|
Name |
Accession |
Description |
Interval |
E-value |
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
37-360 |
3.34e-177 |
|
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: 494.66 E-value: 3.34e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 37 SLWMGPRMIARLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGIIGFVDD 116
Cdd:TIGR00445 1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 117 YRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLAGKDTpatELVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDG 196
Cdd:TIGR00445 81 YRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDT---FIYIPFIKDFMFDLGLFYILLAYFVLVGTSNAVNLTDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 197 LDGLAIMPTVFVAAGFALVAWATGNMNFANYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGA 276
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 277 LGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLAT 356
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALAT 317
|
....
gi 1170956473 357 LKVR 360
Cdd:TIGR00445 318 LKVR 321
|
|
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
61-356 |
3.22e-137 |
|
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: 391.47 E-value: 3.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 61 GPESHFSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGIIGFVDDYRKVVRKDTKGLIARWKYFWMSVI 140
Cdd:cd06852 1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 141 ALGVAFALYLAGKDTpaTELVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATG 220
Cdd:cd06852 81 AIVFALLLYYFNGSG--TLITLPFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 221 NMNFanylhipylrhageLVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVE 300
Cdd:cd06852 159 NAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIE 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1170956473 301 TLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLAT 356
Cdd:cd06852 225 ALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
24-343 |
3.14e-91 |
|
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: 275.08 E-value: 3.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 24 FRAIVSLLTALFISLWMGPRMIARLQKLSFGQVVRndgpESHFSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLT 103
Cdd:COG0472 1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPN----ERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 104 VLIGYGIIGFVDDYRkvvrkdtkGLIARWKYFWMSVIALGVAFALYLAgkdtpaTELVVPFFKDVmpQLGLFYILLAYFV 183
Cdd:COG0472 77 GALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRI------TSLTIPFFGLL--DLGWLYIPLTVFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 184 IVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNmnfanylhipylrhaGELVIVCTAIVGAGLGFLWFNTYPAQV 263
Cdd:COG0472 141 IVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALAGALLGFLWFNFPPAKI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 264 FMGDVGSLALGGALGIIAVLLRQE----FLLVIMGGVFVVETLSVILQVgsfKLRGQRIFR--MAPIHHHYELKGWPEPR 337
Cdd:COG0472 206 FMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQR---VLRGKRIFKadRAHLHHHLELLGWSERQ 282
|
....*.
gi 1170956473 338 VIVRFW 343
Cdd:COG0472 283 VVLRFW 288
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
99-284 |
1.58e-28 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 108.46 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 99 WCVLTVLIGYGIIGFVDDYrkvvrkdtKGLIARWKYFWMSVIALGVAFALYLAgkdtpATELVVPFFKDVMPQLGLFYIL 178
Cdd:pfam00953 1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGGIG-----LTSLGLPFGGGSLELGPWLSIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 179 LAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNMnfanylhipylrhagELVIVCTAIVGAGLGFLWFNT 258
Cdd:pfam00953 68 LTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNL---------------ELALLSLALLGALLGFLPFNF 132
|
170 180
....*....|....*....|....*.
gi 1170956473 259 YPAQVFMGDVGSLALGGALGIIAVLL 284
Cdd:pfam00953 133 YPAKIFMGDSGSLFLGFLLAVLAIIG 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
37-360 |
3.34e-177 |
|
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: 494.66 E-value: 3.34e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 37 SLWMGPRMIARLQKLSFGQVVRNDGPESHFSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGIIGFVDD 116
Cdd:TIGR00445 1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 117 YRKVVRKDTKGLIARWKYFWMSVIALGVAFALYLAGKDTpatELVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDG 196
Cdd:TIGR00445 81 YRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDT---FIYIPFIKDFMFDLGLFYILLAYFVLVGTSNAVNLTDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 197 LDGLAIMPTVFVAAGFALVAWATGNMNFANYLHIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGA 276
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 277 LGIIAVLLRQEFLLVIMGGVFVVETLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLAT 356
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALAT 317
|
....
gi 1170956473 357 LKVR 360
Cdd:TIGR00445 318 LKVR 321
|
|
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
61-356 |
3.22e-137 |
|
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: 391.47 E-value: 3.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 61 GPESHFSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGIIGFVDDYRKVVRKDTKGLIARWKYFWMSVI 140
Cdd:cd06852 1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 141 ALGVAFALYLAGKDTpaTELVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATG 220
Cdd:cd06852 81 AIVFALLLYYFNGSG--TLITLPFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 221 NMNFanylhipylrhageLVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVE 300
Cdd:cd06852 159 NAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIE 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1170956473 301 TLSVILQVGSFKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISLMLVLIGLAT 356
Cdd:cd06852 225 ALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
24-343 |
3.14e-91 |
|
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: 275.08 E-value: 3.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 24 FRAIVSLLTALFISLWMGPRMIARLQKLSFGQVVRndgpESHFSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLT 103
Cdd:COG0472 1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPN----ERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 104 VLIGYGIIGFVDDYRkvvrkdtkGLIARWKYFWMSVIALGVAFALYLAgkdtpaTELVVPFFKDVmpQLGLFYILLAYFV 183
Cdd:COG0472 77 GALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLRI------TSLTIPFFGLL--DLGWLYIPLTVFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 184 IVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNmnfanylhipylrhaGELVIVCTAIVGAGLGFLWFNTYPAQV 263
Cdd:COG0472 141 IVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALAGALLGFLWFNFPPAKI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 264 FMGDVGSLALGGALGIIAVLLRQE----FLLVIMGGVFVVETLSVILQVgsfKLRGQRIFR--MAPIHHHYELKGWPEPR 337
Cdd:COG0472 206 FMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQR---VLRGKRIFKadRAHLHHHLELLGWSERQ 282
|
....*.
gi 1170956473 338 VIVRFW 343
Cdd:COG0472 283 VVLRFW 288
|
|
| GT_MraY-like |
cd06499 |
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ... |
70-281 |
5.76e-31 |
|
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine:polyprenol phosphate D-N-acetylhexosamine-1-phosphate transferases. They catalyze the transfer of a D-N-acetylhexosamine 1-phosphate to a membrane-bound polyprenol phosphate, which is the initiation step of protein N-glycosylation in eukaryotes and peptidoglycan biosynthesis in bacteria. One member, D-N-acetylhexosamine 1-phosphate transferase (GPT) is a eukaryotic enzyme, which is specific for UDP-GlcNAc as donor substrate and dolichol-phosphate as the membrane bound acceptor. The bacterial members MraY, WecA, and WbpL/WbcO utilize undecaprenol phosphate as the acceptor substrate, but use different UDP-sugar donor substrates. MraY-type transferases are highly specific for UDP-N-acetylmuramate-pentapeptide, whereas WecA proteins are selective for UDP-N-acetylglucosamine (UDP-GlcNAc). The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic endproducts implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The eukaryotic reaction is the first step in the assembly of dolichol-linked oligosaccharide intermediates and is essential for N-glycosylation. The prokaryotic reactions lead to the formation of polyprenol-linked oligosaccharides involved in bacterial cell wall and peptidoglycan assembly. Archaeal and eukaryotic enzymes may use the same substrates and are evolutionarily closer than the bacterial enzyme. Archaea possess the same N-glycosylation pathway as eukaryotes. A glycosyl transferase gene Mv1751 in M. voltae encodes for the enzyme that carries out the first step in the pathway, the attachment of GlcNAc to a dolichol lipid carrier in the membrane. A lethal mutation in the alg7 (GPT) gene in Saccharomyces cerevisiae was successfully complemented with Mv1751, the archaea gene.
Pssm-ID: 133460 Cd Length: 185 Bit Score: 115.86 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 70 GTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGIIGFVDDYRKVvrkdTKGLIARWKYFWMSVIALgvaFALY 149
Cdd:cd06499 1 PTPTMGGLAILLGFLLGVLLYIPHSNTLILLALLSGLVAGIVGFIDDLLGL----KVELSEREKLLLQILAAL---FLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 150 LagkdTPATELVVPFFkDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNMNFAnylh 229
Cdd:cd06499 74 I----GGGHTTVTTPL-GFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSA---- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1170956473 230 ipylrhagelvIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIA 281
Cdd:cd06499 145 -----------LLFIILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
99-284 |
1.58e-28 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 108.46 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 99 WCVLTVLIGYGIIGFVDDYrkvvrkdtKGLIARWKYFWMSVIALGVAFALYLAgkdtpATELVVPFFKDVMPQLGLFYIL 178
Cdd:pfam00953 1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGGIG-----LTSLGLPFGGGSLELGPWLSIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 179 LAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNMnfanylhipylrhagELVIVCTAIVGAGLGFLWFNT 258
Cdd:pfam00953 68 LTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNL---------------ELALLSLALLGALLGFLPFNF 132
|
170 180
....*....|....*....|....*.
gi 1170956473 259 YPAQVFMGDVGSLALGGALGIIAVLL 284
Cdd:pfam00953 133 YPAKIFMGDSGSLFLGFLLAVLAIIG 158
|
|
| GT_WecA_like |
cd06853 |
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ... |
68-320 |
1.48e-26 |
|
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: 106.03 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 68 KRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGII---GFVDDYrkvvrkdtKGLIARWKYFWMSVIALGV 144
Cdd:cd06853 5 KGPIPRLGGLAIFLGFLLALLLALLFPFFLLPELLGLLAGATIIvllGLLDDL--------FDLSPKVKLLGQILAALIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 145 AFALYLAgkdtpatELVVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNMnf 224
Cdd:cd06853 77 VFGGGVI-------LSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQV-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 225 anylhipylrhagELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQE-------FLLVIMGGVF 297
Cdd:cd06853 148 -------------LVALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQKsstaispVVPLLILAVP 214
|
250 260
....*....|....*....|...
gi 1170956473 298 VVETLSVILqvgSFKLRGQRIFR 320
Cdd:cd06853 215 LFDTLFVII---RRLLRGRSPFQ 234
|
|
| GT_WbpL_WbcO_like |
cd06854 |
The members of this subfamily catalyze the formation of a phosphodiester bond between a ... |
71-319 |
2.89e-25 |
|
The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments.
Pssm-ID: 133464 Cd Length: 253 Bit Score: 102.32 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 71 TPTMGGIMILTAITVSVLLWAYP---SNPYVWCVLTVLIGYGIIGFVDDYRkvvrkdtkGLIARWKYFwmsVIALGVAFA 147
Cdd:cd06854 15 TPRGGGIAFVLAFLLALLLAAAAgplNDLSYLLLLIGLLLLAAVGFIDDLR--------SLSPKIRLL---VQLLAAALA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 148 LYLAGkdtpatelvVPFFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGnmnfany 227
Cdd:cd06854 84 LYALG---------PLTSLLLNFLPPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAG------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 228 lhipylrhAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLL-----RQEFLLVIMGGVFVVETL 302
Cdd:cd06854 148 --------EPALALLALALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLalsgqSPWAWLLLLSPFLVDATV 219
|
250
....*....|....*..
gi 1170956473 303 SVILQVgsfkLRGQRIF 319
Cdd:cd06854 220 TLLRRL----LRGENIF 232
|
|
| GT_GPT_archaea |
cd06856 |
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ... |
68-317 |
1.04e-21 |
|
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: 93.47 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 68 KRGTPTMGGIMILTAITVS--VLLWAYPSNPYVWCVLTVLIGyGIIGFVDDYRKVVRKDtkgliarwKYFWMSVIALGVA 145
Cdd:cd06856 10 KPEVPEMGGIAVLLGFSLGllFLSALTHSVEALALLITSLLA-GLIGLLDDILGLSQSE--------KVLLTALPAIPLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 146 FalYLAGKDTPATELVVPFFkdvmpqLGLFYILLAYFVIVGTGNAVNLTDGLDGLaiMPTVFVAAGFALVAwatgnmnfa 225
Cdd:cd06856 81 V--LKAGNPLTSLPIGGRVL------GILYYLLIVPLGITGASNAFNMLAGFNGL--EAGMGIIILLALAI--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 226 nylhIPYLRHAGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVLLRQEFLLVIMGGVFVVETLSVI 305
Cdd:cd06856 142 ----ILLINGDYDALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVIDFLLKL 217
|
250
....*....|..
gi 1170956473 306 LQVGSFKLRGQR 317
Cdd:cd06856 218 RSKGGGKEHREK 229
|
|
| GT_MraY_like |
cd06912 |
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ... |
66-281 |
5.96e-12 |
|
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: 63.80 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 66 FSKRGTPTMGGIMILTAITVSVLLWAYPSNPYVWCVLTVLIGYGIIGFVDDYRKVVRKDTKGLIArwkyfwMSVIALGVA 145
Cdd:cd06912 6 FHTRPTPRIGGVAIFLGLLAGLLLLSLLSGSLLLLLLLAALPAFLAGLLEDITKRVSPRIRLLAT------FLSALLAVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 146 FALYLAGKDTPAtelvvpfFKDVMPQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNMnfa 225
Cdd:cd06912 80 LLGASITRLDLP-------GLDLLLSFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDT--- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1170956473 226 nylhipylrhagELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIA 281
Cdd:cd06912 150 ------------DLAFLALLLAGALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
|
|
| GT_GPT_like |
cd06851 |
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ... |
72-283 |
5.97e-10 |
|
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: 58.66 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 72 PTMGGIMILTAITVSVLLW---------AYPSNPYVWCVLTVLIGYgIIGFVDDyrkvvrkdtkglIARWKYFWMSVIAL 142
Cdd:cd06851 14 PEPGGISILIGFVASEITLiffpflsfpHFPISEILAALITSVLGF-SVGIIDD------------RLTMGGWFKPVALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170956473 143 GVAFALYLAGKDTPATELVVPFFKDvmpQLGLFYILLAYFVIVGTGNAVNLTDGLDGLAIMPTVFVAAGFALVAWATGNm 222
Cdd:cd06851 81 FAAAPILLLGAYDSNLDFPLFGGSV---KIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQN- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1170956473 223 nfanylhipylrhaGELVIVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAVL 283
Cdd:cd06851 157 --------------YEIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAIL 203
|
|
| |
