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Conserved domains on  [gi|2312126732|ref|WP_262316763|]
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phospho-N-acetylmuramoyl-pentapeptide-transferase [Lacticaseibacillus parakribbianus]

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 ...
 41-319 2.23e-104

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: 306.72  E-value: 2.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  41 GPKWHAKKNGTPTMGGLILVIAIVASALFAGWWQgqlTLSLLIGLFILVLYGALGFFDDFIKVAMKRNLGLKAWQKLLGQ 120
Cdd:cd06852     1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLD---SPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 121 IVGAAVFLLAYFHEGFPHTLA---LPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIA-VQ 196
Cdd:cd06852    78 FLIAIVFALLLYYFNGSGTLItlpFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAyLA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 197 EARTDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALLLNRPWSLLLIGIVFVCETASVMIQVFVHHF 276
Cdd:cd06852   158 GNAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSFKL 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2312126732 277 FHRRVFKMTPIHHSFEMSGWSEWRIDIVFWLTGAVAGGLYLLL 319
Cdd:cd06852   238 TGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
 
Name Accession Description Interval E-value
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 41-319 2.23e-104

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: 306.72  E-value: 2.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  41 GPKWHAKKNGTPTMGGLILVIAIVASALFAGWWQgqlTLSLLIGLFILVLYGALGFFDDFIKVAMKRNLGLKAWQKLLGQ 120
Cdd:cd06852     1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLD---SPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 121 IVGAAVFLLAYFHEGFPHTLA---LPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIA-VQ 196
Cdd:cd06852    78 FLIAIVFALLLYYFNGSGTLItlpFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAyLA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 197 EARTDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALLLNRPWSLLLIGIVFVCETASVMIQVFVHHF 276
Cdd:cd06852   158 GNAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSFKL 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2312126732 277 FHRRVFKMTPIHHSFEMSGWSEWRIDIVFWLTGAVAGGLYLLL 319
Cdd:cd06852   238 TGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
 17-309 1.20e-81

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: 250.05  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  17 TVILLPLFIGYQRMRKEGQTIREIGPKWHAKKNGTPTMGGLILVIAIVASALFagwWQGQLTLSLLIGLFILVLYGALGF 96
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVL---WAQLGNPYVLLVLFVLLGYGFIGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  97 FDDFIKVAMKRNLGLKAWQKLLGQIVGAAVFLLAYFHEGFPHTLALPFVGS--LNVAWVYVVFAVVWLVGFSNAVNLSDG 174
Cdd:TIGR00445  78 VDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFIKDfmFDLGLFYILLAYFVLVGTSNAVNLTDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 175 IDGLCAGLNVVAFGTYAIIAVQEARTD---------------VLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGM 239
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANfakylhipylkdsgeLVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 240 LAVVALLLNRPWSLLLIGIVFVCETASVMIQVFVHHFFHRRVFKMTPIHHSFEMSGWSEWRIDIVFWLTG 309
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIIS 307
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 5-306 1.95e-75

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: 233.10  E-value: 1.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732   5 EMLIPMVAAFAITVILLPLFIGYQRMRKegqtIREIGPKWHAKKNGTPTMGGLILVIAIVASALFAGWWQGQLTLSLLIG 84
Cdd:COG0472     2 RLLLAFLLAFLLSLLLTPLLIRLARRLG----LVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLLLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  85 LfilVLYGALGFFDDFIkvamkrnlGLKAWQKLLGQIVGAAVFLLAYFhegFPHTLALPFVGSLNVAWVYVVFAVVWLVG 164
Cdd:COG0472    78 A---LLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLL---RITSLTIPFFGLLDLGWLYIPLTVFWIVG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 165 FSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVA 244
Cdd:COG0472   144 VSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALA 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2312126732 245 LLLN----RPWSLLLIGIVFVCETASVMIQVFVHhffHRRVFK--MTPIHHSFEMSGWSEWRIDIVFW 306
Cdd:COG0472   224 ILGRqegaSLLLLLLILGVPVVDTLSVILQRVLR---GKRIFKadRAHLHHHLELLGWSERQVVLRFW 288
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
82-247 3.53e-29

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 109.23  E-value: 3.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  82 LIGLFILVLYGALGFFDDFikvamkrnLGLKAWQKLLGQIVGAAVFLLAYFHEGFPHTLALPFVGSLNVAWVYVVFAVVW 161
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLELGPWLSILLTLFA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 162 LVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLA 241
Cdd:pfam00953  73 IVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLA 152


                  ....*.
gi 2312126732 242 VVALLL 247
Cdd:pfam00953 153 VLAIIG 158
 
Name Accession Description Interval E-value
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
 41-319 2.23e-104

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: 306.72  E-value: 2.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  41 GPKWHAKKNGTPTMGGLILVIAIVASALFAGWWQgqlTLSLLIGLFILVLYGALGFFDDFIKVAMKRNLGLKAWQKLLGQ 120
Cdd:cd06852     1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLD---SPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 121 IVGAAVFLLAYFHEGFPHTLA---LPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIA-VQ 196
Cdd:cd06852    78 FLIAIVFALLLYYFNGSGTLItlpFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAyLA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 197 EARTDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALLLNRPWSLLLIGIVFVCETASVMIQVFVHHF 276
Cdd:cd06852   158 GNAVFLAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSFKL 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2312126732 277 FHRRVFKMTPIHHSFEMSGWSEWRIDIVFWLTGAVAGGLYLLL 319
Cdd:cd06852   238 TGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
 17-309 1.20e-81

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: 250.05  E-value: 1.20e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  17 TVILLPLFIGYQRMRKEGQTIREIGPKWHAKKNGTPTMGGLILVIAIVASALFagwWQGQLTLSLLIGLFILVLYGALGF 96
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVL---WAQLGNPYVLLVLFVLLGYGFIGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  97 FDDFIKVAMKRNLGLKAWQKLLGQIVGAAVFLLAYFHEGFPHTLALPFVGS--LNVAWVYVVFAVVWLVGFSNAVNLSDG 174
Cdd:TIGR00445  78 VDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFIKDfmFDLGLFYILLAYFVLVGTSNAVNLTDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 175 IDGLCAGLNVVAFGTYAIIAVQEARTD---------------VLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGM 239
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANfakylhipylkdsgeLVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 240 LAVVALLLNRPWSLLLIGIVFVCETASVMIQVFVHHFFHRRVFKMTPIHHSFEMSGWSEWRIDIVFWLTG 309
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIIS 307
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 5-306 1.95e-75

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: 233.10  E-value: 1.95e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732   5 EMLIPMVAAFAITVILLPLFIGYQRMRKegqtIREIGPKWHAKKNGTPTMGGLILVIAIVASALFAGWWQGQLTLSLLIG 84
Cdd:COG0472     2 RLLLAFLLAFLLSLLLTPLLIRLARRLG----LVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLLLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  85 LfilVLYGALGFFDDFIkvamkrnlGLKAWQKLLGQIVGAAVFLLAYFhegFPHTLALPFVGSLNVAWVYVVFAVVWLVG 164
Cdd:COG0472    78 A---LLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLL---RITSLTIPFFGLLDLGWLYIPLTVFWIVG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 165 FSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVA 244
Cdd:COG0472   144 VSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALA 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2312126732 245 LLLN----RPWSLLLIGIVFVCETASVMIQVFVHhffHRRVFK--MTPIHHSFEMSGWSEWRIDIVFW 306
Cdd:COG0472   224 ILGRqegaSLLLLLLILGVPVVDTLSVILQRVLR---GKRIFKadRAHLHHHLELLGWSERQVVLRFW 288
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 43-269 3.26e-40

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: 141.09  E-value: 3.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  43 KWHAKKngTPTMGGLILVIAIVASALFAGWWQGQLT---LSLLIGLFILVLygaLGFFDDFIkvamkrnlGLKAWQKLLG 119
Cdd:cd06853     2 KVHKGP--IPRLGGLAIFLGFLLALLLALLFPFFLLpelLGLLAGATIIVL---LGLLDDLF--------DLSPKVKLLG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 120 QIVGAAvfLLAYFHEGFPHTLALPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEAR 199
Cdd:cd06853    69 QILAAL--IVVFGGGVILSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQ 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2312126732 200 TDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALLL----NRPWSLLLIGIVF---VCETASVMI 269
Cdd:cd06853   147 VLVALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGtqksSTAISPVVPLLILavpLFDTLFVII 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 50-244 1.75e-33

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: 121.64  E-value: 1.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  50 GTPTMGGLILVIAIVASALFagwWQGQLTLSLLIGLFILVLYGALGFFDDFIKvamkRNLGLKAWQKLLGQIVGAAVFLL 129
Cdd:cd06499     1 PTPTMGGLAILLGFLLGVLL---YIPHSNTLILLALLSGLVAGIVGFIDDLLG----LKVELSEREKLLLQILAALFLLL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 130 AYFhegFPHTLALPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVT 209
Cdd:cd06499    74 IGG---GHTTVTTPLGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLFIIL 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2312126732 210 IGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVA 244
Cdd:cd06499   151 AGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
 51-264 1.91e-30

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: 115.42  E-value: 1.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  51 TPTMGGLILVIAIVASALFAGWWQGQLTLSLLIGLFILVLYGALGFFDDFIkvamkrnlGLKAWQKLLGQIVGAAVFLLA 130
Cdd:cd06854    15 TPRGGGIAFVLAFLLALLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLR--------SLSPKIRLLVQLLAAALALYA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 131 yfhegfpHTLALPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVTI 210
Cdd:cd06854    87 -------LGPLTSLLLNFLPPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAGEPALALLALALA 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2312126732 211 GAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALLLNR----PWSLLLIGIVFVCET 264
Cdd:cd06854   160 GALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALsgqsPWAWLLLLSPFLVDA 217
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
82-247 3.53e-29

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 109.23  E-value: 3.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  82 LIGLFILVLYGALGFFDDFikvamkrnLGLKAWQKLLGQIVGAAVFLLAYFHEGFPHTLALPFVGSLNVAWVYVVFAVVW 161
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLELGPWLSILLTLFA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 162 LVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLA 241
Cdd:pfam00953  73 IVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLA 152


                  ....*.
gi 2312126732 242 VVALLL 247
Cdd:pfam00953 153 VLAIIG 158
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 52-261 7.68e-25

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: 101.17  E-value: 7.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  52 PTMGGLILVIAIVASALFAGWWQGQLTLSLLIGLFILVlyGALGFFDDFikvamkrnLGLKAWQKLLGQIVGAAVFLLAY 131
Cdd:cd06856    14 PEMGGIAVLLGFSLGLLFLSALTHSVEALALLITSLLA--GLIGLLDDI--------LGLSQSEKVLLTALPAIPLLVLK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 132 fhEGFPHTLaLPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVTIG 211
Cdd:cd06856    84 --AGNPLTS-LPIGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIALILVA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2312126732 212 AMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALLLNRPWSLLLIGIVFV 261
Cdd:cd06856   161 ALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYV 210
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 51-244 2.65e-21

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: 89.61  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  51 TPTMGGLILVIAIVASALFAGWWQGQLTLSLLIGLFILVlygALGFFDDFIKvamkrnlGLKAWQKLLGQIVGAAVFLLa 130
Cdd:cd06912    11 TPRIGGVAIFLGLLAGLLLLSLLSGSLLLLLLLAALPAF---LAGLLEDITK-------RVSPRIRLLATFLSALLAVW- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 131 YFHEGFPHTLALPFVGSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLILCLVTI 210
Cdd:cd06912    80 LLGASITRLDLPGLDLLLSFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDTDLAFLALLLA 159

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2312126732 211 GAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVA 244
Cdd:cd06912   160 GALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 52-246 1.77e-14

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: 71.38  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  52 PTMGGLILVIAIVASAL----FAGWWQGQLTLSLLIGLFILVLYG-ALGFFDDFikvamkrnLGLKAWQKLLGQIVGAAV 126
Cdd:cd06851    14 PEPGGISILIGFVASEItlifFPFLSFPHFPISEILAALITSVLGfSVGIIDDR--------LTMGGWFKPVALAFAAAP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 127 FLLAYFHEGfphTLALPFVG-SLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAGLNVVAFGTYAIIAVQEARTDVLIL 205
Cdd:cd06851    86 ILLLGAYDS---NLDFPLFGgSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQNYEIGIA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2312126732 206 CLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALL 246
Cdd:cd06851   163 CLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAIL 203
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
 58-246 7.10e-08

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: 53.02  E-value: 7.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732  58 ILVIAIVASALFAGWWQGQLTLSLLIGLFILVLYGALGFFDDFikvamkrnLGLKAWQKLLGQIVGAAVFLLAYF----- 132
Cdd:cd06855    39 LIVLFLFIPFPFLKDFPHDKLVEYLSALLSICCMTFLGFADDV--------LDLRWRHKLILPTFASLPLLMVYYgntgi 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312126732 133 -HEGFPHTLALPFvgSLNVAWVYVVFAVVWLVGFSNAVNLSDGIDGLCAG-----------LNVVAFGTYAIIAVQEART 200
Cdd:cd06855   111 tLPIVPLRPLLGT--LIDLGILYYVYMILLAVFCTNSINIYAGINGLEVGqslvialsillYNLLELNGSSGSMTLDAHL 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2312126732 201 DVLILCLVTIGAMIGFLLYNHKPAQIFMGDVGSLALGGMLAVVALL 246
Cdd:cd06855   189 FSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGIL 234
 
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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