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phospho-N-acetylmuramoyl-pentapeptide-transferase [Levilactobacillus hammesii]

Protein Classification

phospho-N-acetylmuramoyl-pentapeptide-transferase( domain architecture ID 10160594)

phospho-N-acetylmuramoyl-pentapeptide-transferase catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; it transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, to produce undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I

EC:  2.7.8.13
Gene Ontology:  GO:0046872|GO:0008963|GO:0009252
PubMed:  7734839|11024259
SCOP:  3002333

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 38-318 3.77e-115

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: 334.07  E-value: 3.77e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  38 GPTWHEKKSGTPTMGGLLYIVAIVIMTLATSWALAPHhmlstTWILLFILVLYGALGMWDDSIKLFHRQNEGLKAWQKLL 117
Cdd:cd06852     1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPE-----VLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 118 GQIVGALILFWVYTHEQLPMALHVPGFGDWH---MSGWYAIFIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAY 194
Cdd:cd06852    76 LQFLIAIVFALLLYYFNGSGTLITLPFFKNGlidLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 195 -QQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLHHELSLLWIGLIFVIETASVMLQVASF 273
Cdd:cd06852   156 lAGNAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSF 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1784521053 274 KLTGKRIFLMSPIHHHFEMKGWSEWKIDLTFWGIGLVTALTGVWT 318
Cdd:cd06852   236 KLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
 
Name Accession Description Interval E-value
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 38-318 3.77e-115

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: 334.07  E-value: 3.77e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  38 GPTWHEKKSGTPTMGGLLYIVAIVIMTLATSWALAPHhmlstTWILLFILVLYGALGMWDDSIKLFHRQNEGLKAWQKLL 117
Cdd:cd06852     1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPE-----VLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 118 GQIVGALILFWVYTHEQLPMALHVPGFGDWH---MSGWYAIFIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAY 194
Cdd:cd06852    76 LQFLIAIVFALLLYYFNGSGTLITLPFFKNGlidLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 195 -QQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLHHELSLLWIGLIFVIETASVMLQVASF 273
Cdd:cd06852   156 lAGNAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSF 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1784521053 274 KLTGKRIFLMSPIHHHFEMKGWSEWKIDLTFWGIGLVTALTGVWT 318
Cdd:cd06852   236 KLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
 14-319 5.17e-89

phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the enzyme catalyzes the first of the lipid cycle reactions. Also known as Muramoyl-Pentapeptide Transferase (murX). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 161884  Cd Length: 321  Bit Score: 268.93  E-value: 5.17e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  14 TVAFMPSLIRYFRARHEGQMIREEGPTWHEKKSGTPTMGGLLYIVAIVIMTLATSWALAPHhmlstTWILLFILVLYGAL 93
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPY-----VLLVLFVLLGYGFI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  94 GMWDDSIKLFHRQNEGLKAWQKLLGQIVGALILFWVYTHEQLPMALHVPGFGDW--HMSGWYAIFIIIWLVGFSNAVNLT 171
Cdd:TIGR00445  76 GFVDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFIKDFmfDLGLFYILLAYFVLVGTSNAVNLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 172 DGLDGLVSGLASIAFTAYGIVAYQQHQIN---------------IAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALG 236
Cdd:TIGR00445 156 DGLDGLAIGPSAIAFGALAILAWATGNANfakylhipylkdsgeLVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 237 GALAAVSILLHHELSLLWIGLIFVIETASVMLQVASFKLTGKRIFLMSPIHHHFEMKGWSEWKIDLTFWGIGLVTALTGV 316
Cdd:TIGR00445 236 GALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVAL 315


                  ...
gi 1784521053 317 WTI 319
Cdd:TIGR00445 316 ATL 318
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 1-305 2.72e-84

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: 255.82  E-value: 2.72e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053   1 MNVVLPLVGGFIITVAFMPSLIRYFRARHegqmIREEGPTWHEKKSGTPTMGGLLYIVAIVIMTLATSWALAPHhmlstT 80
Cdd:COG0472     1 LRLLLAFLLAFLLSLLLTPLLIRLARRLG----LVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPE-----L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  81 WILLFILVLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALILFWVYTHEQlpmALHVPGFGDWHMSGWYAIFIIIW 160
Cdd:COG0472    72 LLLLLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRIT---SLTIPFFGLLDLGWLYIPLTVFW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 161 LVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALA 240
Cdd:COG0472   141 IVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALA 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1784521053 241 AVSILLHHE----LSLLWIGLIFVIETASVMLQVasfKLTGKRIFL--MSPIHHHFEMKGWSEWKIDLTFW 305
Cdd:COG0472   221 ALAILGRQEgaslLLLLLILGVPVVDTLSVILQR---VLRGKRIFKadRAHLHHHLELLGWSERQVVLRFW 288
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
81-246 4.35e-33

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 119.63  E-value: 4.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  81 WILLFILVLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALILFWVYTHEQLPMALhVPGFGDWHMSGWYAIFI-II 159
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILLVLGGIGLTSLGL-PFGGGSLELGPWLSILLtLF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 160 WLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGAL 239
Cdd:pfam00953  72 AIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLL 151


                  ....*..
gi 1784521053 240 AAVSILL 246
Cdd:pfam00953 152 AVLAIIG 158
 
Name Accession Description Interval E-value
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 38-318 3.77e-115

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: 334.07  E-value: 3.77e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  38 GPTWHEKKSGTPTMGGLLYIVAIVIMTLATSWALAPHhmlstTWILLFILVLYGALGMWDDSIKLFHRQNEGLKAWQKLL 117
Cdd:cd06852     1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPE-----VLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 118 GQIVGALILFWVYTHEQLPMALHVPGFGDWH---MSGWYAIFIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAY 194
Cdd:cd06852    76 LQFLIAIVFALLLYYFNGSGTLITLPFFKNGlidLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 195 -QQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLHHELSLLWIGLIFVIETASVMLQVASF 273
Cdd:cd06852   156 lAGNAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSF 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1784521053 274 KLTGKRIFLMSPIHHHFEMKGWSEWKIDLTFWGIGLVTALTGVWT 318
Cdd:cd06852   236 KLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
 14-319 5.17e-89

phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the enzyme catalyzes the first of the lipid cycle reactions. Also known as Muramoyl-Pentapeptide Transferase (murX). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 161884  Cd Length: 321  Bit Score: 268.93  E-value: 5.17e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  14 TVAFMPSLIRYFRARHEGQMIREEGPTWHEKKSGTPTMGGLLYIVAIVIMTLATSWALAPHhmlstTWILLFILVLYGAL 93
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPY-----VLLVLFVLLGYGFI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  94 GMWDDSIKLFHRQNEGLKAWQKLLGQIVGALILFWVYTHEQLPMALHVPGFGDW--HMSGWYAIFIIIWLVGFSNAVNLT 171
Cdd:TIGR00445  76 GFVDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFIKDFmfDLGLFYILLAYFVLVGTSNAVNLT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 172 DGLDGLVSGLASIAFTAYGIVAYQQHQIN---------------IAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALG 236
Cdd:TIGR00445 156 DGLDGLAIGPSAIAFGALAILAWATGNANfakylhipylkdsgeLVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 237 GALAAVSILLHHELSLLWIGLIFVIETASVMLQVASFKLTGKRIFLMSPIHHHFEMKGWSEWKIDLTFWGIGLVTALTGV 316
Cdd:TIGR00445 236 GALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVAL 315


                  ...
gi 1784521053 317 WTI 319
Cdd:TIGR00445 316 ATL 318
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 1-305 2.72e-84

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: 255.82  E-value: 2.72e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053   1 MNVVLPLVGGFIITVAFMPSLIRYFRARHegqmIREEGPTWHEKKSGTPTMGGLLYIVAIVIMTLATSWALAPHhmlstT 80
Cdd:COG0472     1 LRLLLAFLLAFLLSLLLTPLLIRLARRLG----LVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPE-----L 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  81 WILLFILVLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALILFWVYTHEQlpmALHVPGFGDWHMSGWYAIFIIIW 160
Cdd:COG0472    72 LLLLLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRIT---SLTIPFFGLLDLGWLYIPLTVFW 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 161 LVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALA 240
Cdd:COG0472   141 IVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALA 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1784521053 241 AVSILLHHE----LSLLWIGLIFVIETASVMLQVasfKLTGKRIFL--MSPIHHHFEMKGWSEWKIDLTFW 305
Cdd:COG0472   221 ALAILGRQEgaslLLLLLILGVPVVDTLSVILQR---VLRGKRIFKadRAHLHHHLELLGWSERQVVLRFW 288
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 48-268 3.90e-43

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: 148.79  E-value: 3.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  48 TPTMGGllyiVAIVIMTLATSWALAPHHMLSTTWILLFIL--VLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALI 125
Cdd:cd06853     8 IPRLGG----LAIFLGFLLALLLALLFPFFLLPELLGLLAgaTIIVLLGLLDDLF--------DLSPKVKLLGQILAALI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 126 LFWVYTHEQLpmaLHVPGFGDWHMSGWYAIFI-IIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIF 204
Cdd:cd06853    76 VVFGGGVILS---LLGPFGGGIILLGWLSIPLtVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLVALL 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1784521053 205 CFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLHHE-------LSLLWIGLIFVIETASVML 268
Cdd:cd06853   153 ALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQKsstaispVVPLLILAVPLFDTLFVII 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 47-243 1.58e-36

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: 129.73  E-value: 1.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  47 GTPTMGGLLYIVAIVIMTLatswaLAPHHMLSTTWILLFILVLYGALGMWDDSIKLfhrqNEGLKAWQKLLGQIVGALIL 126
Cdd:cd06499     1 PTPTMGGLAILLGFLLGVL-----LYIPHSNTLILLALLSGLVAGIVGFIDDLLGL----KVELSEREKLLLQILAALFL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 127 FWVYTheqLPMALHVPGFGDWHMSGWYAIFIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFCF 206
Cdd:cd06499    72 LLIGG---GHTTVTTPLGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLFI 148

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1784521053 207 AVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVS 243
Cdd:cd06499   149 ILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
81-246 4.35e-33

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 119.63  E-value: 4.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  81 WILLFILVLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALILFWVYTHEQLPMALhVPGFGDWHMSGWYAIFI-II 159
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILLVLGGIGLTSLGL-PFGGGSLELGPWLSILLtLF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 160 WLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGAL 239
Cdd:pfam00953  72 AIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLL 151


                  ....*..
gi 1784521053 240 AAVSILL 246
Cdd:pfam00953 152 AVLAIIG 158
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
 48-261 3.03e-28

The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments.


Pssm-ID: 133464  Cd Length: 253  Bit Score: 109.64  E-value: 3.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  48 TPTMGGLLYIVAIVIMTLAtsWALAPHHMLSTTWILLFILVLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALILF 127
Cdd:cd06854    15 TPRGGGIAFVLAFLLALLL--AAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLR--------SLSPKIRLLVQLLAAALAL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 128 WVYTHEQLPMALHVPGFgdwhmsgWYAIFIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFCFA 207
Cdd:cd06854    85 YALGPLTSLLLNFLPPW-------LIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAGEPALALLALA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1784521053 208 VVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLHHELSLLWIGLIFVI 261
Cdd:cd06854   158 LAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWAWLLLLS 211
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 49-315 1.43e-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: 108.49  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  49 PTMGGLLYIVAIVIMTLATSwalAPHHMLSTTWILLFILvLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALILFW 128
Cdd:cd06856    14 PEMGGIAVLLGFSLGLLFLS---ALTHSVEALALLITSL-LAGLIGLLDDIL--------GLSQSEKVLLTALPAIPLLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 129 VYTHEQLPMalhVPGFGDWHMSGWYAIFIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFCFAV 208
Cdd:cd06856    82 LKAGNPLTS---LPIGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIALIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 209 VGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLHHELSLLWIGLIFVIEtaSVMLQVASFKLTGKRIF------- 281
Cdd:cd06856   159 VAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVID--FLLKLRSKGGGKEHREKptkvled 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1784521053 282 --------LMSPIHHHFEMKGW--SEWKIDLTFWGIGLVTALTG 315
Cdd:cd06856   237 gtlypppdKSSLLTLRLLLRKGpmTEKEVVLVLWALEALLGILA 280
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 48-243 3.75e-23

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: 94.62  E-value: 3.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  48 TPTMGGllyiVAIVIMTLATSWaLAPHHMLSTTWILLFILVLYGALGMWDDSIKLfhrqnegLKAWQKLLGQIVGALILF 127
Cdd:cd06912    11 TPRIGG----VAIFLGLLAGLL-LLSLLSGSLLLLLLLAALPAFLAGLLEDITKR-------VSPRIRLLATFLSALLAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 128 WvYTHEQLPMALhvPGFGDWHMSGWYA--IFIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFC 205
Cdd:cd06912    79 W-LLGASITRLD--LPGLDLLLSFPPFaiIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDTDLAFLA 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1784521053 206 FAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVS 243
Cdd:cd06912   156 LLLAGALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 49-249 1.89e-16

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: 76.77  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  49 PTMGG---LLYIVAIVIMTLATSWALAPHHMLSTTWILLFILVLYGALGMWDDSIklfhrqneGLKAWQKLLGQIVGALI 125
Cdd:cd06851    14 PEPGGisiLIGFVASEITLIFFPFLSFPHFPISEILAALITSVLGFSVGIIDDRL--------TMGGWFKPVALAFAAAP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 126 LFWVYTHEqLPMALHVPGFGDWHMSGWYAIfIIIWLVGFSNAVNLTDGLDGLVSGLASIAFTAYGIVAYQQHQINIAIFC 205
Cdd:cd06851    86 ILLLGAYD-SNLDFPLFGGSVKIPSLYLVL-VVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQNYEIGIAC 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1784521053 206 FAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLHHE 249
Cdd:cd06851   164 LCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVE 207
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
 52-247 1.18e-07

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: 52.25  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053  52 GGLLYIVAIVIMTLATSWALAPHHMLSTTWILLFILVLYGALGMWDDSIKLFHRQneglkawqKLLGQIVGALILFWVY- 130
Cdd:cd06855    34 PGIVFLIVLFLFIPFPFLKDFPHDKLVEYLSALLSICCMTFLGFADDVLDLRWRH--------KLILPTFASLPLLMVYy 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784521053 131 -----THEQLPmaLHVPGFGDWHMSGWYAIFIIIWLVGFSNAVNLTDGLDGLVSG---LASIAFTAYGIV--------AY 194
Cdd:cd06855   106 gntgiTLPIVP--LRPLLGTLIDLGILYYVYMILLAVFCTNSINIYAGINGLEVGqslVIALSILLYNLLelngssgsMT 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1784521053 195 QQHQINIAIFCFAVVGSLLGFLIFNHKPAKIFMGDTGSLALGGALAAVSILLH 247
Cdd:cd06855   184 LDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILGH 236
 
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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