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Conserved domains on  [gi|568958817|ref|XP_006510058|]
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UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase isoform X3 [Mus musculus]

Protein Classification

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

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase 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:0016757|GO:0006047|GO:0016780|GO:0006487
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 ...
 1-210 1.22e-125

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: 360.02  E-value: 1.22e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINIL 80
Cdd:cd06855   72 MTFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIY 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  81 AGINGLEAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFA 156
Cdd:cd06855  150 AGINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFA 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568958817 157 VVGILGHFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 210
Cdd:cd06855  230 VVGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 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 ...
 1-210 1.22e-125

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: 360.02  E-value: 1.22e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINIL 80
Cdd:cd06855   72 MTFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIY 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  81 AGINGLEAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFA 156
Cdd:cd06855  150 AGINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFA 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568958817 157 VVGILGHFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 210
Cdd:cd06855  230 VVGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
1-162 6.85e-28

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 105.38  E-value: 6.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817    1 MIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpfrwilGLHLDLGILYYVYMGLLAVFC-TNAINI 79
Cdd:pfam00953  10 IGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFG-------GGSLELGPWLSILLTLFAIVGlTNAVNF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   80 LAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVG 159
Cdd:pfam00953  83 IDGLDGLAGGVAIIAALALGIIA-------YLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLA 155


                  ...
gi 568958817  160 ILG 162
Cdd:pfam00953 156 IIG 158
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 1-171 8.69e-23

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: 95.19  E-value: 8.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNLRWRHKLLLPTAASLpLLMVYFTNFGNTTIvvpkPFRWILglhlDLGILYYVYMGLLAVFCTNAINIL 80
Cdd:COG0472   81 LGLIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTI----PFFGLL----DLGWLYIPLTVFWIVGVSNAVNLT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  81 AGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGI 160
Cdd:COG0472  152 DGLDGLAAGVSLIAALALAIIA-------YLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAI 224

                        170
                 ....*....|.
gi 568958817 161 LGHFSKTMLLF 171
Cdd:COG0472  225 LGRQEGASLLL 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 ...
 1-210 1.22e-125

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: 360.02  E-value: 1.22e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINIL 80
Cdd:cd06855   72 MTFLGFADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIY 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  81 AGINGLEAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFA 156
Cdd:cd06855  150 AGINGLEVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFA 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568958817 157 VVGILGHFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 210
Cdd:cd06855  230 VVGILGHFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 1-181 9.27e-58

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: 185.01  E-value: 9.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIvvpkpfrwILGLHLDLGILYYVYMGLLAVFCTNAINIL 80
Cdd:cd06851   58 GFSVGIIDDRLTMGGWFKPVALAFAAAPILLLGAYDSNLDFP--------LFGGSVKIPSLYLVLVVFMIVITGNAFNSI 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  81 AGINGLEAGQSLVISASIIVFNLVELEGdyrddhiFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGI 160
Cdd:cd06851  130 AGLNGVEAGFTTIISFALAISLLVQQNY-------EIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAI 202

                        170       180
                 ....*....|....*....|.
gi 568958817 161 LGHFSKTMLLFFMPQVFNFLY 181
Cdd:cd06851  203 LGEVEKIAAVAFIPAIINFFL 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 1-159 1.84e-37

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: 131.27  E-value: 1.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNL----RWRHKLLLPTAASLPLLMVyftNFGNTTIVVPkpfrwiLGLHLDLGILYYVYMGLLAVFCTNA 76
Cdd:cd06499   39 AGIVGFIDDLLGLkvelSEREKLLLQILAALFLLLI---GGGHTTVTTP------LGFVLDLGIFYIPFAIIAIVGATNA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  77 INILAGINGLEAGQSLVISASIIVFNLVELEGDyrddhifSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFA 156
Cdd:cd06499  110 VNLIDGMDGLAAGISVIASIACALFALLSGQTT-------SALLFIILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYA 182


                 ...
gi 568958817 157 VVG 159
Cdd:cd06499  183 AVA 185
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
1-162 6.85e-28

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 105.38  E-value: 6.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817    1 MIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpfrwilGLHLDLGILYYVYMGLLAVFC-TNAINI 79
Cdd:pfam00953  10 IGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFG-------GGSLELGPWLSILLTLFAIVGlTNAVNF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   80 LAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVG 159
Cdd:pfam00953  83 IDGLDGLAGGVAIIAALALGIIA-------YLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLA 155


                  ...
gi 568958817  160 ILG 162
Cdd:pfam00953 156 IIG 158
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 3-230 8.82e-27

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: 105.79  E-value: 8.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   3 FLGFADDVLNLRWRHKLLLPTAASLPLLMVyftNFGNTTIVVPkpfrwiLGLHLDLGILYYVYMGLLAVFCTNAINILAG 82
Cdd:cd06856   53 LIGLLDDILGLSQSEKVLLTALPAIPLLVL---KAGNPLTSLP------IGGRVLGILYYLLIVPLGITGASNAFNMLAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  83 INGLEAGQSLVISASIIVFNLveLEGDYrddhiFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILG 162
Cdd:cd06856  124 FNGLEAGMGIIILLALAIILL--INGDY-----DALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLG 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958817 163 HFSKTMLLFFMPQVFNFLYSLPQLFHIIPcPRHRMPRLnAKTGKLEMSYskfktkNLSFLGTFILKVA 230
Cdd:cd06856  197 GLEIILLILLLPYVIDFLLKLRSKGGGKE-HREKPTKV-LEDGTLYPPP------DKSSLLTLRLLLR 256
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 1-171 8.69e-23

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: 95.19  E-value: 8.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNLRWRHKLLLPTAASLpLLMVYFTNFGNTTIvvpkPFRWILglhlDLGILYYVYMGLLAVFCTNAINIL 80
Cdd:COG0472   81 LGLIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTI----PFFGLL----DLGWLYIPLTVFWIVGVSNAVNLT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  81 AGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGI 160
Cdd:COG0472  152 DGLDGLAAGVSLIAALALAIIA-------YLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAI 224

                        170
                 ....*....|.
gi 568958817 161 LGHFSKTMLLF 171
Cdd:COG0472  225 LGRQEGASLLL 235
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 1-165 2.45e-20

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: 87.93  E-value: 2.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   1 MIFLGFADDVLNLRWRHKLLLPTAASLplLMVYFtnfGNTTIVVPKPFrwiLGLHLDLGILYYVYMGLLAVFCTNAINIL 80
Cdd:cd06853   48 IVLLGLLDDLFDLSPKVKLLGQILAAL--IVVFG---GGVILSLLGPF---GGGIILLGWLSIPLTVLWIVGIINAINLI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817  81 AGINGLEAGQSLVISASIIVFNLVElegdyrdDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGI 160
Cdd:cd06853  120 DGLDGLAGGVALIASLALAILALLN-------GQVLVALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSI 192


                 ....*
gi 568958817 161 LGHFS 165
Cdd:cd06853  193 LGTQK 197
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 3-146 7.76e-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: 70.21  E-value: 7.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   3 FLGFADDVLN--------LRWRHKLLLPTAASLpLLMVYFTNFGNTTIVVPKPFrwILGLHLDLGILYYVYMGLLAVFCT 74
Cdd:cd06852   50 LIGFLDDYLKvvkkrnlgLSARQKLLLQFLIAI-VFALLLYYFNGSGTLITLPF--FKNGLIDLGILYIPFAIFVIVGSS 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568958817  75 NAINILAGINGLEAGQSLVISASIIVFNLVELegdyrdDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDT 146
Cdd:cd06852  127 NAVNLTDGLDGLAAGVSIIVALALAIIAYLAG------NAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDT 192
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 3-159 6.02e-06

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: 46.08  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958817   3 FLGFADDV-LNLRWRHKLLLptAASLPLLMVYFTNFgNTTIVVPKPFRWILGLHLdLGILYYVymgLLAVFCTNAINILA 81
Cdd:cd06912   50 LAGLLEDItKRVSPRIRLLA--TFLSALLAVWLLGA-SITRLDLPGLDLLLSFPP-FAIIFTI---FAVAGVANAFNIID 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568958817  82 GINGLEAGQSLVISASIIvfnLVELEGDYRDDHIFSLYFMipffFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVG 159
Cdd:cd06912  123 GFNGLASGVAIISLLSLA---LVAFQVGDTDLAFLALLLA----GALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 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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