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Conserved domains on  [gi|699607411|ref|XP_009872304|]
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PREDICTED: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase, partial [Apaloderma vittatum]

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 ...
 1-263 1.58e-146

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: 415.11  E-value: 1.58e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411   1 PEAQGVISGAVFLIILFCFIPVPFLRcfveeqcaAFPHDEFVELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASL 80
Cdd:cd06855   27 PESAGLVPGIVFLIVLFLFIPFPFLK--------DFPHDKLVEYLSALLSICCMTFLGFADDVLDLRWRHKLILPTFASL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  81 PLLMVYFTNFGNTTIVVPkpFRALLGMHLDLGILYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVLELT 160
Cdd:cd06855   99 PLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYAGINGLEVGQSLVIALSILLYNLLELN 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 161 GDYG----DDHIFSLYFMIPFFSTTLGLLFHNWYPSRAFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFIPQVLNFLYSL 236
Cdd:cd06855  177 GSSGsmtlDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILGHFSKTLLLFFIPQIINFLYSL 256

                        250       260
                 ....*....|....*....|....*..
gi 699607411 237 PQLFHVIPCPRHRLPRLNPSTGKLEMS 263
Cdd:cd06855  257 PQLFGIVPCPRHRLPKFNPKTGLLEPS 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 ...
 1-263 1.58e-146

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: 415.11  E-value: 1.58e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411   1 PEAQGVISGAVFLIILFCFIPVPFLRcfveeqcaAFPHDEFVELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASL 80
Cdd:cd06855   27 PESAGLVPGIVFLIVLFLFIPFPFLK--------DFPHDKLVEYLSALLSICCMTFLGFADDVLDLRWRHKLILPTFASL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  81 PLLMVYFTNFGNTTIVVPkpFRALLGMHLDLGILYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVLELT 160
Cdd:cd06855   99 PLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYAGINGLEVGQSLVIALSILLYNLLELN 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 161 GDYG----DDHIFSLYFMIPFFSTTLGLLFHNWYPSRAFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFIPQVLNFLYSL 236
Cdd:cd06855  177 GSSGsmtlDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILGHFSKTLLLFFIPQIINFLYSL 256

                        250       260
                 ....*....|....*....|....*..
gi 699607411 237 PQLFHVIPCPRHRLPRLNPSTGKLEMS 263
Cdd:cd06855  257 PQLFGIVPCPRHRLPKFNPKTGLLEPS 283
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
45-215 2.20e-26

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 102.68  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411   45 IGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLPLLMVYFTNFGNTTIVvpkpfraLLGMHLDLGILYYVYMGMLAV 124
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLP-------FGGGSLELGPWLSILLTLFAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  125 FC-TNAINILAGINGIEAGQSLVIAASIIIFNVLeltgdygDDHIFSLYFMIPFFSTTLGLLFHNWYPSRAFVGDTFCYF 203
Cdd:pfam00953  74 VGlTNAVNFIDGLDGLAGGVAIIAALALGIIAYL-------LGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLF 146

                         170
                  ....*....|..
gi 699607411  204 AGMTFAVVGILG 215
Cdd:pfam00953 147 LGFLLAVLAIIG 158
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 33-226 2.12e-21

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: 92.50  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  33 CAAFPHDEFVELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLpLLMVYFTNFGNTTIVVPKPfrallgmhLDLG 112
Cdd:COG0472   60 LLLLALLSNPELLLLLLGALLLGLIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTIPFFGL--------LDLG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 113 ILYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNvleltgdYGDDHIFSLYFMIPFFSTTLGLLFHNWYPS 192
Cdd:COG0472  131 WLYIPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIA-------YLAGQGELALLAAALAGALLGFLWFNFPPA 203

                        170       180       190
                 ....*....|....*....|....*....|....
gi 699607411 193 RAFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFI 226
Cdd:COG0472  204 KIFMGDTGSLFLGFALAALAILGRQEGASLLLLL 237
 
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 ...
 1-263 1.58e-146

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: 415.11  E-value: 1.58e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411   1 PEAQGVISGAVFLIILFCFIPVPFLRcfveeqcaAFPHDEFVELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASL 80
Cdd:cd06855   27 PESAGLVPGIVFLIVLFLFIPFPFLK--------DFPHDKLVEYLSALLSICCMTFLGFADDVLDLRWRHKLILPTFASL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  81 PLLMVYFTNFGNTTIVVPkpFRALLGMHLDLGILYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVLELT 160
Cdd:cd06855   99 PLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYAGINGLEVGQSLVIALSILLYNLLELN 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 161 GDYG----DDHIFSLYFMIPFFSTTLGLLFHNWYPSRAFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFIPQVLNFLYSL 236
Cdd:cd06855  177 GSSGsmtlDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILGHFSKTLLLFFIPQIINFLYSL 256

                        250       260
                 ....*....|....*....|....*..
gi 699607411 237 PQLFHVIPCPRHRLPRLNPSTGKLEMS 263
Cdd:cd06855  257 PQLFGIVPCPRHRLPKFNPKTGLLEPS 283
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 1-234 8.85e-66

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: 207.35  E-value: 8.85e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411   1 PEAQGVISGAVFLIILFCFIPVPFLrcfveeqcaAFPHDEFVELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASL 80
Cdd:cd06851   14 PEPGGISILIGFVASEITLIFFPFL---------SFPHFPISEILAALITSVLGFSVGIIDDRLTMGGWFKPVALAFAAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  81 PLLMVYFTNFGNTTIvvpkpfraLLGMHLDLGILYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVLELT 160
Cdd:cd06851   85 PILLLGAYDSNLDFP--------LFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQN 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 699607411 161 GdygddhiFSLYFMIPFFSTTLGLLFHNWYPSRAFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFIPQVLNFLY 234
Cdd:cd06851  157 Y-------EIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIAAVAFIPAIINFFL 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 35-212 6.10e-39

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: 136.66  E-value: 6.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  35 AFPHDEFVELIGALLAICCMIFLGFADDVLNL----RWRHKLLLPTMASLPLLMVyftNFGNTTIVVPkpfralLGMHLD 110
Cdd:cd06499   20 LYIPHSNTLILLALLSGLVAGIVGFIDDLLGLkvelSEREKLLLQILAALFLLLI---GGGHTTVTTP------LGFVLD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 111 LGILYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVLEltgdyGDDHifSLYFMIPFFSTTLGLLFHNWY 190
Cdd:cd06499   91 LGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLS-----GQTT--SALLFIILAGACLGFLYFNFY 163

                        170       180
                 ....*....|....*....|..
gi 699607411 191 PSRAFVGDTFCYFAGMTFAVVG 212
Cdd:cd06499  164 PAKIFMGDTGSYFLGAAYAAVA 185
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
45-215 2.20e-26

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 102.68  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411   45 IGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLPLLMVYFTNFGNTTIVvpkpfraLLGMHLDLGILYYVYMGMLAV 124
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLP-------FGGGSLELGPWLSILLTLFAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  125 FC-TNAINILAGINGIEAGQSLVIAASIIIFNVLeltgdygDDHIFSLYFMIPFFSTTLGLLFHNWYPSRAFVGDTFCYF 203
Cdd:pfam00953  74 VGlTNAVNFIDGLDGLAGGVAIIAALALGIIAYL-------LGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLF 146

                         170
                  ....*....|..
gi 699607411  204 AGMTFAVVGILG 215
Cdd:pfam00953 147 LGFLLAVLAIIG 158
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 42-233 3.32e-26

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: 105.41  E-value: 3.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  42 VELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLPLLMVyftNFGNTTIVVPKPFRallgmhlDLGILYYVYMGM 121
Cdd:cd06856   39 VEALALLITSLLAGLIGLLDDILGLSQSEKVLLTALPAIPLLVL---KAGNPLTSLPIGGR-------VLGILYYLLIVP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 122 LAV-FCTNAINILAGINGIEAGQSLVIAASIIIfnVLELTGDYgddhiFSLYFMIPFFSTTLGLLFHNWYPSRAFVGDTF 200
Cdd:cd06856  109 LGItGASNAFNMLAGFNGLEAGMGIIILLALAI--ILLINGDY-----DALIIALILVAALLAFLLYNKYPAKVFPGDVG 181

                        170       180       190
                 ....*....|....*....|....*....|...
gi 699607411 201 CYFAGMTFAVVGILGHFSKTMLLFFIPQVLNFL 233
Cdd:cd06856  182 TLPIGALIGTIAVLGGLEIILLILLLPYVIDFL 214
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 33-226 2.12e-21

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: 92.50  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  33 CAAFPHDEFVELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLpLLMVYFTNFGNTTIVVPKPfrallgmhLDLG 112
Cdd:COG0472   60 LLLLALLSNPELLLLLLGALLLGLIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTIPFFGL--------LDLG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 113 ILYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNvleltgdYGDDHIFSLYFMIPFFSTTLGLLFHNWYPS 192
Cdd:COG0472  131 WLYIPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIA-------YLAGQGELALLAAALAGALLGFLWFNFPPA 203

                        170       180       190
                 ....*....|....*....|....*....|....
gi 699607411 193 RAFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFI 226
Cdd:COG0472  204 KIFMGDTGSLFLGFALAALAILGRQEGASLLLLL 237
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 36-227 1.00e-18

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: 84.08  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  36 FPHDEFVELIGALLAICCMIFLGFADDVLNLRWRHKLLLPTMASLplLMVYFtnfGNTTIVVPKPFralLGMHLDLGILY 115
Cdd:cd06853   30 FPFFLLPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAAL--IVVFG---GGVILSLLGPF---GGGIILLGWLS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 116 YVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVLEltgdygdDHIFSLYFMIPFFSTTLGLLFHNWYPSRAF 195
Cdd:cd06853  102 IPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLN-------GQVLVALLALALAGALLGFLPYNFHPARIF 174

                        170       180       190
                 ....*....|....*....|....*....|...
gi 699607411 196 VGDTFCYFAGMTFAVVGILGHF-SKTMLLFFIP 227
Cdd:cd06853  175 MGDAGSLFLGFLLAVLSILGTQkSSTAISPVVP 207
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 42-226 7.76e-13

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: 67.90  E-value: 7.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  42 VELIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTMASLpLLMVYFTNFGNTTIVVPKPFraLLGMHLDLGI 113
Cdd:cd06852   36 PEVLLLLLLTLGFGLIGFLDDYLKvvkkrnlgLSARQKLLLQFLIAI-VFALLLYYFNGSGTLITLPF--FKNGLIDLGI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 114 LYYVYMGMLAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVleLTGDYGDDHIFSLYFMipffSTTLGLLFHNWYPSR 193
Cdd:cd06852  113 LYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAY--LAGNAVFLAVFCAALV----GACLGFLWFNAYPAK 186

                        170       180       190
                 ....*....|....*....|....*....|...
gi 699607411 194 AFVGDTFCYFAGMTFAVVGILghfSKTMLLFFI 226
Cdd:cd06852  187 VFMGDTGSLALGGALAALAIL---TKQELLLLI 216
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 33-212 1.51e-04

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: 42.23  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411  33 CAAFPHDEFVELIGALLAICCMIFLGFADDV-LNLRWRHKLLLPTMASLplLMVYFTNFGNTTIVVPkPFRALLGMHLdL 111
Cdd:cd06912   27 LLLLSLLSGSLLLLLLLAALPAFLAGLLEDItKRVSPRIRLLATFLSAL--LAVWLLGASITRLDLP-GLDLLLSFPP-F 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 699607411 112 GILYYVYMgmlAVFCTNAINILAGINGIEAGQSLVIAASIIIFNVLeltgdYGDDHIFSLYFMipFFSTTLGLLFHNWYP 191
Cdd:cd06912  103 AIIFTIFA---VAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQ-----VGDTDLAFLALL--LAGALLGFLIFNFPF 172

                        170       180
                 ....*....|....*....|.
gi 699607411 192 SRAFVGDTFCYFAGMTFAVVG 212
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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