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Conserved domains on  [gi|1624566919|ref|WP_136409962|]
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glycosyltransferase family 4 protein [Muribaculum gordoncarteri]

Protein Classification

MraY family glycosyltransferase( domain architecture ID 10160628)

MraY family glycosyltransferase similar to Pseudomonas aeruginosa WbpL, a bifunctional enzyme which could initiate both B-band synthesis through the addition of QuiNAc to undecaprenol phosphate, and A-band synthesis by transferring either a GalNAc or a GlcNAc residue

CAZY:  GT4
EC:  2.-.-.-
Gene Ontology:  GO:0016780|GO:0046872|GO:0009252
PubMed:  7734839|11024259
SCOP:  3002333

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
26-265 1.22e-68

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: 214.80  E-value: 1.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  26 IIDKPNLRSSHTTITLRGGGIVF-------YFGAMAYFIVSHGAYPWFMLGLTMIAAVSFVDDLHSMPNRIRLMIQFIAM 98
Cdd:cd06854     1 LLDIPNERSSHTKPTPRGGGIAFvlafllaLLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  99 LLMFHQLGFLTLE------SWWISIAALIVCTGIINAYNFMDGINGITGAYSIAILIPLAIVN-SHIGFIDRSMIYIIGI 171
Cdd:cd06854    81 ALALYALGPLTSLllnflpPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGyLAGEPALALLALALAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 172 SVLVFCIFNFRkRARCFAGDVGSVSIAFILLFMLGALIMATGQVW-YLIFFAVYGVDSVLTIIHRLMLHENIFKPHRKHA 250
Cdd:cd06854   161 ALLGFLPFNWP-PAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWaWLLLLSPFLVDATVTLLRRLLRGENIFQAHRKHL 239
                         250
                  ....*....|....*
gi 1624566919 251 YQIMANElGMPHTLV 265
Cdd:cd06854   240 YQRLARA-GKSHRKV 253
 
Name Accession Description Interval E-value
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
26-265 1.22e-68

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: 214.80  E-value: 1.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  26 IIDKPNLRSSHTTITLRGGGIVF-------YFGAMAYFIVSHGAYPWFMLGLTMIAAVSFVDDLHSMPNRIRLMIQFIAM 98
Cdd:cd06854     1 LLDIPNERSSHTKPTPRGGGIAFvlafllaLLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  99 LLMFHQLGFLTLE------SWWISIAALIVCTGIINAYNFMDGINGITGAYSIAILIPLAIVN-SHIGFIDRSMIYIIGI 171
Cdd:cd06854    81 ALALYALGPLTSLllnflpPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGyLAGEPALALLALALAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 172 SVLVFCIFNFRkRARCFAGDVGSVSIAFILLFMLGALIMATGQVW-YLIFFAVYGVDSVLTIIHRLMLHENIFKPHRKHA 250
Cdd:cd06854   161 ALLGFLPFNWP-PAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWaWLLLLSPFLVDATVTLLRRLLRGENIFQAHRKHL 239
                         250
                  ....*....|....*
gi 1624566919 251 YQIMANElGMPHTLV 265
Cdd:cd06854   240 YQRLARA-GKSHRKV 253
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
1-269 3.28e-45

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: 155.29  E-value: 3.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919   1 MTYLIISVILMAAELAYFKLADRFNIIDKPNLRSSHTTITLRGGGIVFYFGAMAYFIVSHG----AYPWFMLGLTMIAAV 76
Cdd:COG0472     5 LAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALlsnpELLLLLLGALLLGLI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  77 SFVDDLHSMPNRIRLMIQFIAMLLMFHQLGFLT---------LESWWISIA-ALIVCTGIINAYNFMDGINGITGAYSIA 146
Cdd:COG0472    85 GFLDDLLGLSARQKLLGQLLAALLLVLLLLRITsltipffglLDLGWLYIPlTVFWIVGVSNAVNLTDGLDGLAAGVSLI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 147 ILIPLAIVNSHIGFIDRSMIYIIGI-SVLVFCIFNFrKRARCFAGDVGSVSIAFILLFMLGALIMATGQVWY-LIFFAVY 224
Cdd:COG0472   165 AALALAIIAYLAGQGELALLAAALAgALLGFLWFNF-PPAKIFMGDTGSLFLGFALAALAILGRQEGASLLLlLLILGVP 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1624566919 225 GVDSVLTIIHRLMLHENIFKPHRKHAYQIMANeLGMPHTLVSTIY 269
Cdd:COG0472   244 VVDTLSVILQRVLRGKRIFKADRAHLHHHLEL-LGWSERQVVLRF 287
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
68-201 5.52e-15

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 71.09  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  68 LGLTMIAAVSFVDDLHSMPNRIRLMIQFIAMLLM-------------FHQLGFLTLESWWISIAALIVCTGIINAYNFMD 134
Cdd:pfam00953   5 LGALLIGLIGLIDDLLGLSARIKLLLQALAALILlvlggigltslglPFGGGSLELGPWLSILLTLFAIVGLTNAVNFID 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566919 135 GINGITGAYSIAILIPLAIVNSHIGFID-RSMIYIIGISVLVFCIFNFRkRARCFAGDVGSVSIAFIL 201
Cdd:pfam00953  85 GLDGLAGGVAIIAALALGIIAYLLGNLElALLSLALLGALLGFLPFNFY-PAKIFMGDSGSLFLGFLL 151
 
Name Accession Description Interval E-value
GT_WbpL_WbcO_like cd06854
The members of this subfamily catalyze the formation of a phosphodiester bond between a ...
26-265 1.22e-68

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: 214.80  E-value: 1.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  26 IIDKPNLRSSHTTITLRGGGIVF-------YFGAMAYFIVSHGAYPWFMLGLTMIAAVSFVDDLHSMPNRIRLMIQFIAM 98
Cdd:cd06854     1 LLDIPNERSSHTKPTPRGGGIAFvlafllaLLLAAAAGPLNDLSYLLLLIGLLLLAAVGFIDDLRSLSPKIRLLVQLLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  99 LLMFHQLGFLTLE------SWWISIAALIVCTGIINAYNFMDGINGITGAYSIAILIPLAIVN-SHIGFIDRSMIYIIGI 171
Cdd:cd06854    81 ALALYALGPLTSLllnflpPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGyLAGEPALALLALALAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 172 SVLVFCIFNFRkRARCFAGDVGSVSIAFILLFMLGALIMATGQVW-YLIFFAVYGVDSVLTIIHRLMLHENIFKPHRKHA 250
Cdd:cd06854   161 ALLGFLPFNWP-PAKIFMGDVGSTFLGFLLAALLLLLALSGQSPWaWLLLLSPFLVDATVTLLRRLLRGENIFQAHRKHL 239
                         250
                  ....*....|....*
gi 1624566919 251 YQIMANElGMPHTLV 265
Cdd:cd06854   240 YQRLARA-GKSHRKV 253
Rfe COG0472
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ...
1-269 3.28e-45

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: 155.29  E-value: 3.28e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919   1 MTYLIISVILMAAELAYFKLADRFNIIDKPNLRSSHTTITLRGGGIVFYFGAMAYFIVSHG----AYPWFMLGLTMIAAV 76
Cdd:COG0472     5 LAFLLAFLLSLLLTPLLIRLARRLGLVDDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALlsnpELLLLLLGALLLGLI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  77 SFVDDLHSMPNRIRLMIQFIAMLLMFHQLGFLT---------LESWWISIA-ALIVCTGIINAYNFMDGINGITGAYSIA 146
Cdd:COG0472    85 GFLDDLLGLSARQKLLGQLLAALLLVLLLLRITsltipffglLDLGWLYIPlTVFWIVGVSNAVNLTDGLDGLAAGVSLI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 147 ILIPLAIVNSHIGFIDRSMIYIIGI-SVLVFCIFNFrKRARCFAGDVGSVSIAFILLFMLGALIMATGQVWY-LIFFAVY 224
Cdd:COG0472   165 AALALAIIAYLAGQGELALLAAALAgALLGFLWFNF-PPAKIFMGDTGSLFLGFALAALAILGRQEGASLLLlLLILGVP 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1624566919 225 GVDSVLTIIHRLMLHENIFKPHRKHAYQIMANeLGMPHTLVSTIY 269
Cdd:COG0472   244 VVDTLSVILQRVLRGKRIFKADRAHLHHHLEL-LGWSERQVVLRF 287
GT_WecA_like cd06853
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ...
33-254 3.79e-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: 96.02  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  33 RSSHTTITLRGGGIVFYFG-------AMAYFIVSHGAYPWFMLGLTMIAAVSFVDDLHSMPNRIRLMIQFIAMLLM---- 101
Cdd:cd06853     1 RKVHKGPIPRLGGLAIFLGfllalllALLFPFFLLPELLGLLAGATIIVLLGLLDDLFDLSPKVKLLGQILAALIVvfgg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 102 ------FHQLGFLTLESWWISIAALIVCT-GIINAYNFMDGINGITGAYSIAILIPLAIVNSHIGFIDRSMI-YIIGISV 173
Cdd:cd06853    81 gvilslLGPFGGGIILLGWLSIPLTVLWIvGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLVALLaLALAGAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 174 LVFCIFNFRKrARCFAGDVGSVSIAFILLFMLGALIMATGQVWYLIF-FAVYGV---DSVLTIIHRLMLHENIFKPHRKH 249
Cdd:cd06853   161 LGFLPYNFHP-ARIFMGDAGSLFLGFLLAVLSILGTQKSSTAISPVVpLLILAVplfDTLFVIIRRLLRGRSPFQADRDH 239

                  ....*
gi 1624566919 250 AYQIM 254
Cdd:cd06853   240 LHHRL 244
Glycos_transf_4 pfam00953
Glycosyl transferase family 4;
68-201 5.52e-15

Glycosyl transferase family 4;


Pssm-ID: 460008  Cd Length: 158  Bit Score: 71.09  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  68 LGLTMIAAVSFVDDLHSMPNRIRLMIQFIAMLLM-------------FHQLGFLTLESWWISIAALIVCTGIINAYNFMD 134
Cdd:pfam00953   5 LGALLIGLIGLIDDLLGLSARIKLLLQALAALILlvlggigltslglPFGGGSLELGPWLSILLTLFAIVGLTNAVNFID 84
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624566919 135 GINGITGAYSIAILIPLAIVNSHIGFID-RSMIYIIGISVLVFCIFNFRkRARCFAGDVGSVSIAFIL 201
Cdd:pfam00953  85 GLDGLAGGVAIIAALALGIIAYLLGNLElALLSLALLGALLGFLPFNFY-PAKIFMGDSGSLFLGFLL 151
GT_MraY_like cd06912
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ...
30-205 1.59e-11

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: 62.26  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  30 PNLRSSHTTITLRGGGIVFYFGAMAYFIVSHGA----YPWFMLGLTMIAAVSFVDDLHSMPN-RIRLMIQFIAMLLMFHQ 104
Cdd:cd06912     1 DGIQKFHTRPTPRIGGVAIFLGLLAGLLLLSLLsgslLLLLLLAALPAFLAGLLEDITKRVSpRIRLLATFLSALLAVWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 105 LGF-----------LTLESWWISIA-ALIVCTGIINAYNFMDGINGITGAYSIAILIPLAIVNSHIGFIDRSMIYIIGI- 171
Cdd:cd06912    81 LGAsitrldlpgldLLLSFPPFAIIfTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDTDLAFLALLLAg 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1624566919 172 SVLVFCIFNFrKRARCFAGDVGSVSIAFILLFML 205
Cdd:cd06912   161 ALLGFLIFNF-PFGKIFLGDGGAYLLGFLLAWLA 193
GT_MraY cd06852
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ...
40-233 1.88e-08

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: 54.42  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  40 TLRGGGIVFYFGAMAYFIVSHG---AYPWFMLGLTMI-AAVSFVDDL--------HSMPNRIRLMIQFI----AMLLMFH 103
Cdd:cd06852    11 TPTMGGILFILAILISTLLWADldsPEVLLLLLLTLGfGLIGFLDDYlkvvkkrnLGLSARQKLLLQFLiaivFALLLYY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 104 QLG------------FLTLESWWISIAALIVCTGIINAYNFMDGINGITGAYSIAILIPLAIVNSHIGFIDRSMIYIIGI 171
Cdd:cd06852    91 FNGsgtlitlpffknGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAGNAVFLAVFCAAL 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624566919 172 --SVLVFCIFNfRKRARCFAGDVGSVSIAfillFMLGALIMATGQVWYLIFFA-VYGVDSVLTII 233
Cdd:cd06852   171 vgACLGFLWFN-AYPAKVFMGDTGSLALG----GALAALAILTKQELLLLIIGgVFVIEALSVIL 230
GT_GPT_archaea cd06856
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ...
42-197 8.48e-08

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: 52.64  E-value: 8.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  42 RGGGIVFYFGAMA-----YFIVSHGAYPWFMLGLTMIAAVSFVDDLHSMPNRIRLMIQ-FIAMLLMFHQLGFLTLESWWI 115
Cdd:cd06856    15 EMGGIAVLLGFSLgllflSALTHSVEALALLITSLLAGLIGLLDDILGLSQSEKVLLTaLPAIPLLVLKAGNPLTSLPIG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 116 SIAALIVCTGII---------NAYNFMDGINGITGAYSIAILIPLAIVNSHIGFIDRSMIYIIGISVLV-FCIFNfRKRA 185
Cdd:cd06856    95 GRVLGILYYLLIvplgitgasNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDALIIALILVAALLaFLLYN-KYPA 173
                         170
                  ....*....|..
gi 1624566919 186 RCFAGDVGSVSI 197
Cdd:cd06856   174 KVFPGDVGTLPI 185
GT_MraY-like cd06499
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ...
40-213 1.63e-05

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: 44.60  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919  40 TLRGGGIVFYFG---AMAYFIVSHGAYPWFML-GLTMIAAVSFVDDL----HSMPNRIRLMIQF-IAMLLMF-------- 102
Cdd:cd06499     2 TPTMGGLAILLGfllGVLLYIPHSNTLILLALlSGLVAGIVGFIDDLlglkVELSEREKLLLQIlAALFLLLiggghttv 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624566919 103 -HQLGFLTLESWWISIAALIVCTGIINAYNFMDGINGITGAYSIAILIPLAIVNSHIGFIDRSMIYIIGI-SVLVFCIFN 180
Cdd:cd06499    82 tTPLGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLFIILAgACLGFLYFN 161
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1624566919 181 FRKrARCFAGDVGSvsiafillFMLGALIMATG 213
Cdd:cd06499   162 FYP-AKIFMGDTGS--------YFLGAAYAAVA 185
 
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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