NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|512465174|ref|WP_016423002|]
View 

MULTISPECIES: phospho-N-acetylmuramoyl-pentapeptide-transferase [Corynebacterium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
39-355 1.25e-91

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: 275.91  E-value: 1.25e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  39 GPKSHLRKRGTPTMGGIAIIAAIVAGYFLSHLVTyiqtgvgpSASGLLVMFLVLAMGALGFADDFIKLYKGRNLGLNKTA 118
Cdd:cd06852    1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLD--------SPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 119 KLVGQLAAALIFGVLLLQFPDASGLTPgstslslirdIPFLnlaPGPVWFGMIVFLVFVFIVIAAWTNAVNLTDGLDGLA 198
Cdd:cd06852   73 KLLLQFLIAIVFALLLYYFNGSGTLIT----------LPFF---KNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 199 AGATALLLATYTLISFWQFRNSCeaslgsgcynvrdpldIAVISVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAG 278
Cdd:cd06852  140 AGVSIIVALALAIIAYLAGNAVF----------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAA 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512465174 279 LSFVTKTELLMVIIGFIFVMEVASVAIQIAVFQTTGKRVFRMAPLHHHFENGGWAETTVVVRFWLLAGIFNMIGAAI 355
Cdd:cd06852  204 LAILTKQELLLLIIGGVFVIEALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
 
Name Accession Description Interval E-value
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
39-355 1.25e-91

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: 275.91  E-value: 1.25e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  39 GPKSHLRKRGTPTMGGIAIIAAIVAGYFLSHLVTyiqtgvgpSASGLLVMFLVLAMGALGFADDFIKLYKGRNLGLNKTA 118
Cdd:cd06852    1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLD--------SPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 119 KLVGQLAAALIFGVLLLQFPDASGLTPgstslslirdIPFLnlaPGPVWFGMIVFLVFVFIVIAAWTNAVNLTDGLDGLA 198
Cdd:cd06852   73 KLLLQFLIAIVFALLLYYFNGSGTLIT----------LPFF---KNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 199 AGATALLLATYTLISFWQFRNSCeaslgsgcynvrdpldIAVISVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAG 278
Cdd:cd06852  140 AGVSIIVALALAIIAYLAGNAVF----------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAA 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512465174 279 LSFVTKTELLMVIIGFIFVMEVASVAIQIAVFQTTGKRVFRMAPLHHHFENGGWAETTVVVRFWLLAGIFNMIGAAI 355
Cdd:cd06852  204 LAILTKQELLLLIIGGVFVIEALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
15-354 1.69e-69

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: 220.78  E-value: 1.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   15 SVFLTPVLIRKFSAEGLGQEIREEGPKSHLRKRGTPTMGGIAiiaaivagYFLSHLVTYIQTGVGPSASGLLVMFLVLAM 94
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIM--------IVFAIIVSTVLWAQLGNPYVLLVLFVLLGY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   95 GALGFADDFIKLYKGRNLGLNKTAKLVGQLAAALIFGVLLLQFpdasGLTpgstslSLIRDIPFLNLAPGPVWFgmivFL 174
Cdd:TIGR00445  73 GFIGFVDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYY----GPD------TFIYIPFIKDFMFDLGLF----YI 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  175 VFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFWQFRNSCEASLGSGcyNVRDPLDIAVISVAGLGACLGFLW 254
Cdd:TIGR00445 139 LLAYFVLVGTSNAVNLTDGLDGLAIGPSAIAFGALAILAWATGNANFAKYLHIP--YLKDSGELVIFCTALVGASLGFLW 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  255 WNAAPAKIFMGDTGSLALGGLVAGLSFVTKTELLMVIIGFIFVMEVASVAIQIAVFQTTGKRVFRMAPLHHHFENGGWAE 334
Cdd:TIGR00445 217 FNAYPAKVFMGDTGSLALGGALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSE 296
                         330       340
                  ....*....|....*....|
gi 512465174  335 TTVVVRFWLLAGIFNMIGAA 354
Cdd:TIGR00445 297 PRVVVRFWIISLLLALVALA 316
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
2-342 3.03e-59

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: 193.03  E-value: 3.03e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   2 IQLILSGAIAFLVSVFLTPVLIRKFSAEGLGQEIREEgpKSHlrKRGTPTMGGIAIiaaivagyFLSHLVTYIQTGVGPS 81
Cdd:COG0472    1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNER--KSH--KRPTPRMGGIAI--------FLGFLLALLLLALLSN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  82 ASGLLVMFLVLAMGALGFADDFIklykgrnlGLNKTAKLVGQLAAALIFGVLLLQFPDASGLTPGSTSLSlirdipflnl 161
Cdd:COG0472   69 PELLLLLLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRITSLTIPFFGLLDLG---------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 162 apgpvwfgmIVFLVFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFWQfrnsceaslgsgcynvrDPLDIAVI 241
Cdd:COG0472  131 ---------WLYIPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLA-----------------GQGELALL 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 242 SVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLSFVTKTE----LLMVIIGFIFVMEVASVAIQIAVfqtTGKRV 317
Cdd:COG0472  185 AAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQRVL---RGKRI 261
                        330       340
                 ....*....|....*....|....*..
gi 512465174 318 FR--MAPLHHHFENGGWAETTVVVRFW 342
Cdd:COG0472  262 FKadRAHLHHHLELLGWSERQVVLRFW 288
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
85-280 1.15e-20

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 87.66  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   85 LLVMFLVLAMGALGFADDFiklykgrnLGLNKTAKLVGQLAAALIFGVLLLqfpdasgltPGSTSLSLIRDIPFLNLapg 164
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGG---------IGLTSLGLPFGGGSLEL--- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  165 pvwfGMIVFLVFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFwqfrnsceaslgsgcynVRDPLDIAVISVA 244
Cdd:pfam00953  61 ----GPWLSILLTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAY-----------------LLGNLELALLSLA 119
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 512465174  245 GLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLS 280
Cdd:pfam00953 120 LLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLA 155
 
Name Accession Description Interval E-value
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
39-355 1.25e-91

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: 275.91  E-value: 1.25e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  39 GPKSHLRKRGTPTMGGIAIIAAIVAGYFLSHLVTyiqtgvgpSASGLLVMFLVLAMGALGFADDFIKLYKGRNLGLNKTA 118
Cdd:cd06852    1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLD--------SPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 119 KLVGQLAAALIFGVLLLQFPDASGLTPgstslslirdIPFLnlaPGPVWFGMIVFLVFVFIVIAAWTNAVNLTDGLDGLA 198
Cdd:cd06852   73 KLLLQFLIAIVFALLLYYFNGSGTLIT----------LPFF---KNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 199 AGATALLLATYTLISFWQFRNSCeaslgsgcynvrdpldIAVISVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAG 278
Cdd:cd06852  140 AGVSIIVALALAIIAYLAGNAVF----------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAA 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512465174 279 LSFVTKTELLMVIIGFIFVMEVASVAIQIAVFQTTGKRVFRMAPLHHHFENGGWAETTVVVRFWLLAGIFNMIGAAI 355
Cdd:cd06852  204 LAILTKQELLLLIIGGVFVIEALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
15-354 1.69e-69

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: 220.78  E-value: 1.69e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   15 SVFLTPVLIRKFSAEGLGQEIREEGPKSHLRKRGTPTMGGIAiiaaivagYFLSHLVTYIQTGVGPSASGLLVMFLVLAM 94
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIM--------IVFAIIVSTVLWAQLGNPYVLLVLFVLLGY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   95 GALGFADDFIKLYKGRNLGLNKTAKLVGQLAAALIFGVLLLQFpdasGLTpgstslSLIRDIPFLNLAPGPVWFgmivFL 174
Cdd:TIGR00445  73 GFIGFVDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYY----GPD------TFIYIPFIKDFMFDLGLF----YI 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  175 VFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFWQFRNSCEASLGSGcyNVRDPLDIAVISVAGLGACLGFLW 254
Cdd:TIGR00445 139 LLAYFVLVGTSNAVNLTDGLDGLAIGPSAIAFGALAILAWATGNANFAKYLHIP--YLKDSGELVIFCTALVGASLGFLW 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  255 WNAAPAKIFMGDTGSLALGGLVAGLSFVTKTELLMVIIGFIFVMEVASVAIQIAVFQTTGKRVFRMAPLHHHFENGGWAE 334
Cdd:TIGR00445 217 FNAYPAKVFMGDTGSLALGGALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSE 296
                         330       340
                  ....*....|....*....|
gi 512465174  335 TTVVVRFWLLAGIFNMIGAA 354
Cdd:TIGR00445 297 PRVVVRFWIISLLLALVALA 316
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
2-342 3.03e-59

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: 193.03  E-value: 3.03e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   2 IQLILSGAIAFLVSVFLTPVLIRKFSAEGLGQEIREEgpKSHlrKRGTPTMGGIAIiaaivagyFLSHLVTYIQTGVGPS 81
Cdd:COG0472    1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNER--KSH--KRPTPRMGGIAI--------FLGFLLALLLLALLSN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  82 ASGLLVMFLVLAMGALGFADDFIklykgrnlGLNKTAKLVGQLAAALIFGVLLLQFPDASGLTPGSTSLSlirdipflnl 161
Cdd:COG0472   69 PELLLLLLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRITSLTIPFFGLLDLG---------- 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 162 apgpvwfgmIVFLVFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFWQfrnsceaslgsgcynvrDPLDIAVI 241
Cdd:COG0472  131 ---------WLYIPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLA-----------------GQGELALL 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 242 SVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLSFVTKTE----LLMVIIGFIFVMEVASVAIQIAVfqtTGKRV 317
Cdd:COG0472  185 AAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQRVL---RGKRI 261
                        330       340
                 ....*....|....*....|....*..
gi 512465174 318 FR--MAPLHHHFENGGWAETTVVVRFW 342
Cdd:COG0472  262 FKadRAHLHHHLELLGWSERQVVLRFW 288
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
85-280 1.15e-20

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 87.66  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174   85 LLVMFLVLAMGALGFADDFiklykgrnLGLNKTAKLVGQLAAALIFGVLLLqfpdasgltPGSTSLSLIRDIPFLNLapg 164
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGG---------IGLTSLGLPFGGGSLEL--- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  165 pvwfGMIVFLVFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFwqfrnsceaslgsgcynVRDPLDIAVISVA 244
Cdd:pfam00953  61 ----GPWLSILLTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAY-----------------LLGNLELALLSLA 119
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 512465174  245 GLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLS 280
Cdd:pfam00953 120 LLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLA 155
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
85-277 7.75e-14

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: 69.25  E-value: 7.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  85 LLVMFLVLAMGALGFADDfiklYKGRNLGLNKTAKLVGQLAAALIFGVLllqfpdasglTPGSTSLSLIrdipflnlaPG 164
Cdd:cd06499   30 LLALLSGLVAGIVGFIDD----LLGLKVELSEREKLLLQILAALFLLLI----------GGGHTTVTTP---------LG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 165 PVWFGMIVFLVFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLIsfwqfrnsceaslgsgcYNVRDPLDIAVISVA 244
Cdd:cd06499   87 FVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALF-----------------ALLSGQTTSALLFII 149
                        170       180       190
                 ....*....|....*....|....*....|...
gi 512465174 245 GLGACLGFLWWNAAPAKIFMGDTGSLALGGLVA 277
Cdd:cd06499  150 LAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYA 182
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
70-280 2.44e-13

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: 69.05  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  70 LVTYIQTGVGPSASGLLVMFLVLAMGALGFADDFIklykgrnlGLNKTAKLVGQLAAALI---FGVLLLQFPdasgltpg 146
Cdd:cd06853   24 LLLALLFPFFLLPELLGLLAGATIIVLLGLLDDLF--------DLSPKVKLLGQILAALIvvfGGGVILSLL-------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 147 stslslirdIPFLNLAPGPVWFGmIVFLVFVFIVIaawTNAVNLTDGLDGLAAGATALLLATYTLISFwqfrnsceaslg 226
Cdd:cd06853   88 ---------GPFGGGIILLGWLS-IPLTVLWIVGI---INAINLIDGLDGLAGGVALIASLALAILAL------------ 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 512465174 227 sgcynVRDPLDIAVISVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLS 280
Cdd:cd06853  143 -----LNGQVLVALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLS 191
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
70-281 2.21e-12

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: 66.11  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  70 LVTYIQTGVGPSASGLLVMFLVLAmgALGFADDFIklykgrnlGLNKTAKLVGQLAAALIFGVLLLQFPdasgltpgsts 149
Cdd:cd06854   33 LAAAAGPLNDLSYLLLLIGLLLLA--AVGFIDDLR--------SLSPKIRLLVQLLAAALALYALGPLT----------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 150 lslirdIPFLNLAPGPVWfgmivfLVFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFWQfrnsceaslgsgc 229
Cdd:cd06854   92 ------SLLLNFLPPWLI------ALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLA------------- 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 512465174 230 ynvrDPLDIAVISVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLSF 281
Cdd:cd06854  147 ----GEPALALLALALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLL 194
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
85-299 9.41e-11

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: 61.88  E-value: 9.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  85 LLVMFLVLAMGALGFADDFiklykgrnLGLNKTAKLVGQLAAALIFGVLLLQFPdasgltpgstslslirdipFLNLAPG 164
Cdd:cd06856   42 LALLITSLLAGLIGLLDDI--------LGLSQSEKVLLTALPAIPLLVLKAGNP-------------------LTSLPIG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 165 PVWFGMIVFLVFVFIVIAAWTNAVNLTDGLDGLAAGATALLLATYTLISFwqfrnsceaslgsgcynVRDPLDIAVISVA 244
Cdd:cd06856   95 GRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILL-----------------INGDYDALIIALI 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 512465174 245 GLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLSFVTKTELLMVIIGFIFVME 299
Cdd:cd06856  158 LVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVID 212
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
66-280 3.79e-08

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: 53.01  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174  66 FLSHLVTYIQTGVGPSASGLLVMFLVLAMGALGFADDFIKLykgrnlgLNKTAKLVGQLAAALIFGVLLLQfpdasgltp 145
Cdd:cd06912   20 FLGLLAGLLLLSLLSGSLLLLLLLAALPAFLAGLLEDITKR-------VSPRIRLLATFLSALLAVWLLGA--------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512465174 146 gstsLSLIRDIPFLNLAPGPVWFGMIVFLVFVfiviAAWTNAVNLTDGLDGLAAGATALLLATYTLISFwqfrnsceasl 225
Cdd:cd06912   84 ----SITRLDLPGLDLLLSFPPFAIIFTIFAV----AGVANAFNIIDGFNGLASGVAIISLLSLALVAF----------- 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 512465174 226 gsgcyNVRDPlDIAVISVAGLGACLGFLWWNAAPAKIFMGDTGSLALGGLVAGLS 280
Cdd:cd06912  145 -----QVGDT-DLAFLALLLAGALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH