|
Name |
Accession |
Description |
Interval |
E-value |
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
37-360 |
3.02e-151 |
|
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: 428.79 E-value: 3.02e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 37 SLYFGPKLIVALQKMQIGQTVRDDGPQSHLSKSGTPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLFVVGSLGIVGFVDD 116
Cdd:TIGR00445 1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 117 YRKVIRKDSKGLIARWKYFWQSVIAISVASYMYFSsssAAETTLVVPFLKEVMPQLGLFYLVMCYFVIVGTSNAVNLTDG 196
Cdd:TIGR00445 81 YRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYY---GPDTFIYIPFIKDFMFDLGLFYILLAYFVLVGTSNAVNLTDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 197 LDGLAIVPTILVASALAIIAYLTGNVNFSNYLHIPHIPLASELVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGA 276
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 277 LGIIAILVRQELVLMIMGGVFVMEALSVILQVGSYKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISIVLVLAGLAT 356
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALAT 317
|
....
gi 1093984881 357 LKIR 360
Cdd:TIGR00445 318 LKVR 321
|
|
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
61-356 |
3.75e-134 |
|
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: 383.76 E-value: 3.75e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 61 GPQSHLSKSGTPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLFVVGSLGIVGFVDDYRKVIRKDSKGLIARWKYFWQSVI 140
Cdd:cd06852 1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 141 AISVASYMYFSSSSaaETTLVVPFLKEVMPQLGLFYLVMCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTG 220
Cdd:cd06852 81 AIVFALLLYYFNGS--GTLITLPFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 221 NVNFsnylhiphiplaseLVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAILVRQELVLMIMGGVFVME 300
Cdd:cd06852 159 NAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIE 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093984881 301 ALSVILQVGSYKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISIVLVLAGLAT 356
Cdd:cd06852 225 ALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
24-343 |
4.31e-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: 274.70 E-value: 4.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 24 LRAILGILTALFISLYFGPKLIVALQKMQIGqtvrDDGPQSHLSKSGTPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLF 103
Cdd:COG0472 1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLV----DDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 104 VVGSLGIVGFVDDYRkvirkdskGLIARWKYFWQSVIAISVASYMYFssssaaETTLVVPFLKEVmpQLGLFYLVMCYFV 183
Cdd:COG0472 77 GALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLR------ITSLTIPFFGLL--DLGWLYIPLTVFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 184 IVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNvnfsnylhiphiplaSELVVVCTAIVGAGLGFLWFNTYPAQV 263
Cdd:COG0472 141 IVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALAGALLGFLWFNFPPAKI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 264 FMGDVGSLALGGALGIIAILVRQE----LVLMIMGGVFVMEALSVILQvgsYKLRGQRIFR--MAPIHHHYELKGWPEPR 337
Cdd:COG0472 206 FMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQ---RVLRGKRIFKadRAHLHHHLELLGWSERQ 282
|
....*.
gi 1093984881 338 VIVRFW 343
Cdd:COG0472 283 VVLRFW 288
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
99-283 |
2.78e-27 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 105.38 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 99 WVTLFVVGSLGIVGFVDDYrkvirkdsKGLIARWKYFWQSVIAISVASYMYFSSssaaeTTLVVPFLKEVMPQLGLFYLV 178
Cdd:pfam00953 1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGGIGL-----TSLGLPFGGGSLELGPWLSIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 179 MCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNvnfsnylhiphiplaSELVVVCTAIVGAGLGFLWFNT 258
Cdd:pfam00953 68 LTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGN---------------LELALLSLALLGALLGFLPFNF 132
|
170 180
....*....|....*....|....*
gi 1093984881 259 YPAQVFMGDVGSLALGGALGIIAIL 283
Cdd:pfam00953 133 YPAKIFMGDSGSLFLGFLLAVLAII 157
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
37-360 |
3.02e-151 |
|
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: 428.79 E-value: 3.02e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 37 SLYFGPKLIVALQKMQIGQTVRDDGPQSHLSKSGTPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLFVVGSLGIVGFVDD 116
Cdd:TIGR00445 1 SLLLGPKVIPMLKKLKAGQVIRSDGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 117 YRKVIRKDSKGLIARWKYFWQSVIAISVASYMYFSsssAAETTLVVPFLKEVMPQLGLFYLVMCYFVIVGTSNAVNLTDG 196
Cdd:TIGR00445 81 YRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYY---GPDTFIYIPFIKDFMFDLGLFYILLAYFVLVGTSNAVNLTDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 197 LDGLAIVPTILVASALAIIAYLTGNVNFSNYLHIPHIPLASELVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGA 276
Cdd:TIGR00445 158 LDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMGDTGSLALGGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 277 LGIIAILVRQELVLMIMGGVFVMEALSVILQVGSYKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISIVLVLAGLAT 356
Cdd:TIGR00445 238 LGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTKKRIFKMAPIHHHFELKGWSEPRVVVRFWIISLLLALVALAT 317
|
....
gi 1093984881 357 LKIR 360
Cdd:TIGR00445 318 LKVR 321
|
|
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
61-356 |
3.75e-134 |
|
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: 383.76 E-value: 3.75e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 61 GPQSHLSKSGTPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLFVVGSLGIVGFVDDYRKVIRKDSKGLIARWKYFWQSVI 140
Cdd:cd06852 1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 141 AISVASYMYFSSSSaaETTLVVPFLKEVMPQLGLFYLVMCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTG 220
Cdd:cd06852 81 AIVFALLLYYFNGS--GTLITLPFFKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAYLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 221 NVNFsnylhiphiplaseLVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAILVRQELVLMIMGGVFVME 300
Cdd:cd06852 159 NAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIE 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1093984881 301 ALSVILQVGSYKLRGQRIFRMAPIHHHYELKGWPEPRVIVRFWIISIVLVLAGLAT 356
Cdd:cd06852 225 ALSVILQVGSFKLTGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
24-343 |
4.31e-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: 274.70 E-value: 4.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 24 LRAILGILTALFISLYFGPKLIVALQKMQIGqtvrDDGPQSHLSKSGTPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLF 103
Cdd:COG0472 1 LRLLLAFLLAFLLSLLLTPLLIRLARRLGLV----DDPNERKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLLLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 104 VVGSLGIVGFVDDYRkvirkdskGLIARWKYFWQSVIAISVASYMYFssssaaETTLVVPFLKEVmpQLGLFYLVMCYFV 183
Cdd:COG0472 77 GALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLLR------ITSLTIPFFGLL--DLGWLYIPLTVFW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 184 IVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNvnfsnylhiphiplaSELVVVCTAIVGAGLGFLWFNTYPAQV 263
Cdd:COG0472 141 IVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALAGALLGFLWFNFPPAKI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 264 FMGDVGSLALGGALGIIAILVRQE----LVLMIMGGVFVMEALSVILQvgsYKLRGQRIFR--MAPIHHHYELKGWPEPR 337
Cdd:COG0472 206 FMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQ---RVLRGKRIFKadRAHLHHHLELLGWSERQ 282
|
....*.
gi 1093984881 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 |
1.02e-32 |
|
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: 120.48 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 70 GTPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLFVVGSLGIVGFVDDYRKVirkdSKGLIARWKYFWQsviaISVASYMY 149
Cdd:cd06499 1 PTPTMGGLAILLGFLLGVLLYIPHSNTLILLALLSGLVAGIVGFIDDLLGL----KVELSEREKLLLQ----ILAALFLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 150 FSSssAAETTLVVPFlkEVMPQLGLFYLVMCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNVNfsnylh 229
Cdd:cd06499 73 LIG--GGHTTVTTPL--GFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTT------ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1093984881 230 iphiplaseLVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIA 281
Cdd:cd06499 143 ---------SALLFIILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
|
|
| GT_WecA_like |
cd06853 |
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ... |
71-320 |
1.32e-27 |
|
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: 108.73 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 71 TPTMGGLLILAAIFTSTLLWGDL---DNKYVWVTLFVVGSLGIVGFVDDYrkvirkdsKGLIARWKYFWQSVIAISVASY 147
Cdd:cd06853 8 IPRLGGLAIFLGFLLALLLALLFpffLLPELLGLLAGATIIVLLGLLDDL--------FDLSPKVKLLGQILAALIVVFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 148 MYFSSSSaaettLVVPFLKEVMpqLGLFYLVMCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNVnfsny 227
Cdd:cd06853 80 GGVILSL-----LGPFGGGIIL--LGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQV----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 228 lhiphiplasELVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAILVRQE-------LVLMIMGGVFVME 300
Cdd:cd06853 148 ----------LVALLALALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQKsstaispVVPLLILAVPLFD 217
|
250 260
....*....|....*....|
gi 1093984881 301 ALSVILqvgSYKLRGQRIFR 320
Cdd:cd06853 218 TLFVII---RRLLRGRSPFQ 234
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
99-283 |
2.78e-27 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 105.38 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 99 WVTLFVVGSLGIVGFVDDYrkvirkdsKGLIARWKYFWQSVIAISVASYMYFSSssaaeTTLVVPFLKEVMPQLGLFYLV 178
Cdd:pfam00953 1 LGLLLGALLIGLIGLIDDL--------LGLSARIKLLLQALAALILLVLGGIGL-----TSLGLPFGGGSLELGPWLSIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 179 MCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNvnfsnylhiphiplaSELVVVCTAIVGAGLGFLWFNT 258
Cdd:pfam00953 68 LTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGN---------------LELALLSLALLGALLGFLPFNF 132
|
170 180
....*....|....*....|....*
gi 1093984881 259 YPAQVFMGDVGSLALGGALGIIAIL 283
Cdd:pfam00953 133 YPAKIFMGDSGSLFLGFLLAVLAII 157
|
|
| GT_WbpL_WbcO_like |
cd06854 |
The members of this subfamily catalyze the formation of a phosphodiester bond between a ... |
71-319 |
5.07e-22 |
|
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: 93.46 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 71 TPTMGGLLILAAIFTSTLL---WGDLDNKYVWVTLFVVGSLGIVGFVDDYRkvirkdskGLIARWKYFWQSVIAISVasy 147
Cdd:cd06854 15 TPRGGGIAFVLAFLLALLLaaaAGPLNDLSYLLLLIGLLLLAAVGFIDDLR--------SLSPKIRLLVQLLAAALA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 148 myfsssSAAETTLVVPFLKEVMPQLGLFYLVmcyFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGnvnfsny 227
Cdd:cd06854 84 ------LYALGPLTSLLLNFLPPWLIALLLL---LAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAG------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 228 lhiphiplASELVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAIL-----VRQELVLMIMgGVFVMEAL 302
Cdd:cd06854 148 --------EPALALLALALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLlalsgQSPWAWLLLL-SPFLVDAT 218
|
250
....*....|....*..
gi 1093984881 303 SVILQvgsYKLRGQRIF 319
Cdd:cd06854 219 VTLLR---RLLRGENIF 232
|
|
| GT_GPT_archaea |
cd06856 |
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ... |
72-309 |
2.43e-20 |
|
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: 89.61 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 72 PTMGGLLILAAI-FTSTLLWGDLDNKYVWVTLFVVGSLGIVGFVDDYRKVIRKDskgliarwKYFWQSVIAISVASYMYF 150
Cdd:cd06856 14 PEMGGIAVLLGFsLGLLFLSALTHSVEALALLITSLLAGLIGLLDDILGLSQSE--------KVLLTALPAIPLLVLKAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 151 ssssaaeTTLVVPFLKEVMPqLGLFYLVMCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNVnfsnylhi 230
Cdd:cd06856 86 -------NPLTSLPIGGRVL-GILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDY-------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1093984881 231 phiplasELVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAILVRQELVLMIMGGVFVMEALSVILQVG 309
Cdd:cd06856 150 -------DALIIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVIDFLLKLRSKG 221
|
|
| GT_MraY_like |
cd06912 |
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ... |
71-281 |
3.38e-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: 64.57 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 71 TPTMGGLLILAAIFTSTLLWGDLDNKYVWVTLFVVGSLGIVGFVDDYrkvirkdSKGLIARWKYFWQSVIAISVASYMYF 150
Cdd:cd06912 11 TPRIGGVAIFLGLLAGLLLLSLLSGSLLLLLLLAALPAFLAGLLEDI-------TKRVSPRIRLLATFLSALLAVWLLGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 151 SSSSaaettLVVPFLKEVMpQLGLFYLVMCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNVnfsnylhi 230
Cdd:cd06912 84 SITR-----LDLPGLDLLL-SFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDT-------- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1093984881 231 phiplasELVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIA 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 |
2.59e-09 |
|
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: 56.74 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 72 PTMGGLLILAAIFTSTLLWGDLDNKY--------VWVTLFVVGSLGIVGFVDDyrkviRKDSKGliarwkyfWQSVIAIS 143
Cdd:cd06851 14 PEPGGISILIGFVASEITLIFFPFLSfphfpiseILAALITSVLGFSVGIIDD-----RLTMGG--------WFKPVALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 144 VASyMYFSSSSAAETTLVVPFLKEVMpQLGLFYLVMCYFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNvn 223
Cdd:cd06851 81 FAA-APILLLGAYDSNLDFPLFGGSV-KIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQN-- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 224 fsnylhiphiplaSELVVVCTAIVGAGLGFLWFNTYPAQVFMGDVGSLALGGALGIIAIL 283
Cdd:cd06851 157 -------------YEIGIACLCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAIL 203
|
|
| GT_GPT_euk |
cd06855 |
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ... |
102-283 |
7.57e-05 |
|
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: 43.77 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 102 LFVVGSLGIVGFVDDYrkvirkdskgLIARWKYFWQSVIAISVASYM-YFSSSSAAETTLVVPFLKEVMPQLGLFYLVMC 180
Cdd:cd06855 66 LLSICCMTFLGFADDV----------LDLRWRHKLILPTFASLPLLMvYYGNTGITLPIVPLRPLLGTLIDLGILYYVYM 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1093984881 181 YFVIVGTSNAVNLTDGLDGLAIVPTILVASALAIIAYLTGNVNFSNYLHIPHipLASELVVVCtaIVGAGLGFLWFNTYP 260
Cdd:cd06855 136 ILLAVFCTNSINIYAGINGLEVGQSLVIALSILLYNLLELNGSSGSMTLDAH--LFSLYLLLP--FIAVSLALLYYNWYP 211
|
170 180
....*....|....*....|...
gi 1093984881 261 AQVFMGDVGSLALGGALGIIAIL 283
Cdd:cd06855 212 SKVFVGDTFTYFAGMVFAVVGIL 234
|
|
| |
