|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-345 |
5.00e-144 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 412.22 E-value: 5.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 1 MLAVLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTG 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 81 KAKKWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtAPVTVTG 160
Cdd:COG0707 83 QARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPK-KKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 161 NPVRRSVIEADRAAGRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARpNLHIVHITGPKELDAVTKALAltDD 240
Cdd:COG0707 162 NPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYA--AA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 241 EARRWHLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFATADHQTTNARAWVESGAAFMMPDDELGSD 320
Cdd:COG0707 239 IRPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340
....*....|....*....|....*
gi 1976321855 321 EFKAKLFALIDDASVRESMVAAARA 345
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARA 343
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-345 |
6.31e-129 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 373.70 E-value: 6.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 1 MLAVLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTG 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 81 KAKKWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtAPVTVTG 160
Cdd:PRK00726 82 QARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFK-PKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 161 NPVRRSVIEADRAAGRamFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARPNlhIVHITGPKELDAVTKALALTDD 240
Cdd:PRK00726 161 NPVREEILALAAPPAR--LAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAYAAGIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 241 earrWHLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFATADHQTTNARAWVESGAAFMMPDDELGSD 320
Cdd:PRK00726 237 ----AEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPE 312
|
330 340
....*....|....*....|....*
gi 1976321855 321 EFKAKLFALIDDASVRESMVAAARA 345
Cdd:PRK00726 313 KLAEKLLELLSDPERLEAMAEAARA 337
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
4-345 |
1.87e-121 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 354.60 E-value: 1.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 4 VLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTGKAK 83
Cdd:cd03785 3 LIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 84 KWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtAPVTVTGNPV 163
Cdd:cd03785 83 KILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPA-AKVVVTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 164 RRSVIEADRAagRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARpNLHIVHITGPKELDAVTKALALTDDEAR 243
Cdd:cd03785 162 REEILNLRKE--LKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLGINVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 244 rwhLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFATADHQTTNARAWVESGAAFMMPDDELGSDEFK 323
Cdd:cd03785 239 ---VFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLA 315
|
330 340
....*....|....*....|..
gi 1976321855 324 AKLFALIDDASVRESMVAAARA 345
Cdd:cd03785 316 EAILDLLNDPERLKKMAEAAKK 337
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-344 |
3.20e-92 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273460 [Multi-domain] Cd Length: 348 Bit Score: 279.94 E-value: 3.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 1 MLAVLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTG 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 81 KAKKWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtapvTVTG 160
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHFEA----VLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 161 NPVRRSVIEADraAGRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARPNLhIVHITGPKELDAVTKALAltdd 240
Cdd:TIGR01133 157 NPVRKEIRSLP--VPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQ---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 241 EARRWHLLGYQDR-MGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFAtADHQTTNARAWVESGAAFMMPDDELGS 319
Cdd:TIGR01133 230 ELGQEKIVTFIDEnMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLP 308
|
330 340
....*....|....*....|....*
gi 1976321855 320 DEFKAKLFALIDDASVRESMVAAAR 344
Cdd:TIGR01133 309 EKLLEALLKLLLDPANLENMAEAAR 333
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-139 |
1.41e-37 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 132.03 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 4 VLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTGKAK 83
Cdd:pfam03033 2 VLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKAF 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1976321855 84 KWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAV 139
Cdd:pfam03033 82 RILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-345 |
5.00e-144 |
|
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 412.22 E-value: 5.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 1 MLAVLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTG 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 81 KAKKWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtAPVTVTG 160
Cdd:COG0707 83 QARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPK-KKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 161 NPVRRSVIEADRAAGRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARpNLHIVHITGPKELDAVTKALAltDD 240
Cdd:COG0707 162 NPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEA-RLQVVHQTGKGDYEEVRAAYA--AA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 241 EARRWHLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFATADHQTTNARAWVESGAAFMMPDDELGSD 320
Cdd:COG0707 239 IRPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340
....*....|....*....|....*
gi 1976321855 321 EFKAKLFALIDDASVRESMVAAARA 345
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARA 343
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-345 |
6.31e-129 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 373.70 E-value: 6.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 1 MLAVLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTG 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 81 KAKKWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtAPVTVTG 160
Cdd:PRK00726 82 QARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFK-PKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 161 NPVRRSVIEADRAAGRamFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARPNlhIVHITGPKELDAVTKALALTDD 240
Cdd:PRK00726 161 NPVREEILALAAPPAR--LAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEALQ--VIHQTGKGDLEEVRAAYAAGIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 241 earrWHLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFATADHQTTNARAWVESGAAFMMPDDELGSD 320
Cdd:PRK00726 237 ----AEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPE 312
|
330 340
....*....|....*....|....*
gi 1976321855 321 EFKAKLFALIDDASVRESMVAAARA 345
Cdd:PRK00726 313 KLAEKLLELLSDPERLEAMAEAARA 337
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
4-345 |
1.87e-121 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 354.60 E-value: 1.87e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 4 VLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTGKAK 83
Cdd:cd03785 3 LIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 84 KWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtAPVTVTGNPV 163
Cdd:cd03785 83 KILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPA-AKVVVTGNPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 164 RRSVIEADRAagRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARpNLHIVHITGPKELDAVTKALALTDDEAR 243
Cdd:cd03785 162 REEILNLRKE--LKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLER-GIQVIHQTGKGDYDEVKKLYEDLGINVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 244 rwhLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFATADHQTTNARAWVESGAAFMMPDDELGSDEFK 323
Cdd:cd03785 239 ---VFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVLA 315
|
330 340
....*....|....*....|..
gi 1976321855 324 AKLFALIDDASVRESMVAAARA 345
Cdd:cd03785 316 EAILDLLNDPERLKKMAEAAKK 337
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-344 |
3.20e-92 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273460 [Multi-domain] Cd Length: 348 Bit Score: 279.94 E-value: 3.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 1 MLAVLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTG 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 81 KAKKWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLGAtapvTVTG 160
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHFEA----VLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 161 NPVRRSVIEADraAGRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLARPNLhIVHITGPKELDAVTKALAltdd 240
Cdd:TIGR01133 157 NPVRKEIRSLP--VPRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQ-IVHQGGKGDLEKVKNVYQ---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 241 EARRWHLLGYQDR-MGETLAAADAIVSRAGATSLAEISALAIPALLVPYPFAtADHQTTNARAWVESGAAFMMPDDELGS 319
Cdd:TIGR01133 230 ELGQEKIVTFIDEnMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLP 308
|
330 340
....*....|....*....|....*
gi 1976321855 320 DEFKAKLFALIDDASVRESMVAAAR 344
Cdd:TIGR01133 309 EKLLEALLKLLLDPANLENMAEAAR 333
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
4-322 |
4.38e-50 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 171.19 E-value: 4.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 4 VLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTGKAK 83
Cdd:PRK12446 5 VFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVMDAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 84 KWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAVCVTYECSAESLgATAPVTVTGNPV 163
Cdd:PRK12446 85 VRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHL-PKEKVIYTGSPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 164 RRSVIEADRAAGRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLArpNLHIVHITGPKELDAvtkalALTDDEA- 242
Cdd:PRK12446 164 REEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPELLL--KYQIVHLCGKGNLDD-----SLQNKEGy 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 243 RRWHLLGyqDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYP-FATADHQTTNARAWVESGAAFMMPDDELGSDE 321
Cdd:PRK12446 237 RQFEYVH--GELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSkFASRGDQILNAESFERQGYASVLYEEDVTVNS 314
|
.
gi 1976321855 322 F 322
Cdd:PRK12446 315 L 315
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
4-139 |
1.41e-37 |
|
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.
Pssm-ID: 427107 [Multi-domain] Cd Length: 139 Bit Score: 132.03 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 4 VLSGGGTAGHINPALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTGKAK 83
Cdd:pfam03033 2 VLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKAF 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1976321855 84 KWFADIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLARRADAV 139
Cdd:pfam03033 82 RILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
187-347 |
2.22e-32 |
|
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.
Pssm-ID: 427711 [Multi-domain] Cd Length: 166 Bit Score: 118.97 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 187 MLLVFGGSLGARHINEAVVALKDELLARPNLHIVHITGPKELDAVTKALALTDDEArrwHLLGYQDRMGETLAAADAIVS 266
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGINY---EVFPFIDNMAEYIKAADLVIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 267 RAGATSLAEISALAIPALLVPYPFATADHQTTNARAWVESGAAFMMPDDELGSDEFKAKLFALIDDASVRESMVAAARAQ 346
Cdd:pfam04101 78 RAGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKAS 157
|
.
gi 1976321855 347 K 347
Cdd:pfam04101 158 G 158
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
2-348 |
1.52e-17 |
|
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340861 [Multi-domain] Cd Length: 364 Bit Score: 82.75 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 2 LAVLSGGGTAGHINPALALADELVSRG--WDVRF-----AGTPGgVESRLVPAAGIPFTAFEASG-FDRSHPASLAKGVA 73
Cdd:cd17507 1 VLILTASTGGGHIQAAQALKEAFREKFdnYEVIIedllkYSNPV-VNKILKRGEKLYKKAPTLYKlFYNLTSDRLNSISN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 74 KIAA-STGKAKKWFADIKPDVVVG--FGGYVCIPVARAAEKTGVPVV------------LHEQNSVAGMANKYLARRADA 138
Cdd:cd17507 80 KAARlGLKKLKELLREEQPDVIIStfPLMSALVELFKRKGLLPIPVYtvitdyvlhstwIHPEVDRYFVASEEVKRELVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 139 VCVTYEcsaeslgataPVTVTGNPVRRSVIEA-DRAAGRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDellARPNL 217
Cdd:cd17507 160 RGVTPS----------QIKVTGIPVRPSFAEVrDKDEARNELNLSPDKPTVLLMGGGGGMGPVKETVEALLD---SLRAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 218 HIVHITGPKEldAVTKALALTDDEARRWHLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVPYPfatADHQT 297
Cdd:cd17507 227 QVLVVCGKNK--KLYEKLSGLEEDYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDPI---PGQEE 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1976321855 298 TNARAWVESGAAFMMPDDElgsdEFKAKLFALIDDASVRESMVAAARAQKT 348
Cdd:cd17507 302 ENADFLENNGAGIIARDPE----ELLEIVARLIDPPSLLRMMSEAAKELKP 348
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
9-347 |
1.98e-13 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 69.50 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 9 GTAGHINPALALADELVSRGWDVRFAGTPGGVEsrLVPAAGIPFTAFeasgfdrshpaslakgvakiaastgkakkwfad 88
Cdd:COG1819 8 GGRGHVNPLLALARALRARGHEVTFATGPDFAD--LVEAAGLEFVDW--------------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 89 iKPDVVVgfGGYVCIPVARAAEKTGVPVVLHeqnSVAGMAnkyLARRADavcvtyecsaeslgaTAPVTVTGNPVRRSVI 168
Cdd:COG1819 53 -RPDLVV--SDPLALAAALAAEALGIPVVSL---TPPELE---YPRPPD---------------PANVRFVGPLLPDGPA 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 169 EADRAAGRAmfdlAEDDFMLLVFGGSLGARHINEAVVAlkdELLARPNLHIVHITGPKELDAVtkalaltDDEARRWHLL 248
Cdd:COG1819 109 ELPPWLEED----AGRPLVYVTLGTSANDRADLLRAVL---EALADLGVRVVVTTGGLDPAEL-------GPLPDNVRVV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 249 GYQDrMGETLAAADAIVSRAGATSLAEISALAIPALLVPYpfaTADhQTTNARAWVESGAAFMMPDDELGSDEFKAKLFA 328
Cdd:COG1819 175 DYVP-QDALLPRADAVVHHGGAGTTAEALRAGVPQVVVPF---GGD-QPLNAARVERLGAGLALPPRRLTAEALRAALRR 249
|
330
....*....|....*....
gi 1976321855 329 LIDDASVREsmvAAARAQK 347
Cdd:COG1819 250 LLADPSYRE---RAARLAA 265
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
153-336 |
1.94e-11 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 64.87 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 153 TAPVTVTGNpVRRSVIEADRAAGRAMFDLAEDDFML-LVFGGSLGARHINEAVVALkdELLARPNLHIVHITGPKELDAV 231
Cdd:COG4671 186 ADKVRYTGY-VARPAPEPPPEERDALGLLPEEPLILvSAGGGGDGAELLEAALAAA--ELLPPPDHRWLLVTGPFMPAAD 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 232 TKALALTDDEARRWHLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLVpyPFATAD-HQTTNARAWVESGAAF 310
Cdd:COG4671 263 RAALRARAAALPNVTVERFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIV--PRTAPRtEQLIRAERLAELGLVD 340
|
170 180
....*....|....*....|....*.
gi 1976321855 311 MMPDDELGSDEFKAKLFALIDDASVR 336
Cdd:COG4671 341 VLHPEDLTPEALARAIAAALARPPRR 366
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
156-332 |
1.41e-10 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 62.05 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 156 VTVTGNPVRRSVIEA-DRAAGRAMFDLAEDDFMLLVFGGSLGarhINEAVVALKDELLARPNLHIVHITGPKEldAVTKA 234
Cdd:PRK13609 172 VVETGIPIRSSFELKiNPDIIYNKYQLCPNKKILLIMAGAHG---VLGNVKELCQSLMSVPDLQVVVVCGKNE--ALKQS 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 235 LA-LTDDEARRWHLLGYQDRMGETLAAADAIVSRAGATSLAEISALAIPALLV-PYPfataDHQTTNARAWVESGAAFMM 312
Cdd:PRK13609 247 LEdLQETNPDALKVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKGAAVVI 322
|
170 180
....*....|....*....|
gi 1976321855 313 PDDElgsdEFKAKLFALIDD 332
Cdd:PRK13609 323 RDDE----EVFAKTEALLQD 338
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
9-347 |
1.61e-10 |
|
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.
Pssm-ID: 340817 [Multi-domain] Cd Length: 404 Bit Score: 61.80 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 9 GTAGHINPALALADELVSRGWDVRFAGTPGGVESRlVPAAGIPFTAFEASGFDRSHPASLAKGVAKIAASTGKAKKWFAD 88
Cdd:cd03784 9 PGQGHVNPMLPLAKALAARGHEVTVATPPFNFADL-VEAAGLTFVPVGDDPDELELDSETNLGPDSLLELLRRLLKAADE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 89 I------------KPDVVVgfGGYVCIPVARAAEKTGVPVVLHeQNSVAGMANKYLARRADAVCVTYECSAESLGATAPV 156
Cdd:cd03784 88 LlddllaalrsswKPDLVI--ADPFAYAGPLVAEELGIPSVRL-FTGPATLLSAYLHPFGVLNLLLSSLLEPELFLDPLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 157 TV-------------TGNPVRRSVIEADRAAGRAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDELLA----RPNLHI 219
Cdd:cd03784 165 EVldrlrerlglppfSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSVLGGLRIVPKNGPLPDELWEWLDkqppRSVVYV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 220 -----VHITGPKELDAVTKALALTDDE---ARRWHLLGYQDRMGET------------LA--AADAIVSRAGATSLAEIS 277
Cdd:cd03784 245 sfgsmVRDLPEELLELIAEALASLGQRflwVVGPDPLGGLERLPDNvlvvkwvpqdelLAhpAVGAFVTHGGWNSTLEAL 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 278 ALAIPALLVPYpfaTADhQTTNARAWVESGAAFMMPDDELGSDEFKAKLFALIDDASVREsmvAAARAQK 347
Cdd:cd03784 325 YAGVPMVVVPL---FAD-QPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRR---AAELLAE 387
|
|
| MGT |
TIGR01426 |
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) ... |
11-337 |
7.26e-09 |
|
glycosyltransferase, MGT family; This model describes the MGT (macroside glycosyltransferase) subfamily of the UDP-glucuronosyltransferase family. Members include a number of glucosyl transferases for macrolide antibiotic inactivation, but also include transferases of glucose-related sugars for macrolide antibiotic production. [Cellular processes, Toxin production and resistance]
Pssm-ID: 273616 [Multi-domain] Cd Length: 392 Bit Score: 57.00 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 11 AGHINPALALADELVSRGWDVRFAGTPGGVESrlVPAAGIPF----TAFEASGFDR-SHPASLAKGVAKIAASTGKA--- 82
Cdd:TIGR01426 6 HGHVNPTLGVVEELVARGHRVTYATTEEFAER--VEAAGAEFvlygSALPPPDNPPeNTEEEPIDIIEKLLDEAEDVlpq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 83 -KKWFADIKPDVVVgfGGYVCIPVARAAEKTGVPVV-----------LHEQNSVAGMANKYLARRADAVCVTYECSAESL 150
Cdd:TIGR01426 84 lEEAYKGDRPDLIV--YDIASWTGRLLARKWDVPVIssfptfaaneeFEEMVSPAGEGSAEEGAIAERGLAEYVARLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 151 ----GATAPVTVTGNPVRR----------SVIEADR----------AAGRAMFDLA-----EDDFMLLVFGGSLGARH-- 199
Cdd:TIGR01426 162 leehGITTPPVEFLAAPRRdlnlvytpkaFQPAGETfddsftfvgpCIGDRKEDGSwerpgDGRPVVLISLGTVFNNQps 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 200 -INEAVVALKDEllarpNLHIVHITG----PKELDAVTKALaltddEARRW--HLlgyqdrmgETLAAADAIVSRAGATS 272
Cdd:TIGR01426 242 fYRTCVEAFRDL-----DWHVVLSVGrgvdPADLGELPPNV-----EVRQWvpQL--------EILKKADAFITHGGMNS 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1976321855 273 LAEISALAIPALLVPypfATADhQTTNARAWVESGAAFMMPDDELGSDEFKAKLFALIDDASVRE 337
Cdd:TIGR01426 304 TMEALFNGVPMVAVP---QGAD-QPMTARRIAELGLGRHLPPEEVTAEKLREAVLAVLSDPRYAE 364
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
8-345 |
1.39e-08 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 56.01 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 8 GGTAGHInpaLALADELVSRGWDVRFAgTPGGVESRLVPAAGIPFTAFEASGFDRSHPASLAKgvakiaastgKAKKWFA 87
Cdd:cd03801 14 GGAERHV---RELARALAARGHDVTVL-TPADPGEPPEELEDGVIVPLLPSLAALLRARRLLR----------ELRPLLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 88 DIKPDVVVGFGGYVCIPVARAAEKTGVPVVLHEQNSVAGMANKYLA-------------RRADAVCVTYECSAESLGAT- 153
Cdd:cd03801 80 LRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAaerrllaraeallRRADAVIAVSEALRDELRALg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 154 ----APVTVTGNPVRrsvIEADRAAGRAMFDLAEDDFMLLVFgGSLGARH-INEAVVALKDELLARPN--LHIVHITGPK 226
Cdd:cd03801 160 gippEKIVVIPNGVD---LERFSPPLRRKLGIPPDRPVLLFV-GRLSPRKgVDLLLEALAKLLRRGPDvrLVIVGGDGPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 227 ELDAVTKALALTDdearRWHLLGY--QDRMGETLAAADAIV--SRAGATSLAEISALAIPALLVpypfATAdhqTTNARA 302
Cdd:cd03801 236 RAELEELELGLGD----RVRFLGFvpDEELPALYAAADVFVlpSRYEGFGLVVLEAMAAGLPVV----ATD---VGGLPE 304
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1976321855 303 WVESGAAFMMPDDELgSDEFKAKLFALIDDASVRESMVAAARA 345
Cdd:cd03801 305 VVEDGEGGLVVPPDD-VEALADALLRLLADPELRARLGRAARE 346
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
17-152 |
6.78e-08 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 51.63 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 17 ALALADELVSRGWDVRFAGTPGGVESRLVPAAGIPFTAFEAsGFDRSHPASLAkgvakiaaSTGKAKKWFADIKPDVVVG 96
Cdd:pfam13579 7 VLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPV-PPRPSPLADLA--------ALRRLRRLLRAERPDVVHA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1976321855 97 FGGYVCIPVARAAEKTGVPVVLHEQN-----------SVAGMANKYLARRADAVCVTYECSAESLGA 152
Cdd:pfam13579 78 HSPTAGLAARLARRRRGVPLVVTVHGlaldygsgwkrRLARALERRLLRRADAVVVVSEAEAELLRA 144
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
158-285 |
1.15e-05 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 46.89 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 158 VTGNPVRRSVIEADRAAG--RAMFDLAEDDFMLLVFGGSLGARHINEAVVALKDEL----LARPNLHIVHITGPkeldav 231
Cdd:PLN02605 177 VYGLPIRPSFARAVRPKDelRRELGMDEDLPAVLLMGGGEGMGPLEETARALGDSLydknLGKPIGQVVVICGR------ 250
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1976321855 232 TKALALTDdEARRWHLL----GYQDRMGETLAAADAIVSRAGATSLAEISALAIPALL 285
Cdd:PLN02605 251 NKKLQSKL-ESRDWKIPvkvrGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIIL 307
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
77-345 |
1.22e-03 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 40.40 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 77 ASTGKAKKWFADIKPDVVVGFGGY--VCIPVARAAEKTGVPVVLH-----EQNSVA-------------GMANKYLARRA 136
Cdd:cd03794 85 ALAALLKLLVREERPDVIIAYSPPitLGLAALLLKKLRGAPFILDvrdlwPESLIAlgvlkkgsllkllKKLERKLYRLA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 137 DAVCVTYECSAESLGATApvtVTGNPVrrSVIE--------ADRAAGRAMFDLAEDDFMLLVFGGSLG-ARHInEAVVAL 207
Cdd:cd03794 165 DAIIVLSPGLKEYLLRKG---VPKEKI--IVIPnwadleefKPPPKDELRKKLGLDDKFVVVYAGNIGkAQGL-ETLLEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 208 KDELLARPNLHIVHI---TGPKELDAVTKALALTDDearrwHLLGYQ--DRMGETLAAADA-IVSRA-----GATS---L 273
Cdd:cd03794 239 AERLKRRPDIRFLFVgdgDEKERLKELAKARGLDNV-----TFLGRVpkEEVPELLSAADVgLVPLKdnpanRGSSpskL 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1976321855 274 AEISALAIPALlvpypfATADhqTTNARAWVESGAAFMMPDDElgSDEFKAKLFALIDDASVRESMVAAARA 345
Cdd:cd03794 314 FEYMAAGKPIL------ASDD--GGSDLAVEINGCGLVVEPGD--PEALADAILELLDDPELRRAMGENGRE 375
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
81-281 |
8.11e-03 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 38.07 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 81 KAKKWFADIKPDVV--VGFGGYVCIPVArAAEKTGVPVVLHEQNSV-----AGMANKYLARRADAVCVTYECSAESL--- 150
Cdd:cd03807 70 RLAKLIRKRNPDVVhtWMYHADLIGGLA-AKLAGGVKVIWSVRSSNipqrlTRLVRKLCLLLSKFSPATVANSSAVAefh 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1976321855 151 ---GATAPVTVT----GNPVRRSVIEADRAAGRAMFDLAEDDFMLlvfgGSLGARH----INEAVVALKDELLARPNLHI 219
Cdd:cd03807 149 qeqGYAKNKIVViyngIDLFKLSPDDASRARARRRLGLAEDRRVI----GIVGRLHpvkdHSDLLRAAALLVETHPDLRL 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1976321855 220 VHI-TGP--KELDAVTKALALTDdearRWHLLGYQDRMGETLAAADAIV--SRAGATSLAEISALAI 281
Cdd:cd03807 225 LLVgRGPerPNLERLLLELGLED----RVHLLGERSDVPALLPAMDIFVlsSRTEGFPNALLEAMAC 287
|
|
| |
