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Conserved domains on  [gi|499595672|ref|WP_011276406|]
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MULTISPECIES: glycosyltransferase family 4 protein [Staphylococcus]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10001440)

glycosyltransferase family 4 protein such as undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase, which catalyzes the formation of a phosphodiester bond between a decaprenyl- or undecaprenyl-phosphate molecule, respectively, and N-acetylglucosamine 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 1-289 1.48e-95

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: 285.87  E-value: 1.48e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672   1 MYTLLLIAVTLVISLILTPMIIKVSIKFDLVDRPNFRKVHTKPVSVLGGTVILLSFLIGIWLGHPIE-REVKPLVMGAIV 79
Cdd:COG0472    1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSnPELLLLLLGALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  80 MYLVGLIDDIYDLKPILKLIGQIVAASIVAFYGITIDFISFPMGPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASG 159
Cdd:COG0472   81 LGLIGFLDDLLGLSARQKLLGQLLAALLLVLLLLRITSLTIPFFGLLDLGWLYIPLTVFWIVGVSNAVNLTDGLDGLAAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 160 VSAIGLITIAFIAILQANVFIIMICSVLIGSLLGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLGfkNITFISLFFPIV 239
Cdd:COG0472  161 VSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILG--RQEGASLLLLLL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 499595672 240 ILAVPFIDTLFAMIRRMRNGQHIMQADKSHLHHKLLALGYSHRQTVLLIY 289
Cdd:COG0472  239 ILGVPVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRFW 288
 
Name Accession Description Interval E-value
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 1-289 1.48e-95

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: 285.87  E-value: 1.48e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672   1 MYTLLLIAVTLVISLILTPMIIKVSIKFDLVDRPNFRKVHTKPVSVLGGTVILLSFLIGIWLGHPIE-REVKPLVMGAIV 79
Cdd:COG0472    1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSnPELLLLLLGALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  80 MYLVGLIDDIYDLKPILKLIGQIVAASIVAFYGITIDFISFPMGPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASG 159
Cdd:COG0472   81 LGLIGFLDDLLGLSARQKLLGQLLAALLLVLLLLRITSLTIPFFGLLDLGWLYIPLTVFWIVGVSNAVNLTDGLDGLAAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 160 VSAIGLITIAFIAILQANVFIIMICSVLIGSLLGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLGfkNITFISLFFPIV 239
Cdd:COG0472  161 VSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILG--RQEGASLLLLLL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 499595672 240 ILAVPFIDTLFAMIRRMRNGQHIMQADKSHLHHKLLALGYSHRQTVLLIY 289
Cdd:COG0472  239 ILGVPVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRFW 288
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 37-279 1.86e-89

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: 268.97  E-value: 1.86e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  37 RKVHTKPVSVLGGTVILLSFLIGIWLGHPIE----REVKPLVMGAIVMYLVGLIDDIYDLKPILKLIGQIVAASIVAFYG 112
Cdd:cd06853    1 RKVHKGPIPRLGGLAIFLGFLLALLLALLFPffllPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAALIVVFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 113 ITIDFISFPM-GPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIGSL 191
Cdd:cd06853   81 GVILSLLGPFgGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLVALLALALAGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 192 LGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLG-FKNITFISLFFPIVILAVPFIDTLFAMIRRMRNGQHIMQADKSHL 270
Cdd:cd06853  161 LGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGtQKSSTAISPVVPLLILAVPLFDTLFVIIRRLLRGRSPFQADRDHL 240


                 ....*....
gi 499595672 271 HHKLLALGY 279
Cdd:cd06853  241 HHRLLRLGL 249
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
73-225 4.03e-36

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 128.49  E-value: 4.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672   73 LVMGAIVMYLVGLIDDIYDLKPILKLIGQIVAASIVAFY---GITIDFISFPMGPTIHFGILSIPITIIWIVAITNAINL 149
Cdd:pfam00953   3 LLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLggiGLTSLGLPFGGGSLELGPWLSILLTLFAIVGLTNAVNF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595672  150 IDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIGSLLGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLG 225
Cdd:pfam00953  83 IDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLAIIG 158
 
Name Accession Description Interval E-value
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 1-289 1.48e-95

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: 285.87  E-value: 1.48e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672   1 MYTLLLIAVTLVISLILTPMIIKVSIKFDLVDRPNFRKVHTKPVSVLGGTVILLSFLIGIWLGHPIE-REVKPLVMGAIV 79
Cdd:COG0472    1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSnPELLLLLLGALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  80 MYLVGLIDDIYDLKPILKLIGQIVAASIVAFYGITIDFISFPMGPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASG 159
Cdd:COG0472   81 LGLIGFLDDLLGLSARQKLLGQLLAALLLVLLLLRITSLTIPFFGLLDLGWLYIPLTVFWIVGVSNAVNLTDGLDGLAAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 160 VSAIGLITIAFIAILQANVFIIMICSVLIGSLLGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLGfkNITFISLFFPIV 239
Cdd:COG0472  161 VSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILG--RQEGASLLLLLL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 499595672 240 ILAVPFIDTLFAMIRRMRNGQHIMQADKSHLHHKLLALGYSHRQTVLLIY 289
Cdd:COG0472  239 ILGVPVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRFW 288
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 37-279 1.86e-89

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: 268.97  E-value: 1.86e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  37 RKVHTKPVSVLGGTVILLSFLIGIWLGHPIE----REVKPLVMGAIVMYLVGLIDDIYDLKPILKLIGQIVAASIVAFYG 112
Cdd:cd06853    1 RKVHKGPIPRLGGLAIFLGFLLALLLALLFPffllPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAALIVVFGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 113 ITIDFISFPM-GPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIGSL 191
Cdd:cd06853   81 GVILSLLGPFgGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLVALLALALAGAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 192 LGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLG-FKNITFISLFFPIVILAVPFIDTLFAMIRRMRNGQHIMQADKSHL 270
Cdd:cd06853  161 LGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGtQKSSTAISPVVPLLILAVPLFDTLFVIIRRLLRGRSPFQADRDHL 240


                 ....*....
gi 499595672 271 HHKLLALGY 279
Cdd:cd06853  241 HHRLLRLGL 249
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
 30-284 8.64e-47

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: 159.72  E-value: 8.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  30 LVDRPNFRKVHTKPVSVLGGTVILLSFLIGI----WLGHPIEREVKPLVMGAIVMYLVGLIDDIYDLKPILKLIGQIVAA 105
Cdd:cd06854    1 LLDIPNERSSHTKPTPRGGGIAFVLAFLLALllaaAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 106 sIVAFYGITIDFISFPMgptIHFGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQANVFIIMICS 185
Cdd:cd06854   81 -ALALYALGPLTSLLLN---FLPPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAGEPALALLAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 186 VLIGSLLGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLGFknITFISLFFPIVILAVPFIDTLFAMIRRMRNGQHIMQA 265
Cdd:cd06854  157 ALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLA--LSGQSPWAWLLLLSPFLVDATVTLLRRLLRGENIFQA 234

                        250
                 ....*....|....*....
gi 499595672 266 DKSHLHHKLLALGYSHRQT 284
Cdd:cd06854  235 HRKHLYQRLARAGKSHRKV 253
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
73-225 4.03e-36

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 128.49  E-value: 4.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672   73 LVMGAIVMYLVGLIDDIYDLKPILKLIGQIVAASIVAFY---GITIDFISFPMGPTIHFGILSIPITIIWIVAITNAINL 149
Cdd:pfam00953   3 LLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLggiGLTSLGLPFGGGSLELGPWLSILLTLFAIVGLTNAVNF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499595672  150 IDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIGSLLGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLG 225
Cdd:pfam00953  83 IDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLAIIG 158
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 48-302 1.85e-35

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: 130.69  E-value: 1.85e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  48 GGTVILLSFLIGIWLGHPIE-REVKPLVMGAIVMYLVGLIDDI--------YDLKPILKLIGQIVAASIVAFY-----GI 113
Cdd:cd06852   15 GGILFILAILISTLLWADLDsPEVLLLLLLTLGFGLIGFLDDYlkvvkkrnLGLSARQKLLLQFLIAIVFALLlyyfnGS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 114 TIDFIS-FPMGPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQAN-VFIIMICSVLIGSL 191
Cdd:cd06852   95 GTLITLpFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAGNaVFLAVFCAALVGAC 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 192 LGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLgfknitfISLFFPIVILA-VPFIDTLFAM------------IRRMrn 258
Cdd:cd06852  175 LGFLWFNAYPAKVFMGDTGSLALGGALAALAIL-------TKQELLLLIIGgVFVIEALSVIlqvgsfkltgkrIFKM-- 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499595672 259 gqhimqadkSHLHHKLLALGYSHRQTVLLIYSIAILFSLSSIIL 302
Cdd:cd06852  246 ---------APLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 43-219 5.29e-31

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: 115.86  E-value: 5.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  43 PVSVLGGTVILLSFLIGIWLGHPIE-REVKPLVMGAIVMYLVGLIDDIYDLKPIL----KLIGQIVAASIVAFYGITIDF 117
Cdd:cd06499    1 PTPTMGGLAILLGFLLGVLLYIPHSnTLILLALLSGLVAGIVGFIDDLLGLKVELsereKLLLQILAALFLLLIGGGHTT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 118 ISFPMGPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIGSLLGFLCF 197
Cdd:cd06499   81 VTTPLGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLFIILAGACLGFLYF 160

                        170       180
                 ....*....|....*....|..
gi 499595672 198 NFHPAKIFLGDSGALLIGFIIG 219
Cdd:cd06499  161 NFYPAKIFMGDTGSYFLGAAYA 182
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 34-222 2.68e-30

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: 114.26  E-value: 2.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  34 PNFRKVHTKPVSVLGGTVILLSFLIGIWLGHPIEREVK-PLVMGAIVMYLVGLIDDI-YDLKPILKLIGQIVAASI-VAF 110
Cdd:cd06912    1 DGIQKFHTRPTPRIGGVAIFLGLLAGLLLLSLLSGSLLlLLLLAALPAFLAGLLEDItKRVSPRIRLLATFLSALLaVWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 111 YGITIDFISFPMGPTIH-FGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIG 189
Cdd:cd06912   81 LGASITRLDLPGLDLLLsFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDTDLAFLALLLAG 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 499595672 190 SLLGFLCFNFHPAKIFLGDSGALLIGFIIGFLS 222
Cdd:cd06912  161 ALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 47-240 2.87e-25

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: 103.10  E-value: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  47 LGGTVILLSFLIGIWLGHPIEREVKPLVMGAIVM--YLVGLIDDIYDLKPILKLIGQIVAASIVAFYGITIDFISFPMGP 124
Cdd:cd06856   16 MGGIAVLLGFSLGLLFLSALTHSVEALALLITSLlaGLIGLLDDILGLSQSEKVLLTALPAIPLLVLKAGNPLTSLPIGG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 125 TIHFGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIGSLLGFLCFNFHPAKI 204
Cdd:cd06856   96 RVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIALILVAALLAFLLYNKYPAKV 175

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499595672 205 FLGDSGALLIGFIIGFLSLLGFKNITFISLFFPIVI 240
Cdd:cd06856  176 FPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVI 211
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 43-240 4.54e-17

This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and archaeal GPT-like glycosyltransferases. 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. GPT activity has been identified in all eukaryotic cells examined to date. 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 archaeal gene, indicating eukaryotic and archaeal enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme, which uses a different substrate.


Pssm-ID: 133461  Cd Length: 223  Bit Score: 79.08  E-value: 4.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  43 PVSVLGGTVILLSFLIGIWLGHPIEREVKP---------LVMGAIVMYLVGLIDDIYDLKPILKLIGQIVAAS---IVAF 110
Cdd:cd06851   12 MIPEPGGISILIGFVASEITLIFFPFLSFPhfpiseilaALITSVLGFSVGIIDDRLTMGGWFKPVALAFAAApilLLGA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 111 YGITIDFISFpmGPTIHFGILSIPITIIWIVAITNAINLIDGLDGLASGVSAIGLITIAFIAILQANVFIIMICSVLIGS 190
Cdd:cd06851   92 YDSNLDFPLF--GGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQNYEIGIACLCLAFA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 499595672 191 LLGFLCFNFHPAKIFLGDSGALLIGFIIGFLSLLGFKNITFISLFFPIVI 240
Cdd:cd06851  170 SLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIAAVAFIPAII 219
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
 78-240 1.61e-09

UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (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-glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. A series of six conserved motifs designated A through F, ranging in length from 5 to 13 amino acid residues, has been identified in this family. They have been determined to be important for stable expression, substrate binding, or catalytic activities.


Pssm-ID: 133465  Cd Length: 283  Bit Score: 58.03  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672  78 IVMYLVGLIDDIYDLKPILKLIGQIVAA---SIVAFYGITIDFISFPMGPTIHFGILSIPITIIWIVAI----TNAINLI 150
Cdd:cd06855   70 CCMTFLGFADDVLDLRWRHKLILPTFASlplLMVYYGNTGITLPIVPLRPLLGTLIDLGILYYVYMILLavfcTNSINIY 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499595672 151 DGLDGLASGVSAIGLITIAFI-----------AILQANVFIIMICSVLIGSLLGFLCFNFHPAKIFLGDSGALLIGFIIG 219
Cdd:cd06855  150 AGINGLEVGQSLVIALSILLYnllelngssgsMTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFA 229

                        170       180
                 ....*....|....*....|.
gi 499595672 220 FLSLLGFKNITFISLFFPIVI 240
Cdd:cd06855  230 VVGILGHFSKTLLLFFIPQII 250
 
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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