi 2462631488 242 KVVHFLGSMKPWNY 255
Cdd:pfam01501 237 AVIHYNGPTKPWLD 250
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
37-288 2.22e-111

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: 329.61  E-value: 2.22e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  37 QAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLafLKRPELGLT 116
Cdd:cd02537     1 EAYVTLLTNDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANL--LKRPRFKDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 117 LTKLHCWTLTHYSKCVFLDADTLVLSNVDELFDR-GEFSAAPDPGWPDCFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGA 195
Cdd:cd02537    79 YTKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLpGEFAAAPDCGWPDLFNSGVFVLKPSEETFNDLLDALQDTPSFDGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 196 DQGLLNSFFRNWSttdIHKHLPFIYNLSSNTMYTYSPAfKQFGSSAKVVHFLGSMKPWNYKYNPQSGSVLEQGSVsssqH 275
Cdd:cd02537   159 DQGLLNSYFSDRG---IWKRLPFTYNALKPLRYLHPEA-LWFGDEIKVVHFIGGDKPWSWWRDPETKEKDDYNEL----H 230
                         250
                  ....*....|...
gi 2462631488 276 QaaflhLWWTVYQ 288
Cdd:cd02537   231 Q-----WWWDIYD 238
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
37-255 1.45e-50

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: 173.01  E-value: 1.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  37 QAFVTLATNDIYCQGALVLGQSLRRHRLT-RKLVVLITPQVSSLLRVI-----LSKVFDEVIEVNLIDSAdyiHLAFLKR 110
Cdd:cd00505     1 IAIVIVATGDEYLRGAIVLMKSVLRHRTKpLRFHVLTNPLSDTFKAALdnlrkLYNFNYELIPVDILDSV---DSEHLKR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 111 PELGLTLTKLHCWTLT-HYSKCVFLDADTLVLSNVDELFDR----GEFSAAPDPGWP----------------DCFNSGV 169
Cdd:cd00505    78 PIKIVTLTKLHLPNLVpDYDKILYVDADILVLTDIDELWDTplggQELAAAPDPGDRregkyyrqkrshlagpDYFNSGV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 170 FVFQPSLHTHKLLLQHAMEHGSF-----DGADQGLLNSFFRNWSttDIHKHLPFIYNLSSNTMYTYSPAFKQFGSSAKVV 244
Cdd:cd00505   158 FVVNLSKERRNQLLKVALEKWLQslsslSGGDQDLLNTFFKQVP--FIVKSLPCIWNVRLTGCYRSLNCFKAFVKNAKVI 235
                         250
                  ....*....|.
gi 2462631488 245 HFLGSMKPWNY 255
Cdd:cd00505   236 HFNGPTKPWNK 246
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
35-222 1.03e-26

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 109.05  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  35 TDQAFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSAD---------YIHL 105
Cdd:COG5597    12 SRRAYVTLVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGARLVRVDLLPTSDafnarhargRLHG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 106 A--FLK--RPELGLTL---TKLHCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPD--PGWPDC--FNSGVFVFQP 174
Cdd:COG5597    92 AapFTKgrKPAFHTPLdnfCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPEFSAAPNvyESLADFhrLNSGVFTARP 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462631488 175 SLHTHKLLLQHAMEHGSF-DGADQGLLNSFFRNWsttdihkH-LPFIYNL 222
Cdd:COG5597   172 SQATFEAMLARLDAPGAFwRRTDQTFLQTFFPDW-------HgLPVFMNM 214
PLN00176 PLN00176
galactinol synthase
23-255 4.69e-22

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 97.07  E-value: 4.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  23 PTSASQSAGMTVTDQAFVT-LATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQVSSLLRVILSK---VFDEVIEVNLID 98
Cdd:PLN00176    9 KIAASPKALAKPAKRAYVTfLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSqgcIVREIEPVYPPE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  99 SADYIHLAFLKrpelgLTLTKLHCWTLTHYSKCVFLDADTLVLSNVDELFD--RGEFSAAPD------------------ 158
Cdd:PLN00176   89 NQTQFAMAYYV-----INYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDlpDGYFYAVMDcfcektwshtpqykigyc 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 159 ---PG---WPD--------CFNSGVFVFQPSLHTHKLLLQHAMEHGSFDGADQGLLNSFFRnwsttDIHKHLPFIYNLSS 224
Cdd:PLN00176  164 qqcPDkvtWPAelgpppplYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFR-----DIYKPIPPVYNLVL 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2462631488 225 nTMYTYSPAFKQFgSSAKVVHFL--GSmKPWNY 255
Cdd:PLN00176  239 -AMLWRHPENVEL-DKVKVVHYCaaGS-KPWRY 268
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
40-255 7.92e-18

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: 83.14  E-value: 7.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  40 VTLATNDIYCQGALVLGQSLRRHRLTRKL-VVLITPQVSSLLRVI---LSKVFDEVIEVNLIDSADYIHLAFLK----RP 111
Cdd:pfam01501   2 IALALDKNYLLGASVSIKSLLKNNSDFALnFHIFTDDIPVENLDIlnwLASSYKPVLPLLESDIKIFEYFSKLKlrspKY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 112 ELGLTLTKLHCWTLT-HYSKCVFLDADTLVLSNVDELFD----------------------RGEFSAAPDPGWPDCFNSG 168
Cdd:pfam01501  82 WSLLNYLRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDidlggkvlaavednyfqrypnfSEPIILENFGPPACYFNAG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 169 VFVFQPSLHTHKLLLQHAME-------HGSFDGADQGLLNSFFRnwsttDIHKHLPFIYNLSSNTMYTYSPAFKQFGSSA 241
Cdd:pfam01501 162 MLLFDLDAWRKENITERYIKwlnlnenRTLWKLGDQDPLNIVFY-----GKVKPLDPRWNVLGLGYYNKKKSLNEITENA 236
                         250
                  ....*....|....
gi 2462631488 242 KVVHFLGSMKPWNY 255
Cdd:pfam01501 237 AVIHYNGPTKPWLD 250
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
42-255 5.08e-16

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: 77.64  E-value: 5.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  42 LATNDIYCQGALVLGQSLRRHRLTRKLVV-LITPQVS----SLLRVILSKvFDEVIEVNLIDSADYIHLaflkrpelglt 116
Cdd:cd04194     5 FAIDDNYAPYLAVTIKSILANNSKRDYDFyILNDDISeenkKKLKELLKK-YNSSIEFIKIDNDDFKFF----------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 117 LTKLHCWTLT------------HYSKCVFLDADTLVLSNVDELFDRgEFS-----AAPDPGWPDC--------------- 164
Cdd:cd04194    73 PATTDHISYAtyyrllipdllpDYDKVLYLDADIIVLGDLSELFDI-DLGdnllaAVRDPFIEQEkkrkrrlggyddgsy 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 165 FNSGVFVFQ-PSLHTHKL---LLQHAMEHGSFDGA-DQGLLNSFFRNwsttDIhKHLPFIYNLsSNTMYTYSPA------ 233
Cdd:cd04194   152 FNSGVLLINlKKWREENItekLLELIKEYGGRLIYpDQDILNAVLKD----KI-LYLPPRYNF-QTGFYYLLKKkskeeq 225
                         250       260
                  ....*....|....*....|...
gi 2462631488 234 -FKQFGSSAKVVHFLGSMKPWNY 255
Cdd:cd04194   226 eLEEARKNPVIIHYTGSDKPWNK 248
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
40-258 1.64e-15

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 76.94  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  40 VTLATNDIYCQGALVLGQSLRRHRLTRKL-VVLITPQVSSLLRVILSKVFDE---VIEVNLIDSADYIHLAFLKR--PEl 113
Cdd:COG1442     8 IVFAIDDNYLPGLGVSIASLLENNPDRPYdFHILTDGLSDENKERLEALAAKynvSIEFIDVDDELLKDLPVSKHisKA- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 114 glTLTKLHCWTL--THYSKCVFLDADTLVLSNVDELFDRgEFS-----AAPDPGWP----------------DCFNSGVF 170
Cdd:COG1442    87 --TYYRLLIPELlpDDYDKVLYLDADTLVLGDLSELWDI-DLGgnllaAVRDGTVTgsqkkrakrlglpdddGYFNSGVL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 171 VF-QPSLHTHKL---LLQHAMEHGS-FDGADQGLLNSFFRNWSttdihKHLPFIYNLSSNTMYTYSPAFKQFG-----SS 240
Cdd:COG1442   164 LInLKKWREENItekALEFLKENPDkLKYPDQDILNIVLGGKV-----KFLPPRYNYQYSLYYELKDKSNKKEllearKN 238
                         250
                  ....*....|....*...
gi 2462631488 241 AKVVHFLGSMKPWNYKYN 258
Cdd:COG1442   239 PVIIHYTGPTKPWHKWCT 256
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
38-289 3.75e-13

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: 69.76  E-value: 3.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488  38 AFVTLATNDIYCQGALVLGQSLRRHRLTRKLVVLITPQ-----VSSLLRVILSKVFDEVIeVNLIDsadyIHLAFLKRPE 112
Cdd:cd06914     2 AYVNYATNADYLCNALILFEQLRRLGSKAKLVLLVPETlldrnLDDFVRRDLLLARDKVI-VKLIP----VIIASGGDAY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 113 LGLTLTKLHCWTLTHYSKCVFLDADTLVLSNVDELF---DRGEFsAAPDPGWPdcFNSGVFVFQPSLHTHKLLLQ--HAM 187
Cdd:cd06914    77 WAKSLTKLRAFNQTEYDRIIYFDSDSIIRHPMDELFflpNYIKF-AAPRAYWK--FASHLMVIKPSKEAFKELMTeiLPA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631488 188 EHGSFDGADQGLLNSFFRN----------------------WSTTDIHKHlpFIYNLSSNtMYTYSPafKQFGSSAKVVH 245
Cdd:cd06914   154 YLNKKNEYDMDLINEEFYNskqlfkpsvlvlphrqyglltgEFREKLHKS--FLSNAQHL-YEKWDP--DDVFKESKVIH 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462631488 246 FLGSM--KPWNYK-----YNPQSGSVLEQGSVSSSQHQAAflHLWWTVYQN 289
Cdd:cd06914   229 FSDSPlpKPWNYNnlediYCIEKIYCKMVKPRLEDDCRAC--DLWNSLYAD 277
 
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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