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Conserved domains on  [gi|568958809|ref|XP_006510054|]
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UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase isoform X1 [Mus musculus]

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 ...
 3-286 7.80e-156

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: 439.37  E-value: 7.80e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809   3 RHFIAARLCGQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqcKAFPHHEFVALIGALLAICCMIFLGF 82
Cdd:cd06855    6 PLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCMTFLGF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  83 ADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGL 162
Cdd:cd06855   78 ADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYAGINGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 163 EAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILG 238
Cdd:cd06855  156 EVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568958809 239 HFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 286
Cdd:cd06855  236 HFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 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 ...
 3-286 7.80e-156

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: 439.37  E-value: 7.80e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809   3 RHFIAARLCGQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqcKAFPHHEFVALIGALLAICCMIFLGF 82
Cdd:cd06855    6 PLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCMTFLGF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  83 ADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGL 162
Cdd:cd06855   78 ADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYAGINGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 163 EAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILG 238
Cdd:cd06855  156 EVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568958809 239 HFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 286
Cdd:cd06855  236 HFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
68-238 1.46e-29

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 111.54  E-value: 1.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809   68 IGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpfrwilGLHLDLGILYYVYMGLLAV 147
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFG-------GGSLELGPWLSILLTLFAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  148 FC-TNAINILAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYF 226
Cdd:pfam00953  74 VGlTNAVNFIDGLDGLAGGVAIIAALALGIIA-------YLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLF 146

                         170
                  ....*....|..
gi 568958809  227 AGMTFAVVGILG 238
Cdd:pfam00953 147 LGFLLAVLAIIG 158
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 59-247 4.45e-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: 100.20  E-value: 4.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  59 FPHHEFVALIGALLAICcmiFLGFADDVLNLRWRHKLLLPTAASLpLLMVYFTNFGNTTIvvpkPFRWILglhlDLGILY 138
Cdd:COG0472   66 LSNPELLLLLLGALLLG---LIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTI----PFFGLL----DLGWLY 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 139 YVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVF 218
Cdd:COG0472  134 IPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIA-------YLAGQGELALLAAALAGALLGFLWFNFPPAKIF 206

                        170       180
                 ....*....|....*....|....*....
gi 568958809 219 VGDTFCYFAGMTFAVVGILGHFSKTMLLF 247
Cdd:COG0472  207 MGDTGSLFLGFALAALAILGRQEGASLLL 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 ...
 3-286 7.80e-156

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: 439.37  E-value: 7.80e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809   3 RHFIAARLCGQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqcKAFPHHEFVALIGALLAICCMIFLGF 82
Cdd:cd06855    6 PLFIKAGLYGIDLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFL--------KDFPHDKLVEYLSALLSICCMTFLGF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  83 ADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpFRWILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGL 162
Cdd:cd06855   78 ADDVLDLRWRHKLILPTFASLPLLMVYYGNTGITLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYAGINGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 163 EAGQSLVISASIIVFNLVELEGD----YRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILG 238
Cdd:cd06855  156 EVGQSLVIALSILLYNLLELNGSsgsmTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILG 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 568958809 239 HFSKTMLLFFMPQVFNFLYSLPQLFHIIPCPRHRMPRLNAKTGKLEMS 286
Cdd:cd06855  236 HFSKTLLLFFIPQIINFLYSLPQLFGIVPCPRHRLPKFNPKTGLLEPS 283
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 12-257 8.03e-73

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: 226.23  E-value: 8.03e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  12 GQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLncfveeqckAFPHHEFVALIGALLAICCMIFLGFADDVLNLRW 91
Cdd:cd06851    2 GKDMNKKGNVMIPEPGGISILIGFVASEITLIFFPFL---------SFPHFPISEILAALITSVLGFSVGIIDDRLTMGG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  92 RHKLLLPTAASLPLLMVYFTNFGNTTIvvpkpfrwILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVIS 171
Cdd:cd06851   73 WFKPVALAFAAAPILLLGAYDSNLDFP--------LFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIIS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 172 ASIIVFNLVELEGdyrddhiFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQ 251
Cdd:cd06851  145 FALAISLLVQQNY-------EIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIAAVAFIPA 217


                 ....*.
gi 568958809 252 VFNFLY 257
Cdd:cd06851  218 IINFFL 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 23-235 6.40e-43

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: 147.83  E-value: 6.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  23 IPESQGVISGAVFLIILFCFIPfpflncfveeqckafphHEFVALIGALLAICCMIFLGFADDVLNL----RWRHKLLLP 98
Cdd:cd06499    2 TPTMGGLAILLGFLLGVLLYIP-----------------HSNTLILLALLSGLVAGIVGFIDDLLGLkvelSEREKLLLQ 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  99 TAASLPLLMVyftNFGNTTIVVPkpfrwiLGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFN 178
Cdd:cd06499   65 ILAALFLLLI---GGGHTTVTTP------LGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFA 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568958809 179 LVELEGDyrddhifSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVG 235
Cdd:cd06499  136 LLSGQTT-------SALLFIILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 12-306 3.54e-30

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: 116.96  E-value: 3.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  12 GQDLNKLSQQQIPESQGVISGAVFLIILFCFIPFPFLNcfveeqckafphhEFVALIGALLAICcmiFLGFADDVLNLRW 91
Cdd:cd06856    2 GRDVHKPGKPEVPEMGGIAVLLGFSLGLLFLSALTHSV-------------EALALLITSLLAG---LIGLLDDILGLSQ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  92 RHKLLLPTAASLPLLMVyftNFGNTTIVVPkpfrwiLGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVIS 171
Cdd:cd06856   66 SEKVLLTALPAIPLLVL---KAGNPLTSLP------IGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIIL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 172 ASIIVFNLveLEGDYrddhiFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQ 251
Cdd:cd06856  137 LALAIILL--INGDY-----DALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPY 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568958809 252 VFNFLYSLPQLFHIIPcPRHRMPRLnAKTGKLEMSYskfktkNLSFLGTFILKVA 306
Cdd:cd06856  210 VIDFLLKLRSKGGGKE-HREKPTKV-LEDGTLYPPP------DKSSLLTLRLLLR 256
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
68-238 1.46e-29

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 111.54  E-value: 1.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809   68 IGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPkpfrwilGLHLDLGILYYVYMGLLAV 147
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFG-------GGSLELGPWLSILLTLFAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  148 FC-TNAINILAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYF 226
Cdd:pfam00953  74 VGlTNAVNFIDGLDGLAGGVAIIAALALGIIA-------YLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLF 146

                         170
                  ....*....|..
gi 568958809  227 AGMTFAVVGILG 238
Cdd:pfam00953 147 LGFLLAVLAIIG 158
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 59-247 4.45e-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: 100.20  E-value: 4.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  59 FPHHEFVALIGALLAICcmiFLGFADDVLNLRWRHKLLLPTAASLpLLMVYFTNFGNTTIvvpkPFRWILglhlDLGILY 138
Cdd:COG0472   66 LSNPELLLLLLGALLLG---LIGFLDDLLGLSARQKLLGQLLAAL-LLVLLLLRITSLTI----PFFGLL----DLGWLY 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 139 YVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNlvelegdYRDDHIFSLYFMIPFFFTTLGLLYHNWYPSRVF 218
Cdd:COG0472  134 IPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIA-------YLAGQGELALLAAALAGALLGFLWFNFPPAKIF 206

                        170       180
                 ....*....|....*....|....*....
gi 568958809 219 VGDTFCYFAGMTFAVVGILGHFSKTMLLF 247
Cdd:COG0472  207 MGDTGSLFLGFALAALAILGRQEGASLLL 235
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 33-241 6.39e-22

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: 93.32  E-value: 6.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  33 AVFLIILFCFIPFPFLNCFVEEQckafphhefvaLIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLplLMVYFtn 112
Cdd:cd06853   15 AIFLGFLLALLLALLFPFFLLPE-----------LLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAAL--IVVFG-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 113 fGNTTIVVPKPFrwiLGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVElegdyrdDHIF 192
Cdd:cd06853   80 -GGVILSLLGPF---GGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLN-------GQVL 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568958809 193 SLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFS 241
Cdd:cd06853  149 VALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQK 197
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 67-222 1.10e-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: 73.68  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  67 LIGALLAICCMIFLGFADDVLN--------LRWRHKLLLPTAASLpLLMVYFTNFGNTTIVVPKPFrwILGLHLDLGILY 138
Cdd:cd06852   38 VLLLLLLTLGFGLIGFLDDYLKvvkkrnlgLSARQKLLLQFLIAI-VFALLLYYFNGSGTLITLPF--FKNGLIDLGILY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 139 YVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELegdyrdDHIFSLYFMIPFFFTTLGLLYHNWYPSRVF 218
Cdd:cd06852  115 IPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG------NAVFLAVFCAALVGACLGFLWFNAYPAKVF 188


                 ....
gi 568958809 219 VGDT 222
Cdd:cd06852  189 MGDT 192
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 56-235 3.25e-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: 47.24  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809  56 CKAFPHHEFVALIGALLAICCMIFLGFADDV-LNLRWRHKLLLptAASLPLLMVYFTNFgNTTIVVPKPFRWILGLHLdL 134
Cdd:cd06912   27 LLLLSLLSGSLLLLLLLAALPAFLAGLLEDItKRVSPRIRLLA--TFLSALLAVWLLGA-SITRLDLPGLDLLLSFPP-F 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568958809 135 GILYYVymgLLAVFCTNAINILAGINGLEAGQSLVISASIIvfnLVELEGDYRDDHIFSLYFMipffFTTLGLLYHNWYP 214
Cdd:cd06912  103 AIIFTI---FAVAGVANAFNIIDGFNGLASGVAIISLLSLA---LVAFQVGDTDLAFLALLLA----GALLGFLIFNFPF 172

                        170       180
                 ....*....|....*....|.
gi 568958809 215 SRVFVGDTFCYFAGMTFAVVG 235
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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