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Conserved domains on  [gi|61214219|sp|Q74JY6|]
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RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase; AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase

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 ...
 39-317 7.06e-108

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: 315.58  E-value: 7.06e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  39 GPKWHEKKSGTPTMGGVVFMLAGVISTLwvlIWQKDLNKTAWILIIAFLGYGIIGFLDDGIKLYFKRNLGLRAWQKLLGQ 118
Cdd:cd06852   1 GPKSHLKKAGTPTMGGILFILAILISTL---LWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 119 IIIAALIITLAFSDHFAFELYI---PFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQE 195
Cdd:cd06852  78 FLIAIVFALLLYYFNGSGTLITlpfFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 196 RNWVIV-VFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIFLHRPWSLLLIGIVFVLETLSVILQVISFQT 274
Cdd:cd06852 158 GNAVFLaVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSFKL 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 61214219 275 TGKRIFKMTPIHHHFEMLGWSEWKVDIVFWIVGLIGSIIYLII 317
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 ...
 39-317 7.06e-108

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: 315.58  E-value: 7.06e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  39 GPKWHEKKSGTPTMGGVVFMLAGVISTLwvlIWQKDLNKTAWILIIAFLGYGIIGFLDDGIKLYFKRNLGLRAWQKLLGQ 118
Cdd:cd06852   1 GPKSHLKKAGTPTMGGILFILAILISTL---LWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 119 IIIAALIITLAFSDHFAFELYI---PFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQE 195
Cdd:cd06852  78 FLIAIVFALLLYYFNGSGTLITlpfFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 196 RNWVIV-VFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIFLHRPWSLLLIGIVFVLETLSVILQVISFQT 274
Cdd:cd06852 158 GNAVFLaVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSFKL 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 61214219 275 TGKRIFKMTPIHHHFEMLGWSEWKVDIVFWIVGLIGSIIYLII 317
Cdd:cd06852 238 TGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
 15-316 3.84e-87

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: 264.31  E-value: 3.84e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219    15 TVIFLPLFIGFMRMKHEGQVIRDEGPKWHEKKSGTPTMGGVVFMLAGVISTLwvlIWQKDLNKTAWILIIAFLGYGIIGF 94
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTV---LWAQLGNPYVLLVLFVLLGYGFIGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219    95 LDDGIKLYFKRNLGLRAWQKLLGQIIIAALIITLAFSDHFAFELYIPFAG--MVRNSFLFSLFVLFWLVGFSNAVNLSDG 172
Cdd:TIGR00445  78 VDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFIKdfMFDLGLFYILLAYFVLVGTSNAVNLTDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219   173 LDGLATGLSIIAYATYAWIAYQERNW---------------VIVVFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGG 237
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNAnfakylhipylkdsgELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61214219   238 LATVSIFLHRPWSLLLIGIVFVLETLSVILQVISFQTTGKRIFKMTPIHHHFEMLGWSEWKVDIVFWIVGLIGSIIYLI 316
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALA 316
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 5-304 1.51e-76

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: 235.79  E-value: 1.51e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219   5 LIPFISSFALTVIFLPLFIGFMRMKHegqvIRDEGPKWHEKKSGTPTMGGVVFMLAGVISTLwvlIWQKDLNKTAWILII 84
Cdd:COG0472   4 LLAFLLAFLLSLLLTPLLIRLARRLG----LVDDPNERKSHKRPTPRMGGIAIFLGFLLALL---LLALLSNPELLLLLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  85 AFLGYGIIGFLDDGIklyfkrnlGLRAWQKLLGQIIIAALIITLAFSDHFafeLYIPFAGMVRNSFLFSLFVLFWLVGFS 164
Cdd:COG0472  77 GALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRITS---LTIPFFGLLDLGWLYIPLTVFWIVGVS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 165 NAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIF 244
Cdd:COG0472 146 NAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAIL 225

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61214219 245 LH----RPWSLLLIGIVFVLETLSVILQVIsfqTTGKRIFK--MTPIHHHFEMLGWSEWKVDIVFW 304
Cdd:COG0472 226 GRqegaSLLLLLLILGVPVVDTLSVILQRV---LRGKRIFKadRAHLHHHLELLGWSERQVVLRFW 288
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
80-245 4.53e-27

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 103.83  E-value: 4.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219    80 WILIIAFLGYGIIGFLDDgiklyfkrNLGLRAWQKLLGQIIIAALIITLAFSDHFAFELYIPFAGMVRNSFLFSLFVLFW 159
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDD--------LLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLELGPWLSILLTLFA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219   160 LVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLA 239
Cdd:pfam00953  73 IVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLA 152


                  ....*.
gi 61214219   240 TVSIFL 245
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 ...
 39-317 7.06e-108

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: 315.58  E-value: 7.06e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  39 GPKWHEKKSGTPTMGGVVFMLAGVISTLwvlIWQKDLNKTAWILIIAFLGYGIIGFLDDGIKLYFKRNLGLRAWQKLLGQ 118
Cdd:cd06852   1 GPKSHLKKAGTPTMGGILFILAILISTL---LWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQ 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 119 IIIAALIITLAFSDHFAFELYI---PFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQE 195
Cdd:cd06852  78 FLIAIVFALLLYYFNGSGTLITlpfFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 196 RNWVIV-VFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIFLHRPWSLLLIGIVFVLETLSVILQVISFQT 274
Cdd:cd06852 158 GNAVFLaVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSFKL 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 61214219 275 TGKRIFKMTPIHHHFEMLGWSEWKVDIVFWIVGLIGSIIYLII 317
Cdd:cd06852 238 TGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
 15-316 3.84e-87

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: 264.31  E-value: 3.84e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219    15 TVIFLPLFIGFMRMKHEGQVIRDEGPKWHEKKSGTPTMGGVVFMLAGVISTLwvlIWQKDLNKTAWILIIAFLGYGIIGF 94
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTV---LWAQLGNPYVLLVLFVLLGYGFIGF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219    95 LDDGIKLYFKRNLGLRAWQKLLGQIIIAALIITLAFSDHFAFELYIPFAG--MVRNSFLFSLFVLFWLVGFSNAVNLSDG 172
Cdd:TIGR00445  78 VDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFIKdfMFDLGLFYILLAYFVLVGTSNAVNLTDG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219   173 LDGLATGLSIIAYATYAWIAYQERNW---------------VIVVFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGG 237
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNAnfakylhipylkdsgELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 61214219   238 LATVSIFLHRPWSLLLIGIVFVLETLSVILQVISFQTTGKRIFKMTPIHHHFEMLGWSEWKVDIVFWIVGLIGSIIYLI 316
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALA 316
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
 5-304 1.51e-76

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: 235.79  E-value: 1.51e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219   5 LIPFISSFALTVIFLPLFIGFMRMKHegqvIRDEGPKWHEKKSGTPTMGGVVFMLAGVISTLwvlIWQKDLNKTAWILII 84
Cdd:COG0472   4 LLAFLLAFLLSLLLTPLLIRLARRLG----LVDDPNERKSHKRPTPRMGGIAIFLGFLLALL---LLALLSNPELLLLLL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  85 AFLGYGIIGFLDDGIklyfkrnlGLRAWQKLLGQIIIAALIITLAFSDHFafeLYIPFAGMVRNSFLFSLFVLFWLVGFS 164
Cdd:COG0472  77 GALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRITS---LTIPFFGLLDLGWLYIPLTVFWIVGVS 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 165 NAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIF 244
Cdd:COG0472 146 NAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAIL 225

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61214219 245 LH----RPWSLLLIGIVFVLETLSVILQVIsfqTTGKRIFK--MTPIHHHFEMLGWSEWKVDIVFW 304
Cdd:COG0472 226 GRqegaSLLLLLLILGVPVVDTLSVILQRV---LRGKRIFKadRAHLHHHLELLGWSERQVVLRFW 288
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
 41-267 6.13e-35

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: 127.22  E-value: 6.13e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  41 KWHEKKsgTPTMGGVVFMLAGVISTLWVLIWQKDLNKTAWILIIAFLGYGIIGFLDDgikLYfkrnlGLRAWQKLLGQII 120
Cdd:cd06853   2 KVHKGP--IPRLGGLAIFLGFLLALLLALLFPFFLLPELLGLLAGATIIVLLGLLDD---LF-----DLSPKVKLLGQIL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 121 IAALIITlaFSDHFAFELYIPFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVI 200
Cdd:cd06853  72 AALIVVF--GGGVILSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLV 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61214219 201 VVFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIFL----HRPWSLLLIGIVF---VLETLSVIL 267
Cdd:cd06853 150 ALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGtqksSTAISPVVPLLILavpLFDTLFVII 223
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
 48-242 3.86e-31

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: 115.48  E-value: 3.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  48 GTPTMGGVVFMLAGVIStlwVLIWQKDLNKTAWILIIAFLGYGIIGFLDDgiklYFKRNLGLRAWQKLLGQIIIAALIIT 127
Cdd:cd06499   1 PTPTMGGLAILLGFLLG---VLLYIPHSNTLILLALLSGLVAGIVGFIDD----LLGLKVELSEREKLLLQILAALFLLL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 128 LAFsdhfAFELYIPFAGMVRN-SFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLS 206
Cdd:cd06499  74 IGG----GHTTVTTPLGFVLDlGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLFII 149

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 61214219 207 VIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVS 242
Cdd:cd06499 150 LAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
80-245 4.53e-27

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 103.83  E-value: 4.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219    80 WILIIAFLGYGIIGFLDDgiklyfkrNLGLRAWQKLLGQIIIAALIITLAFSDHFAFELYIPFAGMVRNSFLFSLFVLFW 159
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDD--------LLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLELGPWLSILLTLFA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219   160 LVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLA 239
Cdd:pfam00953  73 IVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLA 152


                  ....*.
gi 61214219   240 TVSIFL 245
Cdd:pfam00953 153 VLAIIG 158
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
 49-267 2.51e-25

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: 101.94  E-value: 2.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  49 TPTMGGVVFMLAGVISTLWVLIWQKDLNKTAWILIIAFLGYGIIGFLDDGIklyfkrnlGLRAWQKLLGQIIIAALIItl 128
Cdd:cd06854  15 TPRGGGIAFVLAFLLALLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLR--------SLSPKIRLLVQLLAAALAL-- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 129 afsdhFAFELYIPFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLSVI 208
Cdd:cd06854  85 -----YALGPLTSLLLNFLPPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAGEPALALLALALA 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 61214219 209 GGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIFLHR----PWSLLLIGIVFVLETLSVIL 267
Cdd:cd06854 160 GALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALsgqsPWAWLLLLSPFLVDATVTLL 222
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
 50-266 3.93e-19

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: 85.38  E-value: 3.93e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  50 PTMGGVVFMLAGVISTLwVLIWQKDLNKTAWILIIAFLGyGIIGFLDDgiklyfkrNLGLRAWQKLLGQIIIAALIITLA 129
Cdd:cd06856  14 PEMGGIAVLLGFSLGLL-FLSALTHSVEALALLITSLLA-GLIGLLDD--------ILGLSQSEKVLLTALPAIPLLVLK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 130 FSDhfaFELYIPFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLSVIG 209
Cdd:cd06856  84 AGN---PLTSLPIGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIALILVA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 61214219 210 GLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIFLHRPWSLLLIGIVFVLETLSVI 266
Cdd:cd06856 161 ALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVIDFLLKL 217
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
 49-242 4.05e-19

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: 83.45  E-value: 4.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  49 TPTMGGVVFmLAGVISTLWVLIWQKDlnKTAWILIIAFLGYGIIGFLDDgiklYFKRNLglrAWQKLLGQIIIAALIITL 128
Cdd:cd06912  11 TPRIGGVAI-FLGLLAGLLLLSLLSG--SLLLLLLLAALPAFLAGLLED----ITKRVS---PRIRLLATFLSALLAVWL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 129 aFSDHFAFELYIPFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFTLSVI 208
Cdd:cd06912  81 -LGASITRLDLPGLDLLLSFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDTDLAFLALLLA 159

                       170       180       190
                ....*....|....*....|....*....|....
gi 61214219 209 GGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVS 242
Cdd:cd06912 160 GALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
 50-246 8.09e-08

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: 52.12  E-value: 8.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219  50 PTMGGVVFMLAGVISTL-WVLIWQKDLNKTAWILIIAFLGYG----IIGFLDDgiklyfkrNLGLRAWQKLLGQIIIAAL 124
Cdd:cd06851  14 PEPGGISILIGFVASEItLIFFPFLSFPHFPISEILAALITSvlgfSVGIIDD--------RLTMGGWFKPVALAFAAAP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61214219 125 IITLAFSDhfAFELYIPFAGMVRNSFLFSLFVLFWLVGFSNAVNLSDGLDGLATGLSIIAYATYAWIAYQERNWVIVVFT 204
Cdd:cd06851  86 ILLLGAYD--SNLDFPLFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQNYEIGIAC 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 61214219 205 LSVIGGLVGFFIFNHKPAKIFMGDAGSLALGGGLATVSIFLH 246
Cdd:cd06851 164 LCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGE 205
 
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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