|
Name |
Accession |
Description |
Interval |
E-value |
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
66-381 |
1.05e-113 |
|
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: 332.92 E-value: 1.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 66 GAISHAHKAGTPTMGGIIILLSVGGATLLWGAVANTYVWLSLVAMGGLGVVGFADDYVKTVRKQKDGLNAWYKVAGQVAV 145
Cdd:cd06852 1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 146 GLFVGSVLYFHPDfaaYNTFTFIPFLKDQVldydlfrflelgVDLGWLvYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTA 225
Cdd:cd06852 81 AIVFALLLYYFNG---SGTLITLPFFKNGL------------IDLGIL-YIPFAIFVIVGSSNAVNLTDGLDGLAAGVSI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 226 FVSLGLVALVYVSGNAEFatflnvmhlpgtgeLTVFVAAVTAACFGFLWYNGYPATVFMGDTGALALGGAVGSTILMVRK 305
Cdd:cd06852 145 IVALALAIIAYLAGNAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQ 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499722599 306 ELLLPLLGIVYFAEALSVIVQTSYFKYtrrrtgTGKRVFRMAPLHHHYEARGLHEAKIVTRFWIVTAITVIAALLI 381
Cdd:cd06852 211 ELLLLIIGGVFVIEALSVILQVGSFKL------TGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
|
|
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
46-385 |
4.21e-95 |
|
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: 287.03 E-value: 4.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 46 IIRWLRQQQLGEQVREgeaAGAISHAHKAGTPTMGGIIILLSVGGATLLWGAVANTYVWLSLVAMGGLGVVGFADDYVKT 125
Cdd:TIGR00445 8 VIPMLKKLKAGQVIRS---DGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDDYRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 126 VRKQKDGLNAWYKVAGQVAVGLFVGSVLYFhpdfAAYNTFTFIPFLKDQVLDydlfrflelgvdLGWLvYLPVVVFIVTA 205
Cdd:TIGR00445 85 KRKSNKGLTAKQKLFGQIIIALIFCTWLYY----YGPDTFIYIPFIKDFMFD------------LGLF-YILLAYFVLVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 206 VSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVSGNAEFATFLNVMHLPGTGELTVFVAAVTAACFGFLWYNGYPATVFMG 285
Cdd:TIGR00445 148 TSNAVNLTDGLDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 286 DTGALALGGAVGSTILMVRKELLLPLLGIVYFAEALSVIVQTSYFKytrrrtGTGKRVFRMAPLHHHYEARGLHEAKIVT 365
Cdd:TIGR00445 228 DTGSLALGGALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYK------TTKKRIFKMAPIHHHFELKGWSEPRVVV 301
|
330 340
....*....|....*....|
gi 499722599 366 RFWIVTAITVIAALLILRIR 385
Cdd:TIGR00445 302 RFWIISLLLALVALATLKVR 321
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
27-368 |
1.89e-77 |
|
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: 240.41 E-value: 1.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 27 RAALASITALGIALGAGRGIIRWLRQQQLGEQVREgeaagaiSHAHKAGTPTMGGIIILLSVGGATLLWGAVANTYVWLS 106
Cdd:COG0472 2 RLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNE-------RKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 107 LVAMGGLGVVGFADDYVktvrkqkdGLNAWYKVAGQVAVGLFVGSVLYfhpdfaaYNTFTFIPFLKDqvldydlfrflel 186
Cdd:COG0472 75 LLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLL-------RITSLTIPFFGL------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 187 gVDLGWLvYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVSGNaefatflnvmhlpgtGELTVFVAAVT 266
Cdd:COG0472 127 -LDLGWL-YIPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 267 AACFGFLWYNGYPATVFMGDTGALALGGAVGSTILMVRKE----LLLPLLGIVYFAEALSVIVQtsyfkytrrRTGTGKR 342
Cdd:COG0472 190 GALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQ---------RVLRGKR 260
|
330 340
....*....|....*....|....*...
gi 499722599 343 VFR--MAPLHHHYEARGLHEAKIVTRFW 368
Cdd:COG0472 261 IFKadRAHLHHHLELLGWSERQVVLRFW 288
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
107-302 |
8.32e-24 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 96.13 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 107 LVAMGGLGVVGFADDYVktvrkqkdGLNAWYKVAGQVAVGLFVGsvlyfhpdFAAYNTFTFIPFLkdqvldydlfrFLEL 186
Cdd:pfam00953 4 LLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILL--------VLGGIGLTSLGLP-----------FGGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 187 GVDLGWLVYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVSGNAEFAtflnvmhlpgtgeltVFVAAVT 266
Cdd:pfam00953 57 SLELGPWLSILLTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELA---------------LLSLALL 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 499722599 267 AACFGFLWYNGYPATVFMGDTGALALGGAVGSTILM 302
Cdd:pfam00953 122 GALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLAII 157
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
66-381 |
1.05e-113 |
|
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: 332.92 E-value: 1.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 66 GAISHAHKAGTPTMGGIIILLSVGGATLLWGAVANTYVWLSLVAMGGLGVVGFADDYVKTVRKQKDGLNAWYKVAGQVAV 145
Cdd:cd06852 1 GPKSHLKKAGTPTMGGILFILAILISTLLWADLDSPEVLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLLLQFLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 146 GLFVGSVLYFHPDfaaYNTFTFIPFLKDQVldydlfrflelgVDLGWLvYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTA 225
Cdd:cd06852 81 AIVFALLLYYFNG---SGTLITLPFFKNGL------------IDLGIL-YIPFAIFVIVGSSNAVNLTDGLDGLAAGVSI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 226 FVSLGLVALVYVSGNAEFatflnvmhlpgtgeLTVFVAAVTAACFGFLWYNGYPATVFMGDTGALALGGAVGSTILMVRK 305
Cdd:cd06852 145 IVALALAIIAYLAGNAVF--------------LAVFCAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQ 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499722599 306 ELLLPLLGIVYFAEALSVIVQTSYFKYtrrrtgTGKRVFRMAPLHHHYEARGLHEAKIVTRFWIVTAITVIAALLI 381
Cdd:cd06852 211 ELLLLIIGGVFVIEALSVILQVGSFKL------TGKRIFKMAPLHHHFELKGWSETKVVVRFWIISLILALIGLLL 280
|
|
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
46-385 |
4.21e-95 |
|
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: 287.03 E-value: 4.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 46 IIRWLRQQQLGEQVREgeaAGAISHAHKAGTPTMGGIIILLSVGGATLLWGAVANTYVWLSLVAMGGLGVVGFADDYVKT 125
Cdd:TIGR00445 8 VIPMLKKLKAGQVIRS---DGPKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPYVLLVLFVLLGYGFIGFVDDYRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 126 VRKQKDGLNAWYKVAGQVAVGLFVGSVLYFhpdfAAYNTFTFIPFLKDQVLDydlfrflelgvdLGWLvYLPVVVFIVTA 205
Cdd:TIGR00445 85 KRKSNKGLTAKQKLFGQIIIALIFCTWLYY----YGPDTFIYIPFIKDFMFD------------LGLF-YILLAYFVLVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 206 VSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVSGNAEFATFLNVMHLPGTGELTVFVAAVTAACFGFLWYNGYPATVFMG 285
Cdd:TIGR00445 148 TSNAVNLTDGLDGLAIGPSAIAFGALAILAWATGNANFAKYLHIPYLKDSGELVIFCTALVGASLGFLWFNAYPAKVFMG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 286 DTGALALGGAVGSTILMVRKELLLPLLGIVYFAEALSVIVQTSYFKytrrrtGTGKRVFRMAPLHHHYEARGLHEAKIVT 365
Cdd:TIGR00445 228 DTGSLALGGALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYK------TTKKRIFKMAPIHHHFELKGWSEPRVVV 301
|
330 340
....*....|....*....|
gi 499722599 366 RFWIVTAITVIAALLILRIR 385
Cdd:TIGR00445 302 RFWIISLLLALVALATLKVR 321
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
27-368 |
1.89e-77 |
|
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: 240.41 E-value: 1.89e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 27 RAALASITALGIALGAGRGIIRWLRQQQLGEQVREgeaagaiSHAHKAGTPTMGGIIILLSVGGATLLWGAVANTYVWLS 106
Cdd:COG0472 2 RLLLAFLLAFLLSLLLTPLLIRLARRLGLVDDPNE-------RKSHKRPTPRMGGIAIFLGFLLALLLLALLSNPELLLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 107 LVAMGGLGVVGFADDYVktvrkqkdGLNAWYKVAGQVAVGLFVGSVLYfhpdfaaYNTFTFIPFLKDqvldydlfrflel 186
Cdd:COG0472 75 LLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLLLL-------RITSLTIPFFGL------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 187 gVDLGWLvYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVSGNaefatflnvmhlpgtGELTVFVAAVT 266
Cdd:COG0472 127 -LDLGWL-YIPLTVFWIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQ---------------GELALLAAALA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 267 AACFGFLWYNGYPATVFMGDTGALALGGAVGSTILMVRKE----LLLPLLGIVYFAEALSVIVQtsyfkytrrRTGTGKR 342
Cdd:COG0472 190 GALLGFLWFNFPPAKIFMGDTGSLFLGFALAALAILGRQEgaslLLLLLILGVPVVDTLSVILQ---------RVLRGKR 260
|
330 340
....*....|....*....|....*...
gi 499722599 343 VFR--MAPLHHHYEARGLHEAKIVTRFW 368
Cdd:COG0472 261 IFKadRAHLHHHLELLGWSERQVVLRFW 288
|
|
| GT_WecA_like |
cd06853 |
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ... |
72-293 |
6.66e-29 |
|
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: 112.58 E-value: 6.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 72 HKAGTPTMGGIIILLSVGGATLLWGAVA---NTYVWLSLVAMGGLGVVGFADDYVktvrkqkdGLNAWYKVAGQVAVGLF 148
Cdd:cd06853 4 HKGPIPRLGGLAIFLGFLLALLLALLFPfflLPELLGLLAGATIIVLLGLLDDLF--------DLSPKVKLLGQILAALI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 149 VgsvlyfhpdfaayntftfipFLKDQVLDYDLFRFLELGVDLGWLVYlPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVS 228
Cdd:cd06853 76 V--------------------VFGGGVILSLLGPFGGGIILLGWLSI-PLTVLWIVGIINAINLIDGLDGLAGGVALIAS 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499722599 229 LGLVALVYVSGNAEFATFLnvmhlpgtgeltvfvAAVTAACFGFLWYNGYPATVFMGDTGALALG 293
Cdd:cd06853 135 LALAILALLNGQVLVALLA---------------LALAGALLGFLPYNFHPARIFMGDAGSLFLG 184
|
|
| GT_MraY-like |
cd06499 |
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ... |
75-299 |
2.49e-28 |
|
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: 109.31 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 75 GTPTMGGIIILLSVGGATLLWGAVANTYVWLSLVAMGGLGVVGFADDYVKTvrkqKDGLNAWYKVAGQVAVGLFVGsvly 154
Cdd:cd06499 1 PTPTMGGLAILLGFLLGVLLYIPHSNTLILLALLSGLVAGIVGFIDDLLGL----KVELSEREKLLLQILAALFLL---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 155 fhpdfaaynTFTFIPFLKDQVLDYDLfrflelgvDLGWLvYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVSLGLVAL 234
Cdd:cd06499 73 ---------LIGGGHTTVTTPLGFVL--------DLGIF-YIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499722599 235 VYVSGNAEFATFLnvmhlpgtgeltvfvAAVTAACFGFLWYNGYPATVFMGDTGALALGGAVGST 299
Cdd:cd06499 135 ALLSGQTTSALLF---------------IILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAV 184
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
107-302 |
8.32e-24 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 96.13 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 107 LVAMGGLGVVGFADDYVktvrkqkdGLNAWYKVAGQVAVGLFVGsvlyfhpdFAAYNTFTFIPFLkdqvldydlfrFLEL 186
Cdd:pfam00953 4 LLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILL--------VLGGIGLTSLGLP-----------FGGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 187 GVDLGWLVYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVSGNAEFAtflnvmhlpgtgeltVFVAAVT 266
Cdd:pfam00953 57 SLELGPWLSILLTLFAIVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELA---------------LLSLALL 121
|
170 180 190
....*....|....*....|....*....|....*.
gi 499722599 267 AACFGFLWYNGYPATVFMGDTGALALGGAVGSTILM 302
Cdd:pfam00953 122 GALLGFLPFNFYPAKIFMGDSGSLFLGFLLAVLAII 157
|
|
| GT_WbpL_WbcO_like |
cd06854 |
The members of this subfamily catalyze the formation of a phosphodiester bond between a ... |
71-344 |
1.05e-19 |
|
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: 87.68 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 71 AHKAGTPTMGGIIILLSVGGATLL---WGAVANTYVWLSLVAMGGLGVVGFADDYvktvrkqkDGLNAWYKVAGQVAVGL 147
Cdd:cd06854 10 SHTKPTPRGGGIAFVLAFLLALLLaaaAGPLNDLSYLLLLIGLLLLAAVGFIDDL--------RSLSPKIRLLVQLLAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 148 FVgsvLYFHPDFAayntftfipflkdqvldydlfrFLELGVDLGWLVYLPVVVFIVTAVsNAVNLTDGLDGLTTGVTAFV 227
Cdd:cd06854 82 LA---LYALGPLT----------------------SLLLNFLPPWLIALLLLLAIVWII-NLYNFMDGIDGLAGGEALVV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 228 SLGLVALVYVSGNAEFATFLnvmhlpgtgeltvfvAAVTAACFGFLWYNGYPATVFMGDTGALALGGAVGSTILM----- 302
Cdd:cd06854 136 FLALALLGYLAGEPALALLA---------------LALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLlalsg 200
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499722599 303 VRKELLLPLLGiVYFAEALSVIVqtsyfkytrRRTGTGKRVF 344
Cdd:cd06854 201 QSPWAWLLLLS-PFLVDATVTLL---------RRLLRGENIF 232
|
|
| GT_GPT_archaea |
cd06856 |
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ... |
72-342 |
1.75e-19 |
|
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: 87.30 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 72 HKAGT---PTMGGIIILL--SVGGATLLWGAVANTYVWLSLVAMGGlGVVGFADDYVktvrkqkdGLNAWYKVAGQVAVG 146
Cdd:cd06856 6 HKPGKpevPEMGGIAVLLgfSLGLLFLSALTHSVEALALLITSLLA-GLIGLLDDIL--------GLSQSEKVLLTALPA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 147 LFVGSVLYFHPdfaayntftfipflkdqvldydLFRFLELGVDLGWLVYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAF 226
Cdd:cd06856 77 IPLLVLKAGNP----------------------LTSLPIGGRVLGILYYLLIVPLGITGASNAFNMLAGFNGLEAGMGII 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 227 VSLGLVALVYVSGNAEFATFLNVMHlpgtgeltvfvaavtAACFGFLWYNGYPATVFMGDTGALALGGAVGSTILMVRKE 306
Cdd:cd06856 135 ILLALAIILLINGDYDALIIALILV---------------AALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLE 199
|
250 260 270
....*....|....*....|....*....|....*.
gi 499722599 307 LLLPLLGIVYFAEALSVIVqtSYFKYTRRRTGTGKR 342
Cdd:cd06856 200 IILLILLLPYVIDFLLKLR--SKGGGKEHREKPTKV 233
|
|
| GT_MraY_like |
cd06912 |
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ... |
72-293 |
5.28e-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: 64.19 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 72 HKAGTPTMGGIIILLSVGGATLLWGAVANTYVWLSLVAMGGLGVVGFADDYVKTVrkqkdglNAWYKVAGQVAVGLFVgs 151
Cdd:cd06912 7 HTRPTPRIGGVAIFLGLLAGLLLLSLLSGSLLLLLLLAALPAFLAGLLEDITKRV-------SPRIRLLATFLSALLA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 152 vLYFHPdfaAYNTFTFIPFLkDQVLDYdlfrflelgvdlgWLVYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVSLGL 231
Cdd:cd06912 78 -VWLLG---ASITRLDLPGL-DLLLSF-------------PPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499722599 232 VALVyvsgnaefatflnvmHLPGTGELTVFVAAVTAACFGFLWYNGYPATVFMGDTGALALG 293
Cdd:cd06912 140 ALVA---------------FQVGDTDLAFLALLLAGALLGFLIFNFPFGKIFLGDGGAYLLG 186
|
|
| GT_GPT_like |
cd06851 |
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ... |
164-297 |
2.64e-08 |
|
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: 54.04 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 164 TFTFIPFLKDQVLDYDLFRFLELGVDLGWLVYLPVVVFIVTAVSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVSGNAEF 243
Cdd:cd06851 80 AFAAAPILLLGAYDSNLDFPLFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQNYEI 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499722599 244 ATFLNVMhlpgtgeltvfvaavTAACFGFLWYNGYPATVFMGDTGALALGGAVG 297
Cdd:cd06851 160 GIACLCL---------------AFASLAFLYYNKYPSRIFPGDTGAYMFGATYA 198
|
|
| GT_GPT_euk |
cd06855 |
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ... |
180-287 |
7.40e-04 |
|
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: 41.08 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499722599 180 LFRFLELGVDLGWLVYLPVVVFIVTAvSNAVNLTDGLDGLTTGVTAFVSLGLVALVYVsgnaEFATFLNVMHLPGTGELT 259
Cdd:cd06855 117 LRPLLGTLIDLGILYYVYMILLAVFC-TNSINIYAGINGLEVGQSLVIALSILLYNLL----ELNGSSGSMTLDAHLFSL 191
|
90 100
....*....|....*....|....*...
gi 499722599 260 VFVAAVTAACFGFLWYNGYPATVFMGDT 287
Cdd:cd06855 192 YLLLPFIAVSLALLYYNWYPSKVFVGDT 219
|
|
| |
