NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2151565500|ref|WP_228963062|]
View 

MULTISPECIES: glycosyltransferase family 4 protein [Xanthomonas]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10160628)

glycosyltransferase family 4 protein similar to Pseudomonas aeruginosa WbpL, a bifunctional enzyme which could initiate both B-band synthesis through the addition of QuiNAc to undecaprenol phosphate, and A-band synthesis by transferring either a GalNAc or a GlcNAc residue

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
 31-273 1.73e-59

The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments.


:

Pssm-ID: 133464  Cd Length: 253  Bit Score: 191.30  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  31 LLDQPGERRNHSVATPRGGGMAIVAAILSGCVVAGMLWPASRLPVGWFAAGLILVAGVGWWDDHRPLSARLRFSIHLVAS 110
Cdd:cd06854     1 LLDIPNERSSHTKPTPRGGGIAFVLAFLLALLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 111 ASLGWLVTHYTG-------SVVDGILSAAACVVLINVWNFMDGING----LAASQAALAALAFAAVVPAAWSLVGVAVAA 179
Cdd:cd06854    81 ALALYALGPLTSlllnflpPWLIALLLLLAIVWIINLYNFMDGIDGlaggEALVVFLALALLGYLAGEPALALLALALAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 180 ACMGFLPFNFPRARIFLGDGGSGALGYVLAALLALSVAAGQVGWWIgWIPLTAFLVDAGFTLLSRMLTGQRWWEPHSQHV 259
Cdd:cd06854   161 ALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWAW-LLLLSPFLVDATVTLLRRLLRGENIFQAHRKHL 239

                         250
                  ....*....|....
gi 2151565500 260 YQRLARRLANHVPV 273
Cdd:cd06854   240 YQRLARAGKSHRKV 253
 
Name Accession Description Interval E-value
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
 31-273 1.73e-59

The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments.


Pssm-ID: 133464  Cd Length: 253  Bit Score: 191.30  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  31 LLDQPGERRNHSVATPRGGGMAIVAAILSGCVVAGMLWPASRLPVGWFAAGLILVAGVGWWDDHRPLSARLRFSIHLVAS 110
Cdd:cd06854     1 LLDIPNERSSHTKPTPRGGGIAFVLAFLLALLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 111 ASLGWLVTHYTG-------SVVDGILSAAACVVLINVWNFMDGING----LAASQAALAALAFAAVVPAAWSLVGVAVAA 179
Cdd:cd06854    81 ALALYALGPLTSlllnflpPWLIALLLLLAIVWIINLYNFMDGIDGlaggEALVVFLALALLGYLAGEPALALLALALAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 180 ACMGFLPFNFPRARIFLGDGGSGALGYVLAALLALSVAAGQVGWWIgWIPLTAFLVDAGFTLLSRMLTGQRWWEPHSQHV 259
Cdd:cd06854   161 ALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWAW-LLLLSPFLVDATVTLLRRLLRGENIFQAHRKHL 239

                         250
                  ....*....|....
gi 2151565500 260 YQRLARRLANHVPV 273
Cdd:cd06854   240 YQRLARAGKSHRKV 253
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 3-277 2.72e-47

UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440240  Cd Length: 288  Bit Score: 160.68  E-value: 2.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500   3 SLWLWCALHLTIAALGTWLLRRYALHRRLLDQPGERRNHSVATPRGGGMAIVAAILSGCVVAGMLWPASrlpVGWFAAGL 82
Cdd:COG0472     2 RLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPE---LLLLLLGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  83 ILVAGVGWWDDHRPLSARLRFSIHLVASASLGWLVTHYT-------GSVVDGILSAA----ACVVLINVWNFMDGING-- 149
Cdd:COG0472    79 LLLGLIGFLDDLLGLSARQKLLGQLLAALLLVLLLLRITsltipffGLLDLGWLYIPltvfWIVGVSNAVNLTDGLDGla 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 150 --LAASQAALAALAFAAVVPAAWSLVGVAVAAACMGFLPFNFPRARIFLGDGGS---GALGYVLAALLALSVAAGQVGWW 224
Cdd:COG0472   159 agVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSlflGFALAALAILGRQEGASLLLLLL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2151565500 225 IGWIpltaFLVDAGFTLLSRMLTGQRWWEPHSQHVYQRLARRLANHVPVTGVY 277
Cdd:COG0472   239 ILGV----PVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRF 287
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
78-201 1.09e-15

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 73.40  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  78 FAAGLILVAGVGWWDDHRPLSARLRFSIHLVASASLGWL--------------VTHYTGSVVDGILSAAACVVLINVWNF 143
Cdd:pfam00953   3 LLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLggigltslglpfggGSLELGPWLSILLTLFAIVGLTNAVNF 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2151565500 144 MDGING----LAASQAALAALAFAAVVPAAWSLVGVAVAAACMGFLPFNFPRARIFLGDGGS 201
Cdd:pfam00953  83 IDGLDGlaggVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGS 144
 
Name Accession Description Interval E-value
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
 31-273 1.73e-59

The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments.


Pssm-ID: 133464  Cd Length: 253  Bit Score: 191.30  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  31 LLDQPGERRNHSVATPRGGGMAIVAAILSGCVVAGMLWPASRLPVGWFAAGLILVAGVGWWDDHRPLSARLRFSIHLVAS 110
Cdd:cd06854     1 LLDIPNERSSHTKPTPRGGGIAFVLAFLLALLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 111 ASLGWLVTHYTG-------SVVDGILSAAACVVLINVWNFMDGING----LAASQAALAALAFAAVVPAAWSLVGVAVAA 179
Cdd:cd06854    81 ALALYALGPLTSlllnflpPWLIALLLLLAIVWIINLYNFMDGIDGlaggEALVVFLALALLGYLAGEPALALLALALAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 180 ACMGFLPFNFPRARIFLGDGGSGALGYVLAALLALSVAAGQVGWWIgWIPLTAFLVDAGFTLLSRMLTGQRWWEPHSQHV 259
Cdd:cd06854   161 ALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWAW-LLLLSPFLVDATVTLLRRLLRGENIFQAHRKHL 239

                         250
                  ....*....|....
gi 2151565500 260 YQRLARRLANHVPV 273
Cdd:cd06854   240 YQRLARAGKSHRKV 253
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 3-277 2.72e-47

UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440240  Cd Length: 288  Bit Score: 160.68  E-value: 2.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500   3 SLWLWCALHLTIAALGTWLLRRYALHRRLLDQPGERRNHSVATPRGGGMAIVAAILSGCVVAGMLWPASrlpVGWFAAGL 82
Cdd:COG0472     2 RLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPE---LLLLLLGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  83 ILVAGVGWWDDHRPLSARLRFSIHLVASASLGWLVTHYT-------GSVVDGILSAA----ACVVLINVWNFMDGING-- 149
Cdd:COG0472    79 LLLGLIGFLDDLLGLSARQKLLGQLLAALLLVLLLLRITsltipffGLLDLGWLYIPltvfWIVGVSNAVNLTDGLDGla 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 150 --LAASQAALAALAFAAVVPAAWSLVGVAVAAACMGFLPFNFPRARIFLGDGGS---GALGYVLAALLALSVAAGQVGWW 224
Cdd:COG0472   159 agVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSlflGFALAALAILGRQEGASLLLLLL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2151565500 225 IGWIpltaFLVDAGFTLLSRMLTGQRWWEPHSQHVYQRLARRLANHVPVTGVY 277
Cdd:COG0472   239 ILGV----PVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRF 287
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 38-201 2.92e-26

This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. WecA is an UDP-N-acetylglucosamine (GlcNAc):undecaprenyl-phosphate (Und-P) GlcNAc-1-phosphate transferase that catalyzes the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate molecule and N-acetylglucosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylglucosamine precursor. WecA participates in the biosynthesis of O antigen LPS in many enteric bacteria and is also involved in the biosynthesis of enterobacterial common antigen. A conserved short sequence motif and a conserved arginine at a cytosolic loop of this integral membrane protein were shown to be critical in recognition of substrate UDP-N-acetylglucosamine.


Pssm-ID: 133463  Cd Length: 249  Bit Score: 104.49  E-value: 2.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  38 RRNHSVATPRGGGMAIVAAILSGCVVAGMLWPASRLPVGWFAAGLILVAGVGWWDDHRPLSARLRFSIHLVASASL---- 113
Cdd:cd06853     1 RKVHKGPIPRLGGLAIFLGFLLALLLALLFPFFLLPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAALIVvfgg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 114 GWLVTHY----TGSVVDGILS----AAACVVLINVWNFMDGING----LAASQAALAALAFAAVVPAAWSLVGVAVAAAC 181
Cdd:cd06853    81 GVILSLLgpfgGGIILLGWLSipltVLWIVGIINAINLIDGLDGlaggVALIASLALAILALLNGQVLVALLALALAGAL 160

                         170       180
                  ....*....|....*....|
gi 2151565500 182 MGFLPFNFPRARIFLGDGGS 201
Cdd:cd06853   161 LGFLPYNFHPARIFMGDAGS 180
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
78-201 1.09e-15

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 73.40  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  78 FAAGLILVAGVGWWDDHRPLSARLRFSIHLVASASLGWL--------------VTHYTGSVVDGILSAAACVVLINVWNF 143
Cdd:pfam00953   3 LLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLggigltslglpfggGSLELGPWLSILLTLFAIVGLTNAVNF 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2151565500 144 MDGING----LAASQAALAALAFAAVVPAAWSLVGVAVAAACMGFLPFNFPRARIFLGDGGS 201
Cdd:pfam00953  83 IDGLDGlaggVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGS 144
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 35-201 1.36e-15

This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like family. This family contains both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases, which catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate. This is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. The three bacterial members MraY, WecA, and WbpL/WbcO, utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The prokaryotic enzyme-catalyzed reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly.


Pssm-ID: 133467  Cd Length: 193  Bit Score: 73.82  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  35 PGERRNHSVATPRGGGMAIVAAILSGCVVAGmlWPASRLPVGWFAAGLILVAGvGWWDD-HRPLSARLR----FSIHLVA 109
Cdd:cd06912     1 DGIQKFHTRPTPRIGGVAIFLGLLAGLLLLS--LLSGSLLLLLLLAALPAFLA-GLLEDiTKRVSPRIRllatFLSALLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 110 SASLGWLVTHYTGSVVDGILSAA---------ACVVLINVWNFMDGING----LAASQAALAALAFAAVVPAAWSLVGVA 176
Cdd:cd06912    78 VWLLGASITRLDLPGLDLLLSFPpfaiiftifAVAGVANAFNIIDGFNGlasgVAIISLLSLALVAFQVGDTDLAFLALL 157

                         170       180
                  ....*....|....*....|....*
gi 2151565500 177 VAAACMGFLPFNFPRARIFLGDGGS 201
Cdd:cd06912   158 LAGALLGFLIFNFPFGKIFLGDGGA 182
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 45-201 9.12e-12

Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the formation of the first lipid intermediate in the synthesis of bacterial cell wall peptidoglycan. It catalyzes the formation of undecaprenyl-pyrophosphoryl-N-acetylmuramoyl-pentapeptide from UDP-MurNAc-pentapeptide and undecaprenyl-phosphate. It is an integral membrane protein with possibly ten transmembrane domains.


Pssm-ID: 133462  Cd Length: 280  Bit Score: 64.43  E-value: 9.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  45 TPRGGGMAIVAAIlsgcVVAGMLWPASRLPVGWFAAGLIL-VAGVGWWDD--------HRPLSARLRFSIHLVASASLGW 115
Cdd:cd06852    11 TPTMGGILFILAI----LISTLLWADLDSPEVLLLLLLTLgFGLIGFLDDylkvvkkrNLGLSARQKLLLQFLIAIVFAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 116 LVTHYTGSVVD-------------GILSAAACVVLI----NVWNFMDGING-----LAASQAALAALAFAAVVPAAWSLV 173
Cdd:cd06852    87 LLYYFNGSGTLitlpffknglidlGILYIPFAIFVIvgssNAVNLTDGLDGlaagvSIIVALALAIIAYLAGNAVFLAVF 166

                         170       180
                  ....*....|....*....|....*...
gi 2151565500 174 GVAVAAACMGFLPFNFPRARIFLGDGGS 201
Cdd:cd06852   167 CAALVGACLGFLWFNAYPAKVFMGDTGS 194
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 45-202 1.74e-09

Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases. They catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate, which is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. One member, D-N-acetylhexosamine 1-phosphate transferase (GPT) is a eukaryotic enzyme, which is specific for UDP-GlcNAc as donor substrate and dolichol-phosphate as the membrane bound acceptor. The bacterial members MraY, WecA, and WbpL/WbcO utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic endproducts implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The eukaryotic reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for N-glycosylation. The prokaryotic reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly. Archaeal and eukaryotic enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme. Archaea possess the same N-glycosylation pathway as eukaryotes. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene.


Pssm-ID: 133460  Cd Length: 185  Bit Score: 56.54  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  45 TPRGGGMAIVAAILsgcvVAGMLWPASRLPVGWFAAGLILVAG-VGWWDDH----RPLSARLRFSIHLVASASLG----- 114
Cdd:cd06499     2 TPTMGGLAILLGFL----LGVLLYIPHSNTLILLALLSGLVAGiVGFIDDLlglkVELSEREKLLLQILAALFLLliggg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 115 -WLVTHYTGSVVDGILSAAACVVL-----INVWNFMDGINGLAASQAALAALAFAAVVPAAWSLVGVAV----AAACMGF 184
Cdd:cd06499    78 hTTVTTPLGFVLDLGIFYIPFAIIaivgaTNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLfiilAGACLGF 157

                         170
                  ....*....|....*...
gi 2151565500 185 LPFNFPRARIFLGDGGSG 202
Cdd:cd06499   158 LYFNFYPAKIFMGDTGSY 175
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 46-201 1.15e-04

UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-linked glycosylation. Evidence for the existence of the N-glycosylation pathway in archaea has emerged and genes responsible for the pathway have been identified. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene, indicating that eukaryotic and archaeal enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme, which uses a different substrate.


Pssm-ID: 133466  Cd Length: 280  Bit Score: 43.01  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500  46 PRGGGMAIVAAILSGCVVAGMLWPASRLPvgWFAAGLILVAGVGWWDDHRPLSARLRFSIHLVASASLGWLVTHYT---- 121
Cdd:cd06856    14 PEMGGIAVLLGFSLGLLFLSALTHSVEAL--ALLITSLLAGLIGLLDDILGLSQSEKVLLTALPAIPLLVLKAGNPltsl 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2151565500 122 -------GSVVDGILSAAACVVLINVWNFMDGINGLAASQAALAALAFAAVVPAAWSLVGVAVA----AACMGFLPFNFP 190
Cdd:cd06856    92 piggrvlGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIAlilvAALLAFLLYNKY 171

                         170
                  ....*....|.
gi 2151565500 191 RARIFLGDGGS 201
Cdd:cd06856   172 PAKVFPGDVGT 182
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH