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Conserved domains on  [gi|2538595538|ref|WP_294900957|]
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glycosyltransferase family 8 protein [uncultured Pedobacter sp.]

Protein Classification

glycosyltransferase family 8 protein( domain architecture ID 11444513)

glycosyltransferase family 8 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; similar to Escherichia coli lipopolysaccharide 1,2-glucosyltransferase, which adds the glucose(II) group on the galactose(I) group of LPS

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
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-289 8.02e-65

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


:

Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 205.59  E-value: 8.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   1 MENNTLNIFFVLDKNYIVPFTVALTSVLENNKDLKIQVFVLH-ELGKNEVLDIAcnFFKERYEQDVILINFEDKYFNDFF 79
Cdd:COG1442     1 MNKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTdGLSDENKERLE--ALAAKYNVSIEFIDVDDELLKDLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  80 ISEHITKAGYFKLLLGKMIPETVVSGLYIDCDIVVTGSLKDFCNRSFhdstteKETSLLAVTDVRANREIKRLNK--GGA 157
Cdd:COG1442    79 VSKHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDL------GGNLLAAVRDGTVTGSQKKRAKrlGLP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 158 NLTSYFNTGVFYANLKKWRAENMAEKMIEIGRKYGEQLVYLDQDIMNIFFKGD--------------QGELEDTYNKDAA 223
Cdd:COG1442   153 DDDGYFNSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKvkflpprynyqyslYYELKDKSNKKEL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2538595538 224 VKYTKLPIILHYLGNSKPWHYVDNSPNKHIYRKYLKMTPFKNLKPEGISLENFARKYVRLFRQKRS 289
Cdd:COG1442   233 LEARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHLRYLKG 298
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-289 8.02e-65

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 205.59  E-value: 8.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   1 MENNTLNIFFVLDKNYIVPFTVALTSVLENNKDLKIQVFVLH-ELGKNEVLDIAcnFFKERYEQDVILINFEDKYFNDFF 79
Cdd:COG1442     1 MNKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTdGLSDENKERLE--ALAAKYNVSIEFIDVDDELLKDLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  80 ISEHITKAGYFKLLLGKMIPETVVSGLYIDCDIVVTGSLKDFCNRSFhdstteKETSLLAVTDVRANREIKRLNK--GGA 157
Cdd:COG1442    79 VSKHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDL------GGNLLAAVRDGTVTGSQKKRAKrlGLP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 158 NLTSYFNTGVFYANLKKWRAENMAEKMIEIGRKYGEQLVYLDQDIMNIFFKGD--------------QGELEDTYNKDAA 223
Cdd:COG1442   153 DDDGYFNSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKvkflpprynyqyslYYELKDKSNKKEL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2538595538 224 VKYTKLPIILHYLGNSKPWHYVDNSPNKHIYRKYLKMTPFKNLKPEGISLENFARKYVRLFRQKRS 289
Cdd:COG1442   233 LEARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHLRYLKG 298
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
6-244 8.86e-46

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: 154.68  E-value: 8.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   6 LNIFFVLDKNYIVPFTVALTSVLENNKDLKIQVFVLHElGKNEVLDIACNFFKERYEQDVILINFEDKYFNDF-FISEHI 84
Cdd:cd04194     1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILND-DISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFpATTDHI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  85 TKAGYFKLLLGKMIPET--VvsgLYIDCDIVVTGSLKDFCNRSFhdstteKETSLLAVTDVRANREIKRLNK-GGANLTS 161
Cdd:cd04194    80 SYATYYRLLIPDLLPDYdkV---LYLDADIIVLGDLSELFDIDL------GDNLLAAVRDPFIEQEKKRKRRlGGYDDGS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 162 YFNTGVFYANLKKWRAENMAEKMIEIGRKYGEQLVYLDQDIMNIFFKGDQGELEDTYN---------------KDAAVKY 226
Cdd:cd04194   151 YFNSGVLLINLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNfqtgfyyllkkkskeEQELEEA 230
                         250
                  ....*....|....*...
gi 2538595538 227 TKLPIILHYLGNSKPWHY 244
Cdd:cd04194   231 RKNPVIIHYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-244 5.73e-36

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: 129.36  E-value: 5.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   7 NIFFVLDKNYIVPFTVALTSVLENNKD--LKIQVFV--LHELGKNEVLDIACNFfKERYEQDVILIN-FEDKYFNDFFIS 81
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDfaLNFHIFTddIPVENLDILNWLASSY-KPVLPLLESDIKiFEYFSKLKLRSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  82 EHITKAGYFKLLLGKMIPE--TVvsgLYIDCDIVVTGSLKDFCNrsfhdsTTEKETSLLAVTDVRANREI-----KRLNK 154
Cdd:pfam01501  80 KYWSLLNYLRLYLPDLFPKldKI---LYLDADIVVQGDLSPLWD------IDLGGKVLAAVEDNYFQRYPnfsepIILEN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 155 GGANlTSYFNTGVFYANLKKWRAENMAEKMIEIGRKYG--EQLVYLDQDIMNIFFKGDQGELEDTYN---------KDAA 223
Cdd:pfam01501 151 FGPP-ACYFNAGMLLFDLDAWRKENITERYIKWLNLNEnrTLWKLGDQDPLNIVFYGKVKPLDPRWNvlglgyynkKKSL 229
                         250       260
                  ....*....|....*....|.
gi 2538595538 224 VKYTKLPIILHYLGNSKPWHY 244
Cdd:pfam01501 230 NEITENAAVIHYNGPTKPWLD 250
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
2-288 1.85e-19

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 86.73  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   2 ENNTLNIFFVLDKNYIVPFTVALTSVLENNKD--LKIQVFVlhelgkNEVLDIACNFFKERYEQ-----DVILINFEdkY 74
Cdd:PRK15171   22 SKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDksLVFHVFT------DYISDADKQRFSALAKQyntriNIYLINCE--R 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  75 FNDFFISEHITKAGYFKLLLGKMIPETVVSGLYIDCDIVVTGSLKDFCNRSFhdstTEKETSLLaVTDVRANREIKRLNK 154
Cdd:PRK15171   94 LKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDF----AENEIAAV-VAEGDAEWWSKRAQS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 155 -GGANLTS-YFNTGVFYANLKKWRAENMAEKMIEIGR--KYGEQLVYLDQDIMNIFFKGDQGELEDTYNKDAAVKY---- 226
Cdd:PRK15171  169 lQTPGLASgYFNSGFLLINIPAWAQENISAKAIEMLAdpEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNYelkd 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2538595538 227 ------TKLPIILHYLGNSKPWHYVDNSPNKHIYRKYLKMTPFKN---LKPEGISLENFARKYvrLFRQKR 288
Cdd:PRK15171  249 svinpvNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNealLKPVNSNQLRYCAKH--MFKQKH 317
 
Name Accession Description Interval E-value
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
1-289 8.02e-65

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


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 205.59  E-value: 8.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   1 MENNTLNIFFVLDKNYIVPFTVALTSVLENNKDLKIQVFVLH-ELGKNEVLDIAcnFFKERYEQDVILINFEDKYFNDFF 79
Cdd:COG1442     1 MNKNTINIVFAIDDNYLPGLGVSIASLLENNPDRPYDFHILTdGLSDENKERLE--ALAAKYNVSIEFIDVDDELLKDLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  80 ISEHITKAGYFKLLLGKMIPETVVSGLYIDCDIVVTGSLKDFCNRSFhdstteKETSLLAVTDVRANREIKRLNK--GGA 157
Cdd:COG1442    79 VSKHISKATYYRLLIPELLPDDYDKVLYLDADTLVLGDLSELWDIDL------GGNLLAAVRDGTVTGSQKKRAKrlGLP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 158 NLTSYFNTGVFYANLKKWRAENMAEKMIEIGRKYGEQLVYLDQDIMNIFFKGD--------------QGELEDTYNKDAA 223
Cdd:COG1442   153 DDDGYFNSGVLLINLKKWREENITEKALEFLKENPDKLKYPDQDILNIVLGGKvkflpprynyqyslYYELKDKSNKKEL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2538595538 224 VKYTKLPIILHYLGNSKPWHYVDNSPNKHIYRKYLKMTPFKNLKPEGISLENFARKYVRLFRQKRS 289
Cdd:COG1442   233 LEARKNPVIIHYTGPTKPWHKWCTHPYADLYWEYLKKTPWKDIPLKKALRYKQLRKKAKHLRYLKG 298
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
6-244 8.86e-46

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: 154.68  E-value: 8.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   6 LNIFFVLDKNYIVPFTVALTSVLENNKDLKIQVFVLHElGKNEVLDIACNFFKERYEQDVILINFEDKYFNDF-FISEHI 84
Cdd:cd04194     1 MNIVFAIDDNYAPYLAVTIKSILANNSKRDYDFYILND-DISEENKKKLKELLKKYNSSIEFIKIDNDDFKFFpATTDHI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  85 TKAGYFKLLLGKMIPET--VvsgLYIDCDIVVTGSLKDFCNRSFhdstteKETSLLAVTDVRANREIKRLNK-GGANLTS 161
Cdd:cd04194    80 SYATYYRLLIPDLLPDYdkV---LYLDADIIVLGDLSELFDIDL------GDNLLAAVRDPFIEQEKKRKRRlGGYDDGS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 162 YFNTGVFYANLKKWRAENMAEKMIEIGRKYGEQLVYLDQDIMNIFFKGDQGELEDTYN---------------KDAAVKY 226
Cdd:cd04194   151 YFNSGVLLINLKKWREENITEKLLELIKEYGGRLIYPDQDILNAVLKDKILYLPPRYNfqtgfyyllkkkskeEQELEEA 230
                         250
                  ....*....|....*...
gi 2538595538 227 TKLPIILHYLGNSKPWHY 244
Cdd:cd04194   231 RKNPVIIHYTGSDKPWNK 248
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
7-244 5.73e-36

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: 129.36  E-value: 5.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   7 NIFFVLDKNYIVPFTVALTSVLENNKD--LKIQVFV--LHELGKNEVLDIACNFfKERYEQDVILIN-FEDKYFNDFFIS 81
Cdd:pfam01501   1 CIALALDKNYLLGASVSIKSLLKNNSDfaLNFHIFTddIPVENLDILNWLASSY-KPVLPLLESDIKiFEYFSKLKLRSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  82 EHITKAGYFKLLLGKMIPE--TVvsgLYIDCDIVVTGSLKDFCNrsfhdsTTEKETSLLAVTDVRANREI-----KRLNK 154
Cdd:pfam01501  80 KYWSLLNYLRLYLPDLFPKldKI---LYLDADIVVQGDLSPLWD------IDLGGKVLAAVEDNYFQRYPnfsepIILEN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 155 GGANlTSYFNTGVFYANLKKWRAENMAEKMIEIGRKYG--EQLVYLDQDIMNIFFKGDQGELEDTYN---------KDAA 223
Cdd:pfam01501 151 FGPP-ACYFNAGMLLFDLDAWRKENITERYIKWLNLNEnrTLWKLGDQDPLNIVFYGKVKPLDPRWNvlglgyynkKKSL 229
                         250       260
                  ....*....|....*....|.
gi 2538595538 224 VKYTKLPIILHYLGNSKPWHY 244
Cdd:pfam01501 230 NEITENAAVIHYNGPTKPWLD 250
PRK15171 PRK15171
lipopolysaccharide 3-alpha-galactosyltransferase;
2-288 1.85e-19

lipopolysaccharide 3-alpha-galactosyltransferase;


Pssm-ID: 185093 [Multi-domain]  Cd Length: 334  Bit Score: 86.73  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   2 ENNTLNIFFVLDKNYIVPFTVALTSVLENNKD--LKIQVFVlhelgkNEVLDIACNFFKERYEQ-----DVILINFEdkY 74
Cdd:PRK15171   22 SKNSLDIAYGIDKNFLFGCGVSIASVLLNNPDksLVFHVFT------DYISDADKQRFSALAKQyntriNIYLINCE--R 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  75 FNDFFISEHITKAGYFKLLLGKMIPETVVSGLYIDCDIVVTGSLKDFCNRSFhdstTEKETSLLaVTDVRANREIKRLNK 154
Cdd:PRK15171   94 LKSLPSTKNWTYATYFRFIIADYFIDKTDKVLYLDADIACKGSIKELIDLDF----AENEIAAV-VAEGDAEWWSKRAQS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 155 -GGANLTS-YFNTGVFYANLKKWRAENMAEKMIEIGR--KYGEQLVYLDQDIMNIFFKGDQGELEDTYNKDAAVKY---- 226
Cdd:PRK15171  169 lQTPGLASgYFNSGFLLINIPAWAQENISAKAIEMLAdpEIVSRITHLDQDVLNILLAGKVKFIDAKYNTQFSLNYelkd 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2538595538 227 ------TKLPIILHYLGNSKPWHYVDNSPNKHIYRKYLKMTPFKN---LKPEGISLENFARKYvrLFRQKR 288
Cdd:PRK15171  249 svinpvNDETVFIHYIGPTKPWHSWADYPVSQYFLKAKEASPWKNealLKPVNSNQLRYCAKH--MFKQKH 317
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
6-244 1.57e-15

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: 74.40  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538   6 LNIFFVL-DKNYIVPFTVALTSVLENNKD-LKIQVFV--LHELGKNevlDIACNFFKERYEQDVILINFEDkyFNDFFIS 81
Cdd:cd00505     1 IAIVIVAtGDEYLRGAIVLMKSVLRHRTKpLRFHVLTnpLSDTFKA---ALDNLRKLYNFNYELIPVDILD--SVDSEHL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538  82 EHITKA-GYFKLLLGKMIPEtVVSGLYIDCDIVVTGSLKDFCNrsfhdstTEKETSLLAVT---DVRANREIKRLNKGGA 157
Cdd:cd00505    76 KRPIKIvTLTKLHLPNLVPD-YDKILYVDADILVLTDIDELWD-------TPLGGQELAAApdpGDRREGKYYRQKRSHL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 158 NLTSYFNTGVFYANLKKWRAENMAEKMIEIGRKYGEQLVYLDQDIMNIFFKGDQG------------ELEDTYNKDAAVK 225
Cdd:cd00505   148 AGPDYFNSGVFVVNLSKERRNQLLKVALEKWLQSLSSLSGGDQDLLNTFFKQVPFivkslpciwnvrLTGCYRSLNCFKA 227
                         250
                  ....*....|....*....
gi 2538595538 226 YTKLPIILHYLGNSKPWHY 244
Cdd:cd00505   228 FVKNAKVIHFNGPTKPWNK 246
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
162-255 4.89e-06

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: 46.87  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 162 YFNTGVFYanLKKwrAENMAEKMIEiGRKYGEQLVYLDQDIMNIFFKGDQG--ELEDTYNKDAAVKYTKLP--------I 231
Cdd:cd02537   127 LFNSGVFV--LKP--SEETFNDLLD-ALQDTPSFDGGDQGLLNSYFSDRGIwkRLPFTYNALKPLRYLHPEalwfgdeiK 201
                          90       100
                  ....*....|....*....|....
gi 2538595538 232 ILHYLGNSKPWHYVDNSPNKHIYR 255
Cdd:cd02537   202 VVHFIGGDKPWSWWRDPETKEKDD 225
GT8_like_1 cd06429
GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of ...
163-259 2.07e-04

GT8_like_1 represents a subfamily of GT8 with unknown function; A subfamily of glycosyltransferase family 8 with unknown function: Glycosyltransferase family 8 comprises enzymes with a number of known activities; lipopolysaccharide galactosyltransferase lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase and inositol 1-alpha-galactosyltransferase. It is classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed.


Pssm-ID: 133051 [Multi-domain]  Cd Length: 257  Bit Score: 41.99  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538595538 163 FNTGVFYANLKKWRAENMA---EKMIEIGRKYGEQLVYL-DQDIMNIFFKGDQGELEDTYN-----KDAAVKYT--KLPI 231
Cdd:cd06429   150 WNPGVNVVNLTEWRRQNVTetyEKWMELNQEEEVTLWKLiTLPPGLIVFYGLTSPLDPSWHvrglgYNYGIRPQdiKAAA 229
                          90       100
                  ....*....|....*....|....*...
gi 2538595538 232 ILHYLGNSKPWHYVDNSPNKHIYRKYLK 259
Cdd:cd06429   230 VLHFNGNMKPWLRTAIPSYKELWEKYLS 257
 
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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