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Conserved domains on  [gi|42794009|ref|NP_001373|]
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UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase [Homo sapiens]

Protein Classification

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase( domain architecture ID 10160631)

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase which catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate in the dolichol pathway of N-linked protein glycosylation; belongs to glycosyltransferase family 4

EC:  2.7.8.15
Gene Ontology:  GO:0046872|GO:0016780|GO:0006047|GO:0016757
PubMed:  7734839

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
 29-317 1.59e-155

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: 440.14  E-value: 1.59e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  29 IPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLncfvkeqcKAFPHHEFVALIGALLAICCM 108
Cdd:cd06855   1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCM 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 109 IFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRPILGLHLDLGILYYVYMGLLAVFCTNAINILA 188
Cdd:cd06855  73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 189 GINGLEAGQSLVISASIIVFNLVELEGD----CRDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV 264
Cdd:cd06855 151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794009 265 VGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMS 317
Cdd:cd06855 231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
 
Name Accession Description Interval E-value
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
 29-317 1.59e-155

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: 440.14  E-value: 1.59e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  29 IPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLncfvkeqcKAFPHHEFVALIGALLAICCM 108
Cdd:cd06855   1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCM 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 109 IFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRPILGLHLDLGILYYVYMGLLAVFCTNAINILA 188
Cdd:cd06855  73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 189 GINGLEAGQSLVISASIIVFNLVELEGD----CRDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV 264
Cdd:cd06855 151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794009 265 VGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMS 317
Cdd:cd06855 231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
99-269 6.52e-28

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 107.69  E-value: 6.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009    99 IGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIvvpkpfrPILGLHLDLGILYYVYMGLLAV 178
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGL-------PFGGGSLELGPWLSILLTLFAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009   179 FC-TNAINILAGINGLEAGQSLVISASIIVFNLVelegdcrDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYF 257
Cdd:pfam00953  74 VGlTNAVNFIDGLDGLAGGVAIIAALALGIIAYL-------LGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLF 146

                         170
                  ....*....|..
gi 42794009   258 AGMTFAVVGILG 269
Cdd:pfam00953 147 LGFLLAVLAIIG 158
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 15-278 8.81e-24

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: 99.82  E-value: 8.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  15 LIVSLLGFVATVTLIPAFRGHFIAARLCgQDLNKTSRQQ--IPESQGVisgAVFLIILFCFIPFPFLncfvkeqckafPH 92
Cdd:COG0472   4 LLAFLLAFLLSLLLTPLLIRLARRLGLV-DDPNERKSHKrpTPRMGGI---AIFLGFLLALLLLALL-----------SN 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  93 HEFVALIGALLAICcmiFLGFADDVLNLRWRHKLLLPTAASLpLLMVYFTNFGNTTIvvpkpfrPILGLhLDLGILYYVY 172
Cdd:COG0472  69 PELLLLLLGALLLG---LIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTI-------PFFGL-LDLGWLYIPL 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 173 MGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVelegdcrDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGD 252
Cdd:COG0472 137 TVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYL-------AGQGELALLAAALAGALLGFLWFNFPPAKIFMGD 209

                       250       260
                ....*....|....*....|....*.
gi 42794009 253 TFCYFAGMTFAVVGILGHFSKTMLLF 278
Cdd:COG0472 210 TGSLFLGFALAALAILGRQEGASLLL 235
 
Name Accession Description Interval E-value
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
 29-317 1.59e-155

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: 440.14  E-value: 1.59e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  29 IPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLncfvkeqcKAFPHHEFVALIGALLAICCM 108
Cdd:cd06855   1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCM 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 109 IFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRPILGLHLDLGILYYVYMGLLAVFCTNAINILA 188
Cdd:cd06855  73 TFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 189 GINGLEAGQSLVISASIIVFNLVELEGD----CRDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV 264
Cdd:cd06855 151 GINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAV 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42794009 265 VGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMS 317
Cdd:cd06855 231 VGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 43-288 3.31e-72

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: 225.84  E-value: 3.31e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  43 GQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLncfvkeqckAFPHHEFVALIGALLAICCMIFLGFADDVLNLRW 122
Cdd:cd06851   2 GKDMNKKGNVMIPEPGGISILIGFVASEITLIFFPFL---------SFPHFPISEILAALITSVLGFSVGIIDDRLTMGG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 123 RHKLLLPTAASLPLLMVYFTNFGNTTivvpkpfrPILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVIS 202
Cdd:cd06851  73 WFKPVALAFAAAPILLLGAYDSNLDF--------PLFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIIS 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 203 ASIIVFNLVELEGdcrddhvFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQ 282
Cdd:cd06851 145 FALAISLLVQQNY-------EIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIAAVAFIPA 217


                ....*.
gi 42794009 283 VFNFLY 288
Cdd:cd06851 218 IINFFL 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 89-266 2.48e-41

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: 144.37  E-value: 2.48e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  89 AFPHHEFVALIGALLAICCMIFLGFADDVLNL----RWRHKLLLPTAASLPLLMVyftNFGNTTIVVPkpfrpiLGLHLD 164
Cdd:cd06499  20 LYIPHSNTLILLALLSGLVAGIVGFIDDLLGLkvelSEREKLLLQILAALFLLLI---GGGHTTVTTP------LGFVLD 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 165 LGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDcrddhvfSLYFMIPFFFTTLGLLYHNWY 244
Cdd:cd06499  91 LGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTT-------SALLFIILAGACLGFLYFNFY 163

                       170       180
                ....*....|....*....|..
gi 42794009 245 PSRVFVGDTFCYFAGMTFAVVG 266
Cdd:cd06499 164 PAKIFMGDTGSYFLGAAYAAVA 185
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 43-287 3.19e-28

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: 111.96  E-value: 3.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  43 GQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLNcfvkeqckafphhEFVALIGALLAICcmiFLGFADDVLNLRW 122
Cdd:cd06856   2 GRDVHKPGKPEVPEMGGIAVLLGFSLGLLFLSALTHSV-------------EALALLITSLLAG---LIGLLDDILGLSQ 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 123 RHKLLLPTAASLPLLMVyftNFGNTTIVVPkpfrpiLGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVIS 202
Cdd:cd06856  66 SEKVLLTALPAIPLLVL---KAGNPLTSLP------IGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIIL 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 203 ASIIVFNLVelegdcrDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQ 282
Cdd:cd06856 137 LALAIILLI-------NGDYDALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPY 209


                ....*
gi 42794009 283 VFNFL 287
Cdd:cd06856 210 VIDFL 214
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
99-269 6.52e-28

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 107.69  E-value: 6.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009    99 IGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIvvpkpfrPILGLHLDLGILYYVYMGLLAV 178
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGL-------PFGGGSLELGPWLSILLTLFAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009   179 FC-TNAINILAGINGLEAGQSLVISASIIVFNLVelegdcrDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYF 257
Cdd:pfam00953  74 VGlTNAVNFIDGLDGLAGGVAIIAALALGIIAYL-------LGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLF 146

                         170
                  ....*....|..
gi 42794009   258 AGMTFAVVGILG 269
Cdd:pfam00953 147 LGFLLAVLAIIG 158
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 15-278 8.81e-24

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: 99.82  E-value: 8.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  15 LIVSLLGFVATVTLIPAFRGHFIAARLCgQDLNKTSRQQ--IPESQGVisgAVFLIILFCFIPFPFLncfvkeqckafPH 92
Cdd:COG0472   4 LLAFLLAFLLSLLLTPLLIRLARRLGLV-DDPNERKSHKrpTPRMGGI---AIFLGFLLALLLLALL-----------SN 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  93 HEFVALIGALLAICcmiFLGFADDVLNLRWRHKLLLPTAASLpLLMVYFTNFGNTTIvvpkpfrPILGLhLDLGILYYVY 172
Cdd:COG0472  69 PELLLLLLGALLLG---LIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTI-------PFFGL-LDLGWLYIPL 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 173 MGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVelegdcrDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGD 252
Cdd:COG0472 137 TVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYL-------AGQGELALLAAALAGALLGFLWFNFPPAKIFMGD 209

                       250       260
                ....*....|....*....|....*.
gi 42794009 253 TFCYFAGMTFAVVGILGHFSKTMLLF 278
Cdd:COG0472 210 TGSLFLGFALAALAILGRQEGASLLL 235
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 64-272 7.05e-21

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: 91.01  E-value: 7.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  64 AVFLIILFCFIPFPFlncfvkeqckaFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLplLMVYFtn 143
Cdd:cd06853  15 AIFLGFLLALLLALL-----------FPFFLLPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAAL--IVVFG-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 144 fGNTTIVVPKPFrpiLGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVElegdcrdDHVF 223
Cdd:cd06853  80 -GGVILSLLGPF---GGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLN-------GQVL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42794009 224 SLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFS 272
Cdd:cd06853 149 VALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQK 197
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 98-253 4.16e-14

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: 72.14  E-value: 4.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  98 LIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTAASLpLLMVYFTNFGNTTIVVPKPFrpILGLHLDLGILY 169
Cdd:cd06852  38 VLLLLLLTLGFGLIGFLDDYLKvvkkrnlgLSARQKLLLQFLIAI-VFALLLYYFNGSGTLITLPF--FKNGLIDLGILY 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 170 YVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELegdcrdDHVFSLYFMIPFFFTTLGLLYHNWYPSRVF 249
Cdd:cd06852 115 IPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG------NAVFLAVFCAALVGACLGFLWFNAYPAKVF 188


                ....
gi 42794009 250 VGDT 253
Cdd:cd06852 189 MGDT 192
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 87-266 8.57e-05

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: 43.00  E-value: 8.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009  87 CKAFPHHEFVALIGALLAICCMIFLGFADDV-LNLRWRHKLLLptAASLPLLMVYFTNFGNTTIVVPkPFRPILGLHLdL 165
Cdd:cd06912  27 LLLLSLLSGSLLLLLLLAALPAFLAGLLEDItKRVSPRIRLLA--TFLSALLAVWLLGASITRLDLP-GLDLLLSFPP-F 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794009 166 GILYYVymgLLAVFCTNAINILAGINGLEAGQSLVISASIIvfnLVELEGDCRDDHVFSLYFMipffFTTLGLLYHNWYP 245
Cdd:cd06912 103 AIIFTI---FAVAGVANAFNIIDGFNGLASGVAIISLLSLA---LVAFQVGDTDLAFLALLLA----GALLGFLIFNFPF 172

                       170       180
                ....*....|....*....|.
gi 42794009 246 SRVFVGDTFCYFAGMTFAVVG 266
Cdd:cd06912 173 GKIFLGDGGAYLLGFLLAWLA 193
 
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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