|
Name |
Accession |
Description |
Interval |
E-value |
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
41-333 |
7.93e-98 |
|
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: 290.54 E-value: 7.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 41 KQHLAKAGTPTMGGTVFLIVALLVSLIFSIILSKEnsgnlgaTFGILSVVLIYGIIGFLDDFLKIFKQINEGLTPKQKMS 120
Cdd:cd06852 3 KSHLKKAGTPTMGGILFILAILISTLLWADLDSPE-------VLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 121 LQLIAGLIFYFVHVLPSGTSAINI----FGFYLEVGYLYAFFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAY 196
Cdd:cd06852 76 LQFLIAIVFALLLYYFNGSGTLITlpffKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 197 NQTQFDILLII-VIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAISIALRQEWTLLFIGFVYVFETSSVMLQVAYF 275
Cdd:cd06852 156 LAGNAVFLAVFcAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446402165 276 KYTkkktgvGKRIFRMTPFHHHLELGGvsgkgnkWSEWKVDAFLWAIGIFMSAITLAI 333
Cdd:cd06852 236 KLT------GKRIFKMAPLHHHFELKG-------WSETKVVVRFWIISLILALIGLLL 280
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
2-320 |
2.74e-76 |
|
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: 235.79 E-value: 2.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 2 FLSIMAGVIAFVLTVIAIPRFIKFyqLKKIGGQQMHEDVKQHlaKAGTPTMGGTVFLIVALLVSLIFSIILSKEnsgnlg 81
Cdd:COG0472 1 LRLLLAFLLAFLLSLLLTPLLIRL--ARRLGLVDDPNERKSH--KRPTPRMGGIAIFLGFLLALLLLALLSNPE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 82 aTFGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIAGLIFYFVhvLPSGTSAINIFGFYLEVGYLYAFFVLF 161
Cdd:COG0472 71 -LLLLLLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLL--LLRITSLTIPFFGLLDLGWLYIPLTVF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 162 WVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLIIVIMIGALLGFFVFNHKPAKVFMGDVGSLALGAML 241
Cdd:COG0472 140 WIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 242 AAISIALRQE----WTLLFIGFVYVFETSSVMLQVAYFkytkkktgvGKRIFR--MTPFHHHLELGGvsgkgnkWSEWKV 315
Cdd:COG0472 220 AALAILGRQEgaslLLLLLILGVPVVDTLSVILQRVLR---------GKRIFKadRAHLHHHLELLG-------WSERQV 283
|
....*
gi 446402165 316 DAFLW 320
Cdd:COG0472 284 VLRFW 288
|
|
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
15-336 |
7.22e-68 |
|
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: 215.39 E-value: 7.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 15 TVIAIPRFIKFYQLKKIGgQQMHEDV-KQHLAKAGTPTMGGTVFLIVALLVSLIFSIILSKEnsgnlgaTFGILSVVLIY 93
Cdd:TIGR00445 1 SLLLGPKVIPMLKKLKAG-QVIRSDGpKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPY-------VLLVLFVLLGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 94 GIIGFLDDFLKIFKQINEGLTPKQKMSLQLIAGLIFYFVHVLPSGTSAINIFG---FYLEVGYLYAFFVLFWVVGFSNAV 170
Cdd:TIGR00445 73 GFIGFVDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFikdFMFDLGLFYILLAYFVLVGTSNAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 171 NLTDGIDGLASISVVISLITYGIIAYNQTQFD---------------ILLIIVIMIGALLGFFVFNHKPAKVFMGDVGSL 235
Cdd:TIGR00445 153 NLTDGLDGLAIGPSAIAFGALAILAWATGNANfakylhipylkdsgeLVIFCTALVGASLGFLWFNAYPAKVFMGDTGSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 236 ALGAMLAAISIALRQEWTLLFIGFVYVFETSSVMLQVAYFKYTKkktgvgKRIFRMTPFHHHLELGGvsgkgnkWSEWKV 315
Cdd:TIGR00445 233 ALGGALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTK------KRIFKMAPIHHHFELKG-------WSEPRV 299
|
330 340
....*....|....*....|.
gi 446402165 316 DAFLWAIGIFMSAITLAILYL 336
Cdd:TIGR00445 300 VVRFWIISLLLALVALATLKV 320
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
84-248 |
9.94e-31 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 113.85 E-value: 9.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 84 FGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIAGLIFYFVHVLPSGTSAINIFGFYLEVGY-LYAFFVLFW 162
Cdd:pfam00953 1 LGLLLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLELGPwLSILLTLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 163 VVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLIIVIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLA 242
Cdd:pfam00953 73 IVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLA 152
|
....*.
gi 446402165 243 AISIAL 248
Cdd:pfam00953 153 VLAIIG 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GT_MraY |
cd06852 |
Phospho-N-acetylmuramoyl-pentapeptide-transferase (mraY) is an enzyme responsible for the ... |
41-333 |
7.93e-98 |
|
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: 290.54 E-value: 7.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 41 KQHLAKAGTPTMGGTVFLIVALLVSLIFSIILSKEnsgnlgaTFGILSVVLIYGIIGFLDDFLKIFKQINEGLTPKQKMS 120
Cdd:cd06852 3 KSHLKKAGTPTMGGILFILAILISTLLWADLDSPE-------VLLLLLLTLGFGLIGFLDDYLKVVKKRNLGLSARQKLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 121 LQLIAGLIFYFVHVLPSGTSAINI----FGFYLEVGYLYAFFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAY 196
Cdd:cd06852 76 LQFLIAIVFALLLYYFNGSGTLITlpffKNGLIDLGILYIPFAIFVIVGSSNAVNLTDGLDGLAAGVSIIVALALAIIAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 197 NQTQFDILLII-VIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAISIALRQEWTLLFIGFVYVFETSSVMLQVAYF 275
Cdd:cd06852 156 LAGNAVFLAVFcAALVGACLGFLWFNAYPAKVFMGDTGSLALGGALAALAILTKQELLLLIIGGVFVIEALSVILQVGSF 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446402165 276 KYTkkktgvGKRIFRMTPFHHHLELGGvsgkgnkWSEWKVDAFLWAIGIFMSAITLAI 333
Cdd:cd06852 236 KLT------GKRIFKMAPLHHHFELKG-------WSETKVVVRFWIISLILALIGLLL 280
|
|
| Rfe |
COG0472 |
UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate ... |
2-320 |
2.74e-76 |
|
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: 235.79 E-value: 2.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 2 FLSIMAGVIAFVLTVIAIPRFIKFyqLKKIGGQQMHEDVKQHlaKAGTPTMGGTVFLIVALLVSLIFSIILSKEnsgnlg 81
Cdd:COG0472 1 LRLLLAFLLAFLLSLLLTPLLIRL--ARRLGLVDDPNERKSH--KRPTPRMGGIAIFLGFLLALLLLALLSNPE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 82 aTFGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIAGLIFYFVhvLPSGTSAINIFGFYLEVGYLYAFFVLF 161
Cdd:COG0472 71 -LLLLLLGALLLGLIGFLDDLL--------GLSARQKLLGQLLAALLLVLL--LLRITSLTIPFFGLLDLGWLYIPLTVF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 162 WVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLIIVIMIGALLGFFVFNHKPAKVFMGDVGSLALGAML 241
Cdd:COG0472 140 WIVGVSNAVNLTDGLDGLAAGVSLIAALALAIIAYLAGQGELALLAAALAGALLGFLWFNFPPAKIFMGDTGSLFLGFAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 242 AAISIALRQE----WTLLFIGFVYVFETSSVMLQVAYFkytkkktgvGKRIFR--MTPFHHHLELGGvsgkgnkWSEWKV 315
Cdd:COG0472 220 AALAILGRQEgaslLLLLLILGVPVVDTLSVILQRVLR---------GKRIFKadRAHLHHHLELLG-------WSERQV 283
|
....*
gi 446402165 316 DAFLW 320
Cdd:COG0472 284 VLRFW 288
|
|
| mraY |
TIGR00445 |
phospho-N-acetylmuramoyl-pentapeptide-transferase; Involved in peptidoglycan biosynthesis, the ... |
15-336 |
7.22e-68 |
|
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: 215.39 E-value: 7.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 15 TVIAIPRFIKFYQLKKIGgQQMHEDV-KQHLAKAGTPTMGGTVFLIVALLVSLIFSIILSKEnsgnlgaTFGILSVVLIY 93
Cdd:TIGR00445 1 SLLLGPKVIPMLKKLKAG-QVIRSDGpKSHLKKKGTPTMGGIMIVFAIIVSTVLWAQLGNPY-------VLLVLFVLLGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 94 GIIGFLDDFLKIFKQINEGLTPKQKMSLQLIAGLIFYFVHVLPSGTSAINIFG---FYLEVGYLYAFFVLFWVVGFSNAV 170
Cdd:TIGR00445 73 GFIGFVDDYRKIKRKSNKGLTAKQKLFGQIIIALIFCTWLYYYGPDTFIYIPFikdFMFDLGLFYILLAYFVLVGTSNAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 171 NLTDGIDGLASISVVISLITYGIIAYNQTQFD---------------ILLIIVIMIGALLGFFVFNHKPAKVFMGDVGSL 235
Cdd:TIGR00445 153 NLTDGLDGLAIGPSAIAFGALAILAWATGNANfakylhipylkdsgeLVIFCTALVGASLGFLWFNAYPAKVFMGDTGSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 236 ALGAMLAAISIALRQEWTLLFIGFVYVFETSSVMLQVAYFKYTKkktgvgKRIFRMTPFHHHLELGGvsgkgnkWSEWKV 315
Cdd:TIGR00445 233 ALGGALGAVAILTKNEILLVIMGGVFVIETLSVILQVGSYKTTK------KRIFKMAPIHHHFELKG-------WSEPRV 299
|
330 340
....*....|....*....|.
gi 446402165 316 DAFLWAIGIFMSAITLAILYL 336
Cdd:TIGR00445 300 VVRFWIISLLLALVALATLKV 320
|
|
| GT_WecA_like |
cd06853 |
This subfamily contains Escherichia coli WecA, Bacillus subtilis TagO and related proteins. ... |
49-270 |
1.14e-37 |
|
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: 134.92 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 49 TPTMGGTVFLIVALLVSLIFSIIlskeNSGNLGATFGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIAGLI 128
Cdd:cd06853 8 IPRLGGLAIFLGFLLALLLALLF----PFFLLPELLGLLAGATIIVLLGLLDDLF--------DLSPKVKLLGQILAALI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 129 FYFVHVLpSGTSAINIFGFYLEVGYLYAFFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLIIV 208
Cdd:cd06853 76 VVFGGGV-ILSLLGPFGGGIILLGWLSIPLTVLWIVGIINAINLIDGLDGLAGGVALIASLALAILALLNGQVLVALLAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446402165 209 IMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAISIALRQEW-------TLLFIGFVYVFETSSVML 270
Cdd:cd06853 155 ALAGALLGFLPYNFHPARIFMGDAGSLFLGFLLAVLSILGTQKSstaispvVPLLILAVPLFDTLFVII 223
|
|
| GT_MraY-like |
cd06499 |
Glycosyltransferase 4 (GT4) includes both eukaryotic and prokaryotic UDP-D-N-acetylhexosamine: ... |
48-245 |
2.12e-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: 118.94 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 48 GTPTMGGTVFLIVALLVSLIFSiilskenSGNLGATFGILSVVLIYGIIGFLDDFLKIFKqineGLTPKQKMSLQLIAGL 127
Cdd:cd06499 1 PTPTMGGLAILLGFLLGVLLYI-------PHSNTLILLALLSGLVAGIVGFIDDLLGLKV----ELSEREKLLLQILAAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 128 IFYFVHVLPsgTSAINIFGFYLEVGYLYAFFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLII 207
Cdd:cd06499 70 FLLLIGGGH--TTVTTPLGFVLDLGIFYIPFAIIAIVGATNAVNLIDGMDGLAAGISVIASIACALFALLSGQTTSALLF 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 446402165 208 VIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAIS 245
Cdd:cd06499 148 IILAGACLGFLYFNFYPAKIFMGDTGSYFLGAAYAAVA 185
|
|
| Glycos_transf_4 |
pfam00953 |
Glycosyl transferase family 4; |
84-248 |
9.94e-31 |
|
Glycosyl transferase family 4;
Pssm-ID: 460008 Cd Length: 158 Bit Score: 113.85 E-value: 9.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 84 FGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIAGLIFYFVHVLPSGTSAINIFGFYLEVGY-LYAFFVLFW 162
Cdd:pfam00953 1 LGLLLGALLIGLIGLIDDLL--------GLSARIKLLLQALAALILLVLGGIGLTSLGLPFGGGSLELGPwLSILLTLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 163 VVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLIIVIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLA 242
Cdd:pfam00953 73 IVGLTNAVNFIDGLDGLAGGVAIIAALALGIIAYLLGNLELALLSLALLGALLGFLPFNFYPAKIFMGDSGSLFLGFLLA 152
|
....*.
gi 446402165 243 AISIAL 248
Cdd:pfam00953 153 VLAIIG 158
|
|
| GT_WbpL_WbcO_like |
cd06854 |
The members of this subfamily catalyze the formation of a phosphodiester bond between a ... |
49-265 |
1.81e-28 |
|
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: 110.80 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 49 TPTMGGTVFLIVALLVSLIFSIILSkensGNLGATFGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIAG-L 127
Cdd:cd06854 15 TPRGGGIAFVLAFLLALLLAAAAGP----LNDLSYLLLLIGLLLLAAVGFIDDLR--------SLSPKIRLLVQLLAAaL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 128 IFYFVHVLPSgtsainiFGFYLEVGYLYAFFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLII 207
Cdd:cd06854 83 ALYALGPLTS-------LLLNFLPPWLIALLLLLAIVWIINLYNFMDGIDGLAGGEALVVFLALALLGYLAGEPALALLA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446402165 208 VIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAISIALRQE----WTLLFIGFVYVFET 265
Cdd:cd06854 156 LALAGALLGFLPFNWPPAKIFMGDVGSTFLGFLLAALLLLLALSgqspWAWLLLLSPFLVDA 217
|
|
| GT_GPT_archaea |
cd06856 |
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT)-like proteins in archaea. Eukaryotic GPT ... |
46-293 |
6.17e-26 |
|
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: 104.64 E-value: 6.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 46 KAGTPTMGGTVFLIVALLVSLIFSIILSKENSgnlgatFGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIA 125
Cdd:cd06856 10 KPEVPEMGGIAVLLGFSLGLLFLSALTHSVEA------LALLITSLLAGLIGLLDDIL--------GLSQSEKVLLTALP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 126 GLIFYFVHVlpsGTSAINIFGFYLEVGYLYA-FFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDIL 204
Cdd:cd06856 76 AIPLLVLKA---GNPLTSLPIGGRVLGILYYlLIVPLGITGASNAFNMLAGFNGLEAGMGIIILLALAIILLINGDYDAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 205 LIIVIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAISIALRQEWTLLFIGFVYVFEtssvmlqvAYFKYTKKKTGV 284
Cdd:cd06856 153 IIALILVAALLAFLLYNKYPAKVFPGDVGTLPIGALIGTIAVLGGLEIILLILLLPYVID--------FLLKLRSKGGGK 224
|
....*....
gi 446402165 285 GKRIFRMTP 293
Cdd:cd06856 225 EHREKPTKV 233
|
|
| GT_MraY_like |
cd06912 |
This subfamily is composed of uncharacterized bacterial glycosyltransferases in the MraY-like ... |
49-245 |
4.02e-21 |
|
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: 89.22 E-value: 4.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 49 TPTMGGtvfliVALLVSLIFSIILSKENSGNLgaTFGILSVVLIYGIIGFLDDflkifkqINEGLTPKQKMSLQLIAGLI 128
Cdd:cd06912 11 TPRIGG-----VAIFLGLLAGLLLLSLLSGSL--LLLLLLAALPAFLAGLLED-------ITKRVSPRIRLLATFLSALL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 129 FYFVHVLPSGTSAINIFGFYLEVGYLYAFFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLIIV 208
Cdd:cd06912 77 AVWLLGASITRLDLPGLDLLLSFPPFAIIFTIFAVAGVANAFNIIDGFNGLASGVAIISLLSLALVAFQVGDTDLAFLAL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 446402165 209 IMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAIS 245
Cdd:cd06912 157 LLAGALLGFLIFNFPFGKIFLGDGGAYLLGFLLAWLA 193
|
|
| GT_GPT_euk |
cd06855 |
UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) catalyzes the transfer of GlcNAc-1-P from ... |
19-246 |
1.58e-11 |
|
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: 63.80 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 19 IPRFIKFYQLKKIGGQQMHEDVKQHLAKAGTpTMGGTVFLIVALLVSLI--FSIILSKENSGNLGATFGILSVVLIygii 96
Cdd:cd06855 1 IPKFGPLFIKAGLYGIDLNKNGEEKIPESAG-LVPGIVFLIVLFLFIPFpfLKDFPHDKLVEYLSALLSICCMTFL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 97 GFLDDFLKifkqinegLTPKQKMSLQLIAGL---IFYFVH--VLPSGTSAINIFGFYLEVGYLYAFFVLFWVVGFSNAVN 171
Cdd:cd06855 76 GFADDVLD--------LRWRHKLILPTFASLpllMVYYGNtgITLPIVPLRPLLGTLIDLGILYYVYMILLAVFCTNSIN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 172 LTDGIDGL---ASISVVISLITYGII--------AYNQTQFDILLIIVIMIGALLGFFVFNHKPAKVFMGDVGSLALGAM 240
Cdd:cd06855 148 IYAGINGLevgQSLVIALSILLYNLLelngssgsMTLDAHLFSLYLLLPFIAVSLALLYYNWYPSKVFVGDTFTYFAGMV 227
|
....*.
gi 446402165 241 LAAISI 246
Cdd:cd06855 228 FAVVGI 233
|
|
| GT_GPT_like |
cd06851 |
This family includes eukaryotic UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase (GPT) and ... |
50-246 |
3.13e-11 |
|
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: 62.13 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 50 PTMGGT--VFLIVALLVSLIFSIILSKeNSGNLGATFGILSVVLIYGIIGFLDDFLkifkqineGLTPKQKMSLQLIAGL 127
Cdd:cd06851 14 PEPGGIsiLIGFVASEITLIFFPFLSF-PHFPISEILAALITSVLGFSVGIIDDRL--------TMGGWFKPVALAFAAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446402165 128 IFYFVHVLPSGTSAInIFGFYLEVGYLYAFFVLFWVVGFSNAVNLTDGIDGLASISVVISLITYGIIAYNQTQFDILLII 207
Cdd:cd06851 85 PILLLGAYDSNLDFP-LFGGSVKIPSLYLVLVVFMIVITGNAFNSIAGLNGVEAGFTTIISFALAISLLVQQNYEIGIAC 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 446402165 208 VIMIGALLGFFVFNHKPAKVFMGDVGSLALGAMLAAISI 246
Cdd:cd06851 164 LCLAFASLAFLYYNKYPSRIFPGDTGAYMFGATYAVVAI 202
|
|
| |
