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Conserved domains on  [gi|1254710520|ref|WP_097349825|]
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glycosyltransferase family 4 protein [Listeria welshimeri]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10001440)

glycosyltransferase family 4 protein such as undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase, which catalyzes the formation of a phosphodiester bond between a decaprenyl- or undecaprenyl-phosphate molecule, respectively, and N-acetylglucosamine 1-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
3-289 1.36e-90

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: 272.77  E-value: 1.36e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520   3 WMIICICFGVSVLLTPLIRKIALYFDITDKPDQRRINIKPIPSLGGLAIFISFVIGMFLL-PIENEFLWPLLIAAFVMVL 81
Cdd:COG0472     4 LLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLaLLSNPELLLLLLGALLLGL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  82 TGLLDDIMEFKARYKLIGQILAAFIIVFWGnISIDFINLPFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVS 161
Cdd:COG0472    84 IGFLDDLLGLSARQKLLGQLLAALLLVLLL-LRITSLTIPFFGLLDLGWLYIPLTVFWIVGVSNAVNLTDGLDGLAAGVS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 162 TIALLTILGMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMGfkNVTFISLIVPILIL 241
Cdd:COG0472   163 LIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILG--RQEGASLLLLLLIL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1254710520 242 GVPISDTIFAIIRRMVTKQPIAMADKSHLHHCLLRLGFTHRQTVILIY 289
Cdd:COG0472   241 GVPVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRFW 288
 
Name Accession Description Interval E-value
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
3-289 1.36e-90

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: 272.77  E-value: 1.36e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520   3 WMIICICFGVSVLLTPLIRKIALYFDITDKPDQRRINIKPIPSLGGLAIFISFVIGMFLL-PIENEFLWPLLIAAFVMVL 81
Cdd:COG0472     4 LLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLaLLSNPELLLLLLGALLLGL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  82 TGLLDDIMEFKARYKLIGQILAAFIIVFWGnISIDFINLPFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVS 161
Cdd:COG0472    84 IGFLDDLLGLSARQKLLGQLLAALLLVLLL-LRITSLTIPFFGLLDLGWLYIPLTVFWIVGVSNAVNLTDGLDGLAAGVS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 162 TIALLTILGMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMGfkNVTFISLIVPILIL 241
Cdd:COG0472   163 LIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILG--RQEGASLLLLLLIL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1254710520 242 GVPISDTIFAIIRRMVTKQPIAMADKSHLHHCLLRLGFTHRQTVILIY 289
Cdd:COG0472   241 GVPVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRFW 288
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
36-279 1.33e-89

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: 268.97  E-value: 1.33e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  36 RRINIKPIPSLGGLAIFISFVIGMFLLPIENEF----LWPLLIAAFVMVLTGLLDDIMEFKARYKLIGQILAAFIIVFWG 111
Cdd:cd06853     1 RKVHKGPIPRLGGLAIFLGFLLALLLALLFPFFllpeLLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAALIVVFGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 112 NISIDFINLPFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGT 191
Cdd:cd06853    81 GVILSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLVALLALALAGAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 192 LGFLPYNFNPAKIFMGDTGALFLGFIISILSVMG-FKNVTFISLIVPILILGVPISDTIFAIIRRMVTKQPIAMADKSHL 270
Cdd:cd06853   161 LGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGtQKSSTAISPVVPLLILAVPLFDTLFVIIRRLLRGRSPFQADRDHL 240

                  ....*....
gi 1254710520 271 HHCLLRLGF 279
Cdd:cd06853   241 HHRLLRLGL 249
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
70-225 7.69e-35

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 125.02  E-value: 7.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  70 WPLLIAAFVMVLTGLLDDIMEFKARYKLIGQILAAFIIVFWGNISIDFINLPFGGEIH--FGVLSIPLTIIWIVAITNAI 147
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLelGPWLSILLTLFAIVGLTNAV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254710520 148 NLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMG 225
Cdd:pfam00953  81 NFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLAIIG 158
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
35-308 3.36e-21

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: 92.51  E-value: 3.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  35 QRRINIKPIPSLGGLAIFIS-FVIGMFLLPIENEFLWPLLIAAFVMVLTGLLDDIMEFK--------ARYKLIGQILAAF 105
Cdd:TIGR00445  27 KSHLKKKGTPTMGGIMIVFAiIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDDYRKIKrksnkgltAKQKLFGQIIIAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 106 IIVFWGNIS--IDFINLPFGGEIHF--GVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTI------------- 168
Cdd:TIGR00445 107 IFCTWLYYYgpDTFIYIPFIKDFMFdlGLFYILLAYFVLVGTSNAVNLTDGLDGLAIGPSAIAFGALailawatgnanfa 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 169 --LGMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMgfknvtFISLIVPILILGVPIS 246
Cdd:TIGR00445 187 kyLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGALGAVAIL------TKNEILLVIMGGVFVI 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1254710520 247 DTIFAIIR----RMVTKQPIAMADkshLHHCLLRLGFTHRQTVILIYAIAALFSLFAfiftMSTLW 308
Cdd:TIGR00445 261 ETLSVILQvgsyKTTKKRIFKMAP---IHHHFELKGWSEPRVVVRFWIISLLLALVA----LATLK 319
 
Name Accession Description Interval E-value
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
3-289 1.36e-90

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: 272.77  E-value: 1.36e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520   3 WMIICICFGVSVLLTPLIRKIALYFDITDKPDQRRINIKPIPSLGGLAIFISFVIGMFLL-PIENEFLWPLLIAAFVMVL 81
Cdd:COG0472     4 LLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLaLLSNPELLLLLLGALLLGL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  82 TGLLDDIMEFKARYKLIGQILAAFIIVFWGnISIDFINLPFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVS 161
Cdd:COG0472    84 IGFLDDLLGLSARQKLLGQLLAALLLVLLL-LRITSLTIPFFGLLDLGWLYIPLTVFWIVGVSNAVNLTDGLDGLAAGVS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 162 TIALLTILGMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMGfkNVTFISLIVPILIL 241
Cdd:COG0472   163 LIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILG--RQEGASLLLLLLIL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1254710520 242 GVPISDTIFAIIRRMVTKQPIAMADKSHLHHCLLRLGFTHRQTVILIY 289
Cdd:COG0472   241 GVPVVDTLSVILQRVLRGKRIFKADRAHLHHHLELLGWSERQVVLRFW 288
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
36-279 1.33e-89

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: 268.97  E-value: 1.33e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  36 RRINIKPIPSLGGLAIFISFVIGMFLLPIENEF----LWPLLIAAFVMVLTGLLDDIMEFKARYKLIGQILAAFIIVFWG 111
Cdd:cd06853     1 RKVHKGPIPRLGGLAIFLGFLLALLLALLFPFFllpeLLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAALIVVFGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 112 NISIDFINLPFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGT 191
Cdd:cd06853    81 GVILSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLVALLALALAGAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 192 LGFLPYNFNPAKIFMGDTGALFLGFIISILSVMG-FKNVTFISLIVPILILGVPISDTIFAIIRRMVTKQPIAMADKSHL 270
Cdd:cd06853   161 LGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGtQKSSTAISPVVPLLILAVPLFDTLFVIIRRLLRGRSPFQADRDHL 240

                  ....*....
gi 1254710520 271 HHCLLRLGF 279
Cdd:cd06853   241 HHRLLRLGL 249
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
29-284 1.44e-39

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: 140.46  E-value: 1.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  29 ITDKPDQRRINIKPIPSLGGLAIFISFVIGMFLL----PIENEFLWPLLIAAFVMVLTGLLDDIMEFKARYKLIGQILAA 104
Cdd:cd06854     1 LLDIPNERSSHTKPTPRGGGIAFVLAFLLALLLAaaagPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 105 FIIVFWGNISIDFINLPFGGeihfgVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIA 184
Cdd:cd06854    81 ALALYALGPLTSLLLNFLPP-----WLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAGEPALALLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 185 SVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMGFKNVtfISLIVPILILGVPISDTIFAIIRRMVTKQPIAM 264
Cdd:cd06854   156 LALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSG--QSPWAWLLLLSPFLVDATVTLLRRLLRGENIFQ 233
                         250       260
                  ....*....|....*....|
gi 1254710520 265 ADKSHLHHCLLRLGFTHRQT 284
Cdd:cd06854   234 AHRKHLYQRLARAGKSHRKV 253
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
41-301 2.69e-39

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: 140.32  E-value: 2.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  41 KPIPSLGGLAIFISFVIGMFLL-PIENEFLWPLLIAAFVMVLTGLLDDIME--------FKARYKLIGQILAAFIIVFW- 110
Cdd:cd06852     9 AGTPTMGGILFILAILISTLLWaDLDSPEVLLLLLLTLGFGLIGFLDDYLKvvkkrnlgLSARQKLLLQFLIAIVFALLl 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 111 ---GNISIDFINLPF-GGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASV 186
Cdd:cd06852    89 yyfNGSGTLITLPFFkNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAGNAVFLAVFCA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 187 LIAG-TLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMgfkNVTFISLivpILILGVPISDTIFAIIR----RMVTKQP 261
Cdd:cd06852   169 ALVGaCLGFLWFNAYPAKVFMGDTGSLALGGALAALAIL---TKQELLL---LIIGGVFVIEALSVILQvgsfKLTGKRI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1254710520 262 IAMADkshLHHCLLRLGFTHRQTVILIYAIAALFSLFAFI 301
Cdd:cd06852   243 FKMAP---LHHHFELKGWSETKVVVRFWIISLILALIGLL 279
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
70-225 7.69e-35

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 125.02  E-value: 7.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  70 WPLLIAAFVMVLTGLLDDIMEFKARYKLIGQILAAFIIVFWGNISIDFINLPFGGEIH--FGVLSIPLTIIWIVAITNAI 147
Cdd:pfam00953   1 LGLLLGALLIGLIGLIDDLLGLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLelGPWLSILLTLFAIVGLTNAV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1254710520 148 NLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMG 225
Cdd:pfam00953  81 NFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLAIIG 158
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
42-216 7.07e-33

Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases. They catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate, which is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. One member, D-N-acetylhexosamine 1-phosphate transferase (GPT) is a eukaryotic enzyme, which is specific for UDP-GlcNAc as donor substrate and dolichol-phosphate as the membrane bound acceptor. The bacterial members MraY, WecA, and WbpL/WbcO utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic endproducts implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The eukaryotic reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for N-glycosylation. The prokaryotic reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly. Archaeal and eukaryotic enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme. Archaea possess the same N-glycosylation pathway as eukaryotes. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene.


Pssm-ID: 133460  Cd Length: 185  Bit Score: 120.87  E-value: 7.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  42 PIPSLGGLAIFISFVIGMFLL-PIENEFLWPLLIAAFVMVLTGLLDDIMEFK----ARYKLIGQILAAFIIVFWGNISId 116
Cdd:cd06499     1 PTPTMGGLAILLGFLLGVLLYiPHSNTLILLALLSGLVAGIVGFIDDLLGLKvelsEREKLLLQILAALFLLLIGGGHT- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 117 FINLPFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGTLGFLP 196
Cdd:cd06499    80 TVTTPLGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLFIILAGACLGFLY 159
                         170       180
                  ....*....|....*....|
gi 1254710520 197 YNFNPAKIFMGDTGALFLGF 216
Cdd:cd06499   160 FNFYPAKIFMGDTGSYFLGA 179
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
41-222 3.31e-31

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: 116.57  E-value: 3.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  41 KPIPSLGGLAIFISFVIGMFLLPIENEFLWPLLIAAFVMV-LTGLLDDIME-FKARYKLIGQILAAFIIVFWGNISIDFI 118
Cdd:cd06912     9 RPTPRIGGVAIFLGLLAGLLLLSLLSGSLLLLLLLAALPAfLAGLLEDITKrVSPRIRLLATFLSALLAVWLLGASITRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 119 NLPF-GGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGTLGFLPY 197
Cdd:cd06912    89 DLPGlDLLLSFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDTDLAFLALLLAGALLGFLIF 168
                         170       180
                  ....*....|....*....|....*
gi 1254710520 198 NFNPAKIFMGDTGALFLGFIISILS 222
Cdd:cd06912   169 NFPFGKIFLGDGGAYLLGFLLAWLA 193
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
43-240 5.29e-24

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: 99.63  E-value: 5.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  43 IPSLGGLAIFISFVIGMFLLPI--ENEFLWPLLIAAFVMVLTGLLDDIMEFKARYKLIGQILAAFIIVfWGNISIDFINL 120
Cdd:cd06856    13 VPEMGGIAVLLGFSLGLLFLSAltHSVEALALLITSLLAGLIGLLDDILGLSQSEKVLLTALPAIPLL-VLKAGNPLTSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 121 PFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGTLGFLPYNFN 200
Cdd:cd06856    92 PIGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIALILVAALLAFLLYNKY 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1254710520 201 PAKIFMGDTGALFLGFIISILSVMGFKNVTFISLIVPILI 240
Cdd:cd06856   172 PAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVI 211
mraY TIGR00445
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ...
35-308 3.36e-21

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: 92.51  E-value: 3.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  35 QRRINIKPIPSLGGLAIFIS-FVIGMFLLPIENEFLWPLLIAAFVMVLTGLLDDIMEFK--------ARYKLIGQILAAF 105
Cdd:TIGR00445  27 KSHLKKKGTPTMGGIMIVFAiIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDDYRKIKrksnkgltAKQKLFGQIIIAL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 106 IIVFWGNIS--IDFINLPFGGEIHF--GVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTI------------- 168
Cdd:TIGR00445 107 IFCTWLYYYgpDTFIYIPFIKDFMFdlGLFYILLAYFVLVGTSNAVNLTDGLDGLAIGPSAIAFGALailawatgnanfa 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 169 --LGMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMgfknvtFISLIVPILILGVPIS 246
Cdd:TIGR00445 187 kyLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGALGAVAIL------TKNEILLVIMGGVFVI 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1254710520 247 DTIFAIIR----RMVTKQPIAMADkshLHHCLLRLGFTHRQTVILIYAIAALFSLFAfiftMSTLW 308
Cdd:TIGR00445 261 ETLSVILQvgsyKTTKKRIFKMAP---IHHHFELKGWSEPRVVVRFWIISLLLALVA----LATLK 319
GT_GPT_like cd06851
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ...
42-240 9.53e-17

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: 78.31  E-value: 9.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  42 PIPSLGGLAIFISFVIGMFLLPIENEFLWP---------LLIAAFVMVLTGLLDDIMEFKARYKLIGQILAAFIIVFWGN 112
Cdd:cd06851    12 MIPEPGGISILIGFVASEITLIFFPFLSFPhfpiseilaALITSVLGFSVGIIDDRLTMGGWFKPVALAFAAAPILLLGA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 113 ISIDFINLPFGGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTILGMAFIMGDALVIMIASVLIAGTL 192
Cdd:cd06851    92 YDSNLDFPLFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQNYEIGIACLCLAFASL 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1254710520 193 GFLPYNFNPAKIFMGDTGALFLGFIISILSVMGFKNVTFISLIVPILI 240
Cdd:cd06851   172 AFLYYNKYPSRIFPGDTGAYMFGATYAVVAILGEVEKIAAVAFIPAII 219
GT_GPT_euk cd06855
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ...
34-240 2.23e-13

UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from UDP-GlcNAc to dolichol-P to form GlcNAc-P-P-dolichol. The reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for eukaryotic N-glycosylation. GPT activity has been identified in all eukaryotic cells examined to date. A series of six conserved motifs designated A through F, ranging in length from 5 to 13 amino acid residues, has been identified in this family. They have been determined to be important for stable expression, substrate binding, or catalytic activities.


Pssm-ID: 133465  Cd Length: 283  Bit Score: 69.58  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520  34 DQRRINIKPIPSLGGLAIFISFVIGMFLLPIENEF----------LWPLLIAAFVMVLTGLLDDIMEFKARYKLIGQILA 103
Cdd:cd06855    17 DLNKNGEEKIPESAGLVPGIVFLIVLFLFIPFPFLkdfphdklveYLSALLSICCMTFLGFADDVLDLRWRHKLILPTFA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254710520 104 A--FIIVFWGNISIDFINLPF----GGEIHFGVLSIPLTIIWIVAITNAINLIDGLDGLAAGVSTIALLTIL-------- 169
Cdd:cd06855    97 SlpLLMVYYGNTGITLPIVPLrpllGTLIDLGILYYVYMILLAVFCTNSINIYAGINGLEVGQSLVIALSILlynlleln 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1254710520 170 ---GMAFIMGDALVIMIASVLIAGTLGFLPYNFNPAKIFMGDTGALFLGFIISILSVMGFKNVTFISLIVPILI 240
Cdd:cd06855   177 gssGSMTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMVFAVVGILGHFSKTLLLFFIPQII 250
 
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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