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Conserved domains on  [gi|15237827|ref|NP_197768|]
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galactinol synthase 5 [Arabidopsis thaliana]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 10791266)

glycosyltransferase family 8 protein similar to galactinol synthase that catalyzes the first step in the biosynthesis of raffinose family oligosaccharides (RFOs) in plants

CATH:  3.90.550.10
CAZY:  GT8
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN00176 PLN00176
galactinol synthase
1-333 0e+00

galactinol synthase


:

Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 670.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827    1 MTMTVEKRIEADVTVSHeGVERAYVTFLAGNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGCIIRDI 80
Cdd:PLN00176   3 PELTVKKIAASPKALAK-PAKRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQGCIVREI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827   81 EPVYPPENTTGYSMAYYVINYSKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPRGYLYAVKDCFCEVSWSKTPQYKIG 160
Cdd:PLN00176  82 EPVYPPENQTQFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDGYFYAVMDCFCEKTWSHTPQYKIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  161 YCQQSPEKVTWPVEsLGAPPPVYFNAGMLVFGPNLVTYEDLLRVVQITTPTYFAEQDFLNIYFRDIYKPIPSTYNLVMAM 240
Cdd:PLN00176 162 YCQQCPDKVTWPAE-LGPPPPLYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFRDIYKPIPPVYNLVLAM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  241 LWRHPEHIDLDQISVVHYCANGSKPWKFDEAEEHMDREDIKMLVKKWWEIYEDSSLDYKNFV---ETESKLNPVTATLAS 317
Cdd:PLN00176 241 LWRHPENVELDKVKVVHYCAAGSKPWRYTGKEENMDREDIKMLVKKWWDIYNDESLDYKNFVpadEEEVKLQPFIAALSE 320
                        330
                 ....*....|....*.
gi 15237827  318 KKLVGDVltsLAPSAA 333
Cdd:PLN00176 321 AGVVSYV---PAPSAA 333
 
Name Accession Description Interval E-value
PLN00176 PLN00176
galactinol synthase
1-333 0e+00

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 670.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827    1 MTMTVEKRIEADVTVSHeGVERAYVTFLAGNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGCIIRDI 80
Cdd:PLN00176   3 PELTVKKIAASPKALAK-PAKRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQGCIVREI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827   81 EPVYPPENTTGYSMAYYVINYSKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPRGYLYAVKDCFCEVSWSKTPQYKIG 160
Cdd:PLN00176  82 EPVYPPENQTQFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDGYFYAVMDCFCEKTWSHTPQYKIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  161 YCQQSPEKVTWPVEsLGAPPPVYFNAGMLVFGPNLVTYEDLLRVVQITTPTYFAEQDFLNIYFRDIYKPIPSTYNLVMAM 240
Cdd:PLN00176 162 YCQQCPDKVTWPAE-LGPPPPLYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFRDIYKPIPPVYNLVLAM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  241 LWRHPEHIDLDQISVVHYCANGSKPWKFDEAEEHMDREDIKMLVKKWWEIYEDSSLDYKNFV---ETESKLNPVTATLAS 317
Cdd:PLN00176 241 LWRHPENVELDKVKVVHYCAAGSKPWRYTGKEENMDREDIKMLVKKWWDIYNDESLDYKNFVpadEEEVKLQPFIAALSE 320
                        330
                 ....*....|....*.
gi 15237827  318 KKLVGDVltsLAPSAA 333
Cdd:PLN00176 321 AGVVSYV---PAPSAA 333
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
22-294 2.32e-89

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: 267.59  E-value: 2.32e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  22 RAYVTFLAgNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGCIIRDIEPVYPPENTTGYSMAYYVINY 101
Cdd:cd02537   1 EAYVTLLT-NDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANLLKRPRFKDTY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 102 SKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPrGYLYAVKDCFCevswsktpqykigycqqspekvtwpveslgappP 181
Cdd:cd02537  80 TKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLP-GEFAAAPDCGW---------------------------------P 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 182 VYFNAGMLVFGPNLVTYEDLLRVVQITTPTYFAEQDFLNIYFRD--IYKPIPSTYNLVMAMLWRHPE-HIDLDQISVVHY 258
Cdd:cd02537 126 DLFNSGVFVLKPSEETFNDLLDALQDTPSFDGGDQGLLNSYFSDrgIWKRLPFTYNALKPLRYLHPEaLWFGDEIKVVHF 205
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15237827 259 CAnGSKPWKFDEAEEHMDREDIKMLVKKWWEIYEDS 294
Cdd:cd02537 206 IG-GDKPWSWWRDPETKEKDDYNELHQWWWDIYDEL 240
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
25-269 2.58e-57

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: 185.99  E-value: 2.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827    25 VTFLAGNKDYWMLVVGLAKGLRKVKS-AYPLVVATLPDVPEEHRQILVDQGCIIRDIEPVYPPE---------NTTGYSM 94
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSdFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDikifeyfskLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827    95 AYYVINYSKLRIWE-FVEYEKMIYLDGDIQVFKNIDHLFDTPRG--YLYAVKDcfcevswsktpqykiGYCQQSPEKVTW 171
Cdd:pfam01501  81 YWSLLNYLRLYLPDlFPKLDKILYLDADIVVQGDLSPLWDIDLGgkVLAAVED---------------NYFQRYPNFSEP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827   172 PVESLGAPPPVYFNAGMLVFGPNLVTYEDLLRVVQIT-------TPTYFAEQDFLNIYFRDIYKPIPSTYNLVMAM--LW 242
Cdd:pfam01501 146 IILENFGPPACYFNAGMLLFDLDAWRKENITERYIKWlnlnenrTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGyyNK 225
                         250       260
                  ....*....|....*....|....*..
gi 15237827   243 RHPEHIDLDQISVVHYCANgSKPWKFD 269
Cdd:pfam01501 226 KKSLNEITENAAVIHYNGP-TKPWLDI 251
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
19-293 2.41e-24

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 100.20  E-value: 2.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  19 GVERAYVTfLAGNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGC-IIR-DIEPVYPPEN-------- 88
Cdd:COG5597  11 GSRRAYVT-LVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGArLVRvDLLPTSDAFNarhargrl 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  89 ------TTGYSMAYY--VINYSKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPRgylyavkdcFCevswsktpqykig 160
Cdd:COG5597  90 hgaapfTKGRKPAFHtpLDNFCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPE---------FS------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 161 ycqqspekvtwpveslgAPPPVY--------FNAGMLVFGPNLVTYEDLLrvVQITTPTYF---AEQDFLNIYFRDiYKP 229
Cdd:COG5597 148 -----------------AAPNVYesladfhrLNSGVFTARPSQATFEAML--ARLDAPGAFwrrTDQTFLQTFFPD-WHG 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237827 230 IPSTYNLVMAMLWRHPEHIDLDQISVVHYcaNGSKPWKFDeaeeHMDREDIKMLVKKWWEIYED 293
Cdd:COG5597 208 LPVFMNMLQYVWFNLPELWDWPSIRVLHY--QYEKPWQKD----HAKADRLRPLIDLWHAYAGG 265
 
Name Accession Description Interval E-value
PLN00176 PLN00176
galactinol synthase
1-333 0e+00

galactinol synthase


Pssm-ID: 215090 [Multi-domain]  Cd Length: 333  Bit Score: 670.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827    1 MTMTVEKRIEADVTVSHeGVERAYVTFLAGNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGCIIRDI 80
Cdd:PLN00176   3 PELTVKKIAASPKALAK-PAKRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAVLPDVPEEHRRILVSQGCIVREI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827   81 EPVYPPENTTGYSMAYYVINYSKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPRGYLYAVKDCFCEVSWSKTPQYKIG 160
Cdd:PLN00176  82 EPVYPPENQTQFAMAYYVINYSKLRIWEFVEYSKMIYLDGDIQVFENIDHLFDLPDGYFYAVMDCFCEKTWSHTPQYKIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  161 YCQQSPEKVTWPVEsLGAPPPVYFNAGMLVFGPNLVTYEDLLRVVQITTPTYFAEQDFLNIYFRDIYKPIPSTYNLVMAM 240
Cdd:PLN00176 162 YCQQCPDKVTWPAE-LGPPPPLYFNAGMFVFEPSLSTYEDLLETLKITPPTPFAEQDFLNMFFRDIYKPIPPVYNLVLAM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  241 LWRHPEHIDLDQISVVHYCANGSKPWKFDEAEEHMDREDIKMLVKKWWEIYEDSSLDYKNFV---ETESKLNPVTATLAS 317
Cdd:PLN00176 241 LWRHPENVELDKVKVVHYCAAGSKPWRYTGKEENMDREDIKMLVKKWWDIYNDESLDYKNFVpadEEEVKLQPFIAALSE 320
                        330
                 ....*....|....*.
gi 15237827  318 KKLVGDVltsLAPSAA 333
Cdd:PLN00176 321 AGVVSYV---PAPSAA 333
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
22-294 2.32e-89

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: 267.59  E-value: 2.32e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  22 RAYVTFLAgNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGCIIRDIEPVYPPENTTGYSMAYYVINY 101
Cdd:cd02537   1 EAYVTLLT-NDDYLPGALVLGYSLRKVGSSYDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDSANLLKRPRFKDTY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 102 SKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPrGYLYAVKDCFCevswsktpqykigycqqspekvtwpveslgappP 181
Cdd:cd02537  80 TKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLP-GEFAAAPDCGW---------------------------------P 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 182 VYFNAGMLVFGPNLVTYEDLLRVVQITTPTYFAEQDFLNIYFRD--IYKPIPSTYNLVMAMLWRHPE-HIDLDQISVVHY 258
Cdd:cd02537 126 DLFNSGVFVLKPSEETFNDLLDALQDTPSFDGGDQGLLNSYFSDrgIWKRLPFTYNALKPLRYLHPEaLWFGDEIKVVHF 205
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15237827 259 CAnGSKPWKFDEAEEHMDREDIKMLVKKWWEIYEDS 294
Cdd:cd02537 206 IG-GDKPWSWWRDPETKEKDDYNELHQWWWDIYDEL 240
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
25-269 2.58e-57

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: 185.99  E-value: 2.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827    25 VTFLAGNKDYWMLVVGLAKGLRKVKS-AYPLVVATLPDVPEEHRQILVDQGCIIRDIEPVYPPE---------NTTGYSM 94
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSdFALNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDikifeyfskLKLRSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827    95 AYYVINYSKLRIWE-FVEYEKMIYLDGDIQVFKNIDHLFDTPRG--YLYAVKDcfcevswsktpqykiGYCQQSPEKVTW 171
Cdd:pfam01501  81 YWSLLNYLRLYLPDlFPKLDKILYLDADIVVQGDLSPLWDIDLGgkVLAAVED---------------NYFQRYPNFSEP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827   172 PVESLGAPPPVYFNAGMLVFGPNLVTYEDLLRVVQIT-------TPTYFAEQDFLNIYFRDIYKPIPSTYNLVMAM--LW 242
Cdd:pfam01501 146 IILENFGPPACYFNAGMLLFDLDAWRKENITERYIKWlnlnenrTLWKLGDQDPLNIVFYGKVKPLDPRWNVLGLGyyNK 225
                         250       260
                  ....*....|....*....|....*..
gi 15237827   243 RHPEHIDLDQISVVHYCANgSKPWKFD 269
Cdd:pfam01501 226 KKSLNEITENAAVIHYNGP-TKPWLDI 251
Gnt1 COG5597
N-acetylglucosaminyl transferase [Cell wall/membrane/envelope biogenesis];
19-293 2.41e-24

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


Pssm-ID: 444333 [Multi-domain]  Cd Length: 279  Bit Score: 100.20  E-value: 2.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  19 GVERAYVTfLAGNKDYWMLVVGLAKGLRKVKSAYPLVVATLPDVPEEHRQILVDQGC-IIR-DIEPVYPPEN-------- 88
Cdd:COG5597  11 GSRRAYVT-LVTNADYALGATALLRSLRRTGTTADIVVLHTGGVPAAALAPLAALGArLVRvDLLPTSDAFNarhargrl 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  89 ------TTGYSMAYY--VINYSKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTPRgylyavkdcFCevswsktpqykig 160
Cdd:COG5597  90 hgaapfTKGRKPAFHtpLDNFCKLRLWQLVEYDRVVFIDADALVLRNIDRLFDYPE---------FS------------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 161 ycqqspekvtwpveslgAPPPVY--------FNAGMLVFGPNLVTYEDLLrvVQITTPTYF---AEQDFLNIYFRDiYKP 229
Cdd:COG5597 148 -----------------AAPNVYesladfhrLNSGVFTARPSQATFEAML--ARLDAPGAFwrrTDQTFLQTFFPD-WHG 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237827 230 IPSTYNLVMAMLWRHPEHIDLDQISVVHYcaNGSKPWKFDeaeeHMDREDIKMLVKKWWEIYED 293
Cdd:COG5597 208 LPVFMNMLQYVWFNLPELWDWPSIRVLHY--QYEKPWQKD----HAKADRLRPLIDLWHAYAGG 265
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
101-269 3.86e-17

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 80.40  E-value: 3.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 101 YSKLRIWEFV--EYEKMIYLDGDIQVFKNIDHLFDTPRG--YLYAVKDCFCEVSWSKtpqykigycqqspekvtwPVESL 176
Cdd:COG1442  88 YYRLLIPELLpdDYDKVLYLDADTLVLGDLSELWDIDLGgnLLAAVRDGTVTGSQKK------------------RAKRL 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 177 GAPPPV-YFNAGMLVFgpNL------VTYEDLLRVVQITTPTY-FAEQDFLNIYFRDIYKPIPSTYNLVMAMLWRHPEHI 248
Cdd:COG1442 150 GLPDDDgYFNSGVLLI--NLkkwreeNITEKALEFLKENPDKLkYPDQDILNIVLGGKVKFLPPRYNYQYSLYYELKDKS 227
                       170       180
                ....*....|....*....|....*...
gi 15237827 249 DLDQIS-------VVHYCAnGSKPWKFD 269
Cdd:COG1442 228 NKKELLearknpvIIHYTG-PTKPWHKW 254
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
61-268 1.21e-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: 78.03  E-value: 1.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  61 DVPEEHRQIL------VDQGCIIRDIEPVY---PPENTTGYS-MAYYvinysKLRIWEFV-EYEKMIYLDGDIQVFKNID 129
Cdd:cd04194  39 DISEENKKKLkellkkYNSSIEFIKIDNDDfkfFPATTDHISyATYY-----RLLIPDLLpDYDKVLYLDADIIVLGDLS 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 130 HLFDTPRG--YLYAVKDCFCEVSWSKTPQYKigycqqspekvtwpveslGAPPPVYFNAGMLVFgpNL------VTYEDL 201
Cdd:cd04194 114 ELFDIDLGdnLLAAVRDPFIEQEKKRKRRLG------------------GYDDGSYFNSGVLLI--NLkkwreeNITEKL 173
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15237827 202 LRVVQITTPTYFA-EQDFLNIYFRDIYKPIPSTYNLVMAMLWRHPEHIDLDQ--------ISVVHYCanGS-KPWKF 268
Cdd:cd04194 174 LELIKEYGGRLIYpDQDILNAVLKDKILYLPPRYNFQTGFYYLLKKKSKEEQeleearknPVIIHYT--GSdKPWNK 248
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
101-267 6.93e-11

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: 61.69  E-value: 6.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 101 YSKLRIWEFV-EYEKMIYLDGDIQVFKNIDHLFDTPRG--YLYAVKDCFcevsWSKTPQYKIgycqqspEKVTWPVEslg 177
Cdd:cd00505  84 LTKLHLPNLVpDYDKILYVDADILVLTDIDELWDTPLGgqELAAAPDPG----DRREGKYYR-------QKRSHLAG--- 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827 178 appPVYFNAGMLVFGPNLVTYEDLLRVV-----QITTPTYFAEQDFLNIYFR---DIYKPIPSTYNlvmamlWRHPEHID 249
Cdd:cd00505 150 ---PDYFNSGVFVVNLSKERRNQLLKVAlekwlQSLSSLSGGDQDLLNTFFKqvpFIVKSLPCIWN------VRLTGCYR 220
                       170       180
                ....*....|....*....|....*.
gi 15237827 250 --------LDQISVVHYCaNGSKPWK 267
Cdd:cd00505 221 slncfkafVKNAKVIHFN-GPTKPWN 245
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
23-135 9.24e-07

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: 49.73  E-value: 9.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237827  23 AYVTFlAGNKDYWMLVVGLAKGLRKVKSAYPLVV---ATLPDVPEE--HRQILVdqgcIIRDIEPVYPPENT-TGYSMAY 96
Cdd:cd06914   2 AYVNY-ATNADYLCNALILFEQLRRLGSKAKLVLlvpETLLDRNLDdfVRRDLL----LARDKVIVKLIPVIiASGGDAY 76
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15237827  97 YVINYSKLRIWEFVEYEKMIYLDGDIQVFKNIDHLFDTP 135
Cdd:cd06914  77 WAKSLTKLRAFNQTEYDRIIYFDSDSIIRHPMDELFFLP 115
 
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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