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Conserved domains on  [gi|518172454|ref|WP_019342662|]
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phospho-N-acetylmuramoyl-pentapeptide-transferase [Stutzerimonas stutzeri]

Protein Classification

MraY family glycosyltransferase( domain architecture ID 474)

MraY family glycosyltransferase such as phospho-N-acetylmuramoyl-pentapeptide-transferase that 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

CAZY:  GT4
PubMed:  7734839|11024259
SCOP:  3002333

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT_MraY-like super family cl10571
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
37-360 5.33e-135

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.


The actual alignment was detected with superfamily member TIGR00445:

Pssm-ID: 471988  Cd Length: 321  Bit Score: 387.57  E-value: 5.33e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454   37 SLWLGPWLIRTLQLRQIGQAVRTDGPQTHLSKSGTPTMGGALILSAIAISTLLWADLSNRYVWVVLAVTLLFGAIGWVDD 116
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  117 YRKVIEKNSRGLPSRWKYFWQSVFGLGAAVFLYLTAQtpvETTLILPLLKNIEIPLGIGFIVLTYFVIVGSSNAVNLTDG 196
Cdd:TIGR00445  81 YRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGP---DTFIYIPFIKDFMFDLGLFYILLAYFVLVGTSNAVNLTDG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  197 LDGLAIMPTVMVGGGLGIFCYLSGNVNFADYLLIPYIPGAGELIVFCGALIGAGLGFLWFNTYPAQVFMGDVGALALGAA 276
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  277 LGTIAVIVRQEVVLFIMGGVFVMETLSVMIQVASFKLTGKRVFRMAPIHHHFELKGWPEPRVIVRFWIITVILVLVGLAT 356
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALAT 317

                  ....
gi 518172454  357 LKLR 360
Cdd:TIGR00445 318 LKVR 321
 
Name Accession Description Interval E-value
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
37-360 5.33e-135

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: 387.57  E-value: 5.33e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454   37 SLWLGPWLIRTLQLRQIGQAVRTDGPQTHLSKSGTPTMGGALILSAIAISTLLWADLSNRYVWVVLAVTLLFGAIGWVDD 116
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  117 YRKVIEKNSRGLPSRWKYFWQSVFGLGAAVFLYLTAQtpvETTLILPLLKNIEIPLGIGFIVLTYFVIVGSSNAVNLTDG 196
Cdd:TIGR00445  81 YRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGP---DTFIYIPFIKDFMFDLGLFYILLAYFVLVGTSNAVNLTDG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  197 LDGLAIMPTVMVGGGLGIFCYLSGNVNFADYLLIPYIPGAGELIVFCGALIGAGLGFLWFNTYPAQVFMGDVGALALGAA 276
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  277 LGTIAVIVRQEVVLFIMGGVFVMETLSVMIQVASFKLTGKRVFRMAPIHHHFELKGWPEPRVIVRFWIITVILVLVGLAT 356
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALAT 317

                  ....
gi 518172454  357 LKLR 360
Cdd:TIGR00445 318 LKVR 321
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
61-356 4.57e-125

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: 360.65  E-value: 4.57e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  61 GPQTHLSKSGTPTMGGALILSAIAISTLLWADLSNRYVWVVLAVTLLFGAIGWVDDYRKVIEKNSRGLPSRWKYFWQSVF 140
Cdd:cd06852    1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 141 GLGAAVFLYLtaQTPVETTLILPLLKNIEIPLGIGFIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSG 220
Cdd:cd06852   81 AIVFALLLYY--FNGSGTLITLPFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 221 NVNFadyllipyipgageLIVFCGALIGAGLGFLWFNTYPAQVFMGDVGALALGAALGTIAVIVRQEVVLFIMGGVFVME 300
Cdd:cd06852  159 NAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIE 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 518172454 301 TLSVMIQVASFKLTGKRVFRMAPIHHHFELKGWPEPRVIVRFWIITVILVLVGLAT 356
Cdd:cd06852  225 ALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
24-343 7.40e-83

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: 253.51  E-value: 7.40e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  24 LRGILGVLTALVLSLWLGPWLIRTLQLRQIgqavrTDGPQTHLS-KSGTPTMGGALILSAIAISTLLWADLSNRYVWVVL 102
Cdd:COG0472    1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGL-----VDDPNERKShKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 103 AVTLLFGAIGWVDDYRkvieknsrGLPSRWKYFWQSVFGLGAAVFLYLTaqtpveTTLILPLLKniEIPLGIGFIVLTYF 182
Cdd:COG0472   76 LGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRI------TSLTIPFFG--LLDLGWLYIPLTVF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 183 VIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNvnfadyllipyipgaGELIVFCGALIGAGLGFLWFNTYPAQ 262
Cdd:COG0472  140 WIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALAGALLGFLWFNFPPAK 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 263 VFMGDVGALALGAALGTIAVIVRQE----VVLFIMGGVFVMETLSVMIQVasfKLTGKRVFR--MAPIHHHFELKGWPEP 336
Cdd:COG0472  205 IFMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQR---VLRGKRIFKadRAHLHHHLELLGWSER 281

                 ....*..
gi 518172454 337 RVIVRFW 343
Cdd:COG0472  282 QVVLRFW 288
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
99-268 1.89e-22

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 92.28  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454   99 WVVLAVTLLFGAIGWVDDYRkvieknsrGLPSRWKYFWQSVFGLGAAVFLYLTAqtpveTTLILPLLKNIEIPLGIGFIV 178
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILLVLGGIGL-----TSLGLPFGGGSLELGPWLSIL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  179 LTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNVnfadyllipyipgagELIVFCGALIGAGLGFLWFNT 258
Cdd:pfam00953  68 LTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNL---------------ELALLSLALLGALLGFLPFNF 132
                         170
                  ....*....|
gi 518172454  259 YPAQVFMGDV 268
Cdd:pfam00953 133 YPAKIFMGDS 142
 
Name Accession Description Interval E-value
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
37-360 5.33e-135

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: 387.57  E-value: 5.33e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454   37 SLWLGPWLIRTLQLRQIGQAVRTDGPQTHLSKSGTPTMGGALILSAIAISTLLWADLSNRYVWVVLAVTLLFGAIGWVDD 116
Cdd:TIGR00445   1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  117 YRKVIEKNSRGLPSRWKYFWQSVFGLGAAVFLYLTAQtpvETTLILPLLKNIEIPLGIGFIVLTYFVIVGSSNAVNLTDG 196
Cdd:TIGR00445  81 YRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGP---DTFIYIPFIKDFMFDLGLFYILLAYFVLVGTSNAVNLTDG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  197 LDGLAIMPTVMVGGGLGIFCYLSGNVNFADYLLIPYIPGAGELIVFCGALIGAGLGFLWFNTYPAQVFMGDVGALALGAA 276
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  277 LGTIAVIVRQEVVLFIMGGVFVMETLSVMIQVASFKLTGKRVFRMAPIHHHFELKGWPEPRVIVRFWIITVILVLVGLAT 356
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALAT 317

                  ....
gi 518172454  357 LKLR 360
Cdd:TIGR00445 318 LKVR 321
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
61-356 4.57e-125

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: 360.65  E-value: 4.57e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  61 GPQTHLSKSGTPTMGGALILSAIAISTLLWADLSNRYVWVVLAVTLLFGAIGWVDDYRKVIEKNSRGLPSRWKYFWQSVF 140
Cdd:cd06852    1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 141 GLGAAVFLYLtaQTPVETTLILPLLKNIEIPLGIGFIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSG 220
Cdd:cd06852   81 AIVFALLLYY--FNGSGTLITLPFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 221 NVNFadyllipyipgageLIVFCGALIGAGLGFLWFNTYPAQVFMGDVGALALGAALGTIAVIVRQEVVLFIMGGVFVME 300
Cdd:cd06852  159 NAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIE 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 518172454 301 TLSVMIQVASFKLTGKRVFRMAPIHHHFELKGWPEPRVIVRFWIITVILVLVGLAT 356
Cdd:cd06852  225 ALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
24-343 7.40e-83

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: 253.51  E-value: 7.40e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  24 LRGILGVLTALVLSLWLGPWLIRTLQLRQIgqavrTDGPQTHLS-KSGTPTMGGALILSAIAISTLLWADLSNRYVWVVL 102
Cdd:COG0472    1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGL-----VDDPNERKShKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 103 AVTLLFGAIGWVDDYRkvieknsrGLPSRWKYFWQSVFGLGAAVFLYLTaqtpveTTLILPLLKniEIPLGIGFIVLTYF 182
Cdd:COG0472   76 LGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRI------TSLTIPFFG--LLDLGWLYIPLTVF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 183 VIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNvnfadyllipyipgaGELIVFCGALIGAGLGFLWFNTYPAQ 262
Cdd:COG0472  140 WIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALAGALLGFLWFNFPPAK 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 263 VFMGDVGALALGAALGTIAVIVRQE----VVLFIMGGVFVMETLSVMIQVasfKLTGKRVFR--MAPIHHHFELKGWPEP 336
Cdd:COG0472  205 IFMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQR---VLRGKRIFKadRAHLHHHLELLGWSER 281

                 ....*..
gi 518172454 337 RVIVRFW 343
Cdd:COG0472  282 QVVLRFW 288
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
70-268 1.51e-29

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: 112.01  E-value: 1.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  70 GTPTMGGALILSAIAISTLLWADLSNRYVWVVLAVTLLFGAIGWVDDYRKVieknSRGLPSRWKYFWQsvfgLGAAVFLY 149
Cdd:cd06499    1 PTPTMGGLAILLGFLLGVLLYIPHSNTLILLALLSGLVAGIVGFIDDLLGL----KVELSEREKLLLQ----ILAALFLL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 150 LTaqTPVETTLILPLLKNIEipLGIGFIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNVNFAdyll 229
Cdd:cd06499   73 LI--GGGHTTVTTPLGFVLD--LGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSA---- 144
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518172454 230 ipyipgageliVFCGALIGAGLGFLWFNTYPAQVFMGDV 268
Cdd:cd06499  145 -----------LLFIILAGACLGFLYFNFYPAKIFMGDT 172
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
71-267 2.23e-23

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: 97.17  E-value: 2.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  71 TPTMGGALILSAIAISTLLWADLS---NRYVWVVLAVTLLFGAIGWVDDYRkvieknsrGLPSRWKYFWQsvfgLGAAVF 147
Cdd:cd06853    8 IPRLGGLAIFLGFLLALLLALLFPfflLPELLGLLAGATIIVLLGLLDDLF--------DLSPKVKLLGQ----ILAALI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 148 LYLTAqtpVETTLILPLLKNIEIPLGIGFIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNVnfady 227
Cdd:cd06853   76 VVFGG---GVILSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQV----- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 518172454 228 llipyipgagELIVFCGALIGAGLGFLWFNTYPAQVFMGD 267
Cdd:cd06853  148 ----------LVALLALALAGALLGFLPYNFHPARIFMGD 177
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
99-268 1.89e-22

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 92.28  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454   99 WVVLAVTLLFGAIGWVDDYRkvieknsrGLPSRWKYFWQSVFGLGAAVFLYLTAqtpveTTLILPLLKNIEIPLGIGFIV 178
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILLVLGGIGL-----TSLGLPFGGGSLELGPWLSIL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  179 LTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNVnfadyllipyipgagELIVFCGALIGAGLGFLWFNT 258
Cdd:pfam00953  68 LTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNL---------------ELALLSLALLGALLGFLPFNF 132
                         170
                  ....*....|
gi 518172454  259 YPAQVFMGDV 268
Cdd:pfam00953 133 YPAKIFMGDS 142
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
71-268 1.97e-18

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: 83.45  E-value: 1.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  71 TPTMGGALILSAIAISTLLWA---DLSNRYVWVVLAVTLLFGAIGWVDDYRkvieknsrGLPSRWKYFWQSVFglgAAVF 147
Cdd:cd06854   15 TPRGGGIAFVLAFLLALLLAAaagPLNDLSYLLLLIGLLLLAAVGFIDDLR--------SLSPKIRLLVQLLA---AALA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 148 LYLTAQTPVETTLILPllknieiplGIGFIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGnvnfady 227
Cdd:cd06854   84 LYALGPLTSLLLNFLP---------PWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAG------- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 518172454 228 llipyipgAGELIVFCGALIGAGLGFLWFNTYPAQVFMGDV 268
Cdd:cd06854  148 --------EPALALLALALAGALLGFLPFNWPPAKIFMGDV 180
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
72-353 1.04e-15

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: 76.52  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  72 PTMGG-ALILSAIAISTLLWADLSNRYVWVVLAVTLLFGAIGWVDDYRkvieknsrGLPSRWKYFwqsVFGLGAAVFLYL 150
Cdd:cd06856   14 PEMGGiAVLLGFSLGLLFLSALTHSVEALALLITSLLAGLIGLLDDIL--------GLSQSEKVL---LTALPAIPLLVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 151 TAQTPVETTLILPLLKNIEIPlgigfIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNVNFADYLLI 230
Cdd:cd06856   83 KAGNPLTSLPIGGRVLGILYY-----LLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIALI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 231 pyipgagelivfcgaLIGAGLGFLWFNTYPAQVFMGDVGALALGAALGTIAVIVRQEVVLFIMGGVFVMETLsvMIQVAS 310
Cdd:cd06856  158 ---------------LVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVIDFL--LKLRSK 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 311 FKLTGKRVFR---------------MAPIHHHFELKGWP--EPRVIVRFWIITVILVLVG 353
Cdd:cd06856  221 GGGKEHREKPtkvledgtlypppdkSSLLTLRLLLRKGPmtEKEVVLVLWALEALLGILA 280
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
71-267 4.72e-10

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: 58.41  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  71 TPTMGG-ALILSAIAISTLLWADLSNRYVWVVLAVTLLFgAIGWVDDYRKVIEKNSRGLpsrwkyfwqsVFGLGAAVFLY 149
Cdd:cd06912   11 TPRIGGvAIFLGLLAGLLLLSLLSGSLLLLLLLAALPAF-LAGLLEDITKRVSPRIRLL----------ATFLSALLAVW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 150 LTAQTpvETTLILPLLKNIEIPLGIGfIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNVnfadyll 229
Cdd:cd06912   80 LLGAS--ITRLDLPGLDLLLSFPPFA-IIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDT------- 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 518172454 230 ipyipgagELIVFCGALIGAGLGFLWFNTYPAQVFMGD 267
Cdd:cd06912  150 --------DLAFLALLLAGALLGFLIFNFPFGKIFLGD 179
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
72-289 7.21e-06

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: 46.72  E-value: 7.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454  72 PTMGGALILSAIAISTLLWADLSNRY--------VWVVLAVTLLFGAIGWVDDYRKvieknsrglpsrWKYFWQSVFGLG 143
Cdd:cd06851   14 PEPGGISILIGFVASEITLIFFPFLSfphfpiseILAALITSVLGFSVGIIDDRLT------------MGGWFKPVALAF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518172454 144 AAVFLYLTAQtpVETTLILPLLkNIEIPLGIGFIVLTYFVIVGSSNAVNLTDGLDGLAIMPTVMVGGGLGIFCYLSGNvn 223
Cdd:cd06851   82 AAAPILLLGA--YDSNLDFPLF-GGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQN-- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518172454 224 fadyllipyipgaGELIVFCGALIGAGLGFLWFNTYPAQVFMGDVGALALGAALGTIAVIVRQEVV 289
Cdd:cd06851  157 -------------YEIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKI 209
 
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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