|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-365 |
1.15e-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: 413.76 E-value: 1.15e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTT 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 81 LARRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAAEALAdKSRVRVTG 160
Cdd:COG0707 83 QARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFP-KKKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 161 NPVRESVFSATREQGRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDGLLAyGDLHIVQVTGPKELDAVREQLALSPe 240
Cdd:COG0707 162 NPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLE-ARLQVVHQTGKGDYEEVRAAYAAAI- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 241 qQARWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATEDHQTMNAQACVEAGAAYLVADADVEGP 320
Cdd:COG0707 240 -RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 506241181 321 EFARKLRELIEDEDVRARMAAAARAQKTRDAAGLLADAVMEAARA 365
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-365 |
2.24e-127 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 369.84 E-value: 2.24e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTT 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 81 LARRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAAEAlADKSRVRVTG 160
Cdd:PRK00726 82 QARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPE-FFKPKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 161 NPVRESVFSATREqgRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDGLLAYgdLHIVQVTGPKELDAVREQLALSPE 240
Cdd:PRK00726 161 NPVREEILALAAP--PARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEA--LQVIHQTGKGDLEEVRAAYAAGIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 241 qqarWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATEDHQTMNAQACVEAGAAYLVADADVEGP 320
Cdd:PRK00726 237 ----AEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 506241181 321 EFARKLRELIEDEDVRARMAAAARAQKTRDAAGLLADAVMEAARA 365
Cdd:PRK00726 313 KLAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-357 |
3.10e-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: 353.83 E-value: 3.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 3 IVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTTLA 82
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 83 RRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAAEaLADKSRVRVTGNP 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKK-YFPAAKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 163 VRESVFSATREqgRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDgLLAYGDLHIVQVTGPKELDAVREQLalsPEQQ 242
Cdd:cd03785 161 VREEILNLRKE--LKRFGLPPDKPTLLVFGGSQGARAINRAVPKALP-KLLERGIQVIHQTGKGDYDEVKKLY---EDLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 243 ARWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATEDHQTMNAQACVEAGAAYLVADADVEGPEF 322
Cdd:cd03785 235 INVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330 340 350
....*....|....*....|....*....|....*
gi 506241181 323 ARKLRELIEDEDVRARMAAAARAQKTRDAAGLLAD 357
Cdd:cd03785 315 AEAILDLLNDPERLKKMAEAAKKLAKPDAAERIAD 349
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-359 |
1.70e-86 |
|
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: 265.31 E-value: 1.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTT 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 81 LARRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAaealADKSRVRVTG 160
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGA----KDHFEAVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 161 NPVRESVFSATReqGRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDgLLAYGDLHIVQVTGPKELDAVREqlALSPE 240
Cdd:TIGR01133 157 NPVRKEIRSLPV--PRERFGRREGKPTILVLGGSQGAKILNELVPKALA-KLQEKGIQIVHQGGKGDLEKVKN--VYQEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 241 QQARWQLLGYTDhMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATeDHQTMNAQACVEAGAAYLVADADVEGP 320
Cdd:TIGR01133 232 GQEKIVTFIDEN-MAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAA-DDQYYNAKFLEDLGAGLVIRQKELLPE 309
|
330 340 350
....*....|....*....|....*....|....*....
gi 506241181 321 EFARKLRELIEDEDVRARMAAAARAQKTRDAAGLLADAV 359
Cdd:TIGR01133 310 KLLEALLKLLLDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
3-139 |
9.76e-41 |
|
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: 140.12 E-value: 9.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 3 IVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTTLA 82
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 506241181 83 RRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAV 139
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-365 |
1.15e-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: 413.76 E-value: 1.15e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTT 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERGAEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 81 LARRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAAEALAdKSRVRVTG 160
Cdd:COG0707 83 QARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFP-KKKAVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 161 NPVRESVFSATREQGRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDGLLAyGDLHIVQVTGPKELDAVREQLALSPe 240
Cdd:COG0707 162 NPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLE-ARLQVVHQTGKGDYEEVRAAYAAAI- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 241 qQARWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATEDHQTMNAQACVEAGAAYLVADADVEGP 320
Cdd:COG0707 240 -RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 506241181 321 EFARKLRELIEDEDVRARMAAAARAQKTRDAAGLLADAVMEAARA 365
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-365 |
2.24e-127 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 369.84 E-value: 2.24e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTT 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELKKRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKGVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 81 LARRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAAEAlADKSRVRVTG 160
Cdd:PRK00726 82 QARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPE-FFKPKAVVTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 161 NPVRESVFSATREqgRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDGLLAYgdLHIVQVTGPKELDAVREQLALSPE 240
Cdd:PRK00726 161 NPVREEILALAAP--PARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPEA--LQVIHQTGKGDLEEVRAAYAAGIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 241 qqarWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATEDHQTMNAQACVEAGAAYLVADADVEGP 320
Cdd:PRK00726 237 ----AEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 506241181 321 EFARKLRELIEDEDVRARMAAAARAQKTRDAAGLLADAVMEAARA 365
Cdd:PRK00726 313 KLAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
3-357 |
3.10e-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: 353.83 E-value: 3.10e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 3 IVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTTLA 82
Cdd:cd03785 2 ILIAGGGTGGHIFPALALAEELRKRGAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGLRQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 83 RRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAAEaLADKSRVRVTGNP 162
Cdd:cd03785 82 RKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKK-YFPAAKVVVTGNP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 163 VRESVFSATREqgRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDgLLAYGDLHIVQVTGPKELDAVREQLalsPEQQ 242
Cdd:cd03785 161 VREEILNLRKE--LKRFGLPPDKPTLLVFGGSQGARAINRAVPKALP-KLLERGIQVIHQTGKGDYDEVKKLY---EDLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 243 ARWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATEDHQTMNAQACVEAGAAYLVADADVEGPEF 322
Cdd:cd03785 235 INVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330 340 350
....*....|....*....|....*....|....*
gi 506241181 323 ARKLRELIEDEDVRARMAAAARAQKTRDAAGLLAD 357
Cdd:cd03785 315 AEAILDLLNDPERLKKMAEAAKKLAKPDAAERIAD 349
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-359 |
1.70e-86 |
|
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: 265.31 E-value: 1.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTT 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 81 LARRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAaealADKSRVRVTG 160
Cdd:TIGR01133 81 KARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGA----KDHFEAVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 161 NPVRESVFSATReqGRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDgLLAYGDLHIVQVTGPKELDAVREqlALSPE 240
Cdd:TIGR01133 157 NPVRKEIRSLPV--PRERFGRREGKPTILVLGGSQGAKILNELVPKALA-KLQEKGIQIVHQGGKGDLEKVKN--VYQEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 241 QQARWQLLGYTDhMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFATeDHQTMNAQACVEAGAAYLVADADVEGP 320
Cdd:TIGR01133 232 GQEKIVTFIDEN-MAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYAA-DDQYYNAKFLEDLGAGLVIRQKELLPE 309
|
330 340 350
....*....|....*....|....*....|....*....
gi 506241181 321 EFARKLRELIEDEDVRARMAAAARAQKTRDAAGLLADAV 359
Cdd:TIGR01133 310 KLLEALLKLLLDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
3-329 |
6.00e-46 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 160.41 E-value: 6.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 3 IVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTTLA 82
Cdd:PRK12446 4 IVFTGGGSAGHVTPNLAIIPYLKEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGVMDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 83 RRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAVCLTYEHAAEALADKSRVrVTGNP 162
Cdd:PRK12446 84 YVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVI-YTGSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 163 VRESVFSATREQGRARFGVPEGARMLLVTGGSLGARHLNQAV-AALKDGLLAYgdlHIVQVTGPKELDAVREQLalspEQ 241
Cdd:PRK12446 163 VREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVrEALPELLLKY---QIVHLCGKGNLDDSLQNK----EG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 242 QARWQLLGytDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFP-FATEDHQTMNAQACVEAGAAYLVADADVEGP 320
Cdd:PRK12446 236 YRQFEYVH--GELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPLSkFASRGDQILNAESFERQGYASVLYEEDVTVN 313
|
....*....
gi 506241181 321 EFARKLREL 329
Cdd:PRK12446 314 SLIKHVEEL 322
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
3-139 |
9.76e-41 |
|
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: 140.12 E-value: 9.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 3 IVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLTLPKAVLTIQKSTTLA 82
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIVKA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 506241181 83 RRWFDEIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKRAAAV 139
Cdd:pfam03033 81 FRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKV 137
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
187-355 |
1.10e-33 |
|
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: 122.44 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 187 MLLVTGGSLGARHLNQAVAALKDGLLAYGDLHIVQVTGPKELDAVREQLALSPEQqarWQLLGYTDHMGDAMAAADIVVS 266
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLELKGELQVLHQTGKGDLEEVKIDYAELGIN---YEVFPFIDNMAEYIKAADLVIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 267 RAGATSLAEISARALPALLVPFPFATEDHQTMNAQACVEAGAAYLVADADVEGPEFARKLRELIEDEDVRARMAAAARAQ 346
Cdd:pfam04101 78 RAGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKAS 157
|
....*....
gi 506241181 347 KTRDAAGLL 355
Cdd:pfam04101 158 GFKDAAKRL 166
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
142-333 |
5.74e-17 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 81.44 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 142 TYEHAAEaLADKsrVRVTGNpVRESVFSATREqGRARFGVPEGARMLLVT--GGSLGARHLNQAVAALKdgLLAYGDLHI 219
Cdd:COG4671 178 SFPLPAE-IADK--VRYTGY-VARPAPEPPPE-ERDALGLLPEEPLILVSagGGGDGAELLEAALAAAE--LLPPPDHRW 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 220 VQVTGPKELDAVREQLALSPEQQARWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPfATEDHQTMN 299
Cdd:COG4671 251 LLVTGPFMPAADRAALRARAAALPNVTVERFTPDFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRT-APRTEQLIR 329
|
170 180 190
....*....|....*....|....*....|....
gi 506241181 300 AQACVEAGAAYLVADADVEGPEFARKLRELIEDE 333
Cdd:COG4671 330 AERLAELGLVDVLHPEDLTPEALARAIAAALARP 363
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
3-335 |
7.71e-17 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 79.51 E-value: 7.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 3 IVLSGGGTAGHINPALALADVLKQRGCEVRFAGTPTGveARLVREAGIPFTpfeaqgfnrnhpltlpkavltiqksttla 82
Cdd:COG1819 2 ILFVTLGGRGHVNPLLALARALRARGHEVTFATGPDF--ADLVEAAGLEFV----------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 83 rrwfdEIQPDAVVGfgGYVCIPVARAAEQRGIPVVVHeqnsvmgmankylakraaavcLTYEHAAEALADKSRVRVTGnp 162
Cdd:COG1819 51 -----DWRPDLVVS--DPLALAAALAAEALGIPVVSL---------------------TPPELEYPRPPDPANVRFVG-- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 163 vreSVFSATREQGRARFGVPEGARMLLVTGGSL---GARHLNQAVAALKDGllaygDLHIVQVTGPKELDAVREQlalsp 239
Cdd:COG1819 101 ---PLLPDGPAELPPWLEEDAGRPLVYVTLGTSandRADLLRAVLEALADL-----GVRVVVTTGGLDPAELGPL----- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 240 eqQARWQLLGYTDHMgDAMAAADIVVSRAGATSLAEISARALPALLVPFPFatedHQTMNAQACVEAGAAYLVADADVEG 319
Cdd:COG1819 168 --PDNVRVVDYVPQD-ALLPRADAVVHHGGAGTTAEALRAGVPQVVVPFGG----DQPLNAARVERLGAGLALPPRRLTA 240
|
330
....*....|....*.
gi 506241181 320 PEFARKLRELIEDEDV 335
Cdd:COG1819 241 EALRAALRRLLADPSY 256
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
2-309 |
1.34e-16 |
|
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: 80.05 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 2 LIVLSGGGTAGHINPALALADVLKQRG--CEVRF-----AGTPTgVEARLVReaGIPFTPFEAQGFNRNHPLTLPKAVLT 74
Cdd:cd17507 1 VLILTASTGGGHIQAAQALKEAFREKFdnYEVIIedllkYSNPV-VNKILKR--GEKLYKKAPTLYKLFYNLTSDRLNSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 75 IQKSTTLARRWFD----EIQPDAVVG--FGGYVCIPVARAAEQRGIPVV------------VHEQNsvmgmaNKYLakra 136
Cdd:cd17507 78 SNKAARLGLKKLKellrEEQPDVIIStfPLMSALVELFKRKGLLPIPVYtvitdyvlhstwIHPEV------DRYF---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 137 aavCLTYEHAAEALAD---KSRVRVTGNPVRESvFSATR--EQGRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDGL 211
Cdd:cd17507 148 ---VASEEVKRELVERgvtPSQIKVTGIPVRPS-FAEVRdkDEARNELNLSPDKPTVLLMGGGGGMGPVKETVEALLDSL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 212 LAYgdlHIVQVTGPKEldAVREQLALSPEQQARWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLVPFPFA 291
Cdd:cd17507 224 RAG---QVLVVCGKNK--KLYEKLSGLEEDYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDPIPG 298
|
330
....*....|....*...
gi 506241181 292 TEDHqtmNAQACVEAGAA 309
Cdd:cd17507 299 QEEE---NADFLENNGAG 313
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
1-333 |
5.00e-12 |
|
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: 66.81 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIVLSGGGTAGHINPALALADVLKQRGCEVRFAgTPTGVEARLVREAGIPFTP-----------FEAQGFNRNHPLTLP 69
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARGHEVTVA-TPPFNFADLVEAAGLTFVPvgddpdeleldSETNLGPDSLLELLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 70 KAVLTIQKSTT-LARRWFDEIQPDAVVgfGGYVCIPVARAAEQRGIPVVVHeqnSVMgmankylakrAAAVCLTYEHAAE 148
Cdd:cd03784 80 RLLKAADELLDdLLAALRSSWKPDLVI--ADPFAYAGPLVAEELGIPSVRL---FTG----------PATLLSAYLHPFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 149 ALADKSRVRVTGNPVRESVFSATREQgRARFGVPEGARMLLVTGGSLGARHLNQAVAALKDGLLAYGDLHIVQVTGPKEL 228
Cdd:cd03784 145 VLNLLLSSLLEPELFLDPLLEVLDRL-RERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSVLGGLRIVPKNG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 229 DAVRE--------------------QLALSPEQQAR--WQLLGYTDH-----MGDAMAAADI------------------ 263
Cdd:cd03784 224 PLPDElwewldkqpprsvvyvsfgsMVRDLPEELLEliAEALASLGQrflwvVGPDPLGGLErlpdnvlvvkwvpqdell 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241181 264 -------VVSRAGATSLAEISARALPALLVPFpFAteDhQTMNAQACVEAGAAYLVADADVEGPEFARKLRELIEDE 333
Cdd:cd03784 304 ahpavgaFVTHGGWNSTLEALYAGVPMVVVPL-FA--D-QPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDE 376
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
154-361 |
1.05e-09 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 59.35 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 154 SRVRVTGNPVRESvFSATREQGR--ARFGVPEGARMLLVTGGSLGARhlnQAVAALKDGLLAYGDLHIVQVTGPKEldAV 231
Cdd:PRK13609 170 EQVVETGIPIRSS-FELKINPDIiyNKYQLCPNKKILLIMAGAHGVL---GNVKELCQSLMSVPDLQVVVVCGKNE--AL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 232 REQLALSPEQQA-RWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPALLV-PFPfateDHQTMNAQACVEAGAA 309
Cdd:PRK13609 244 KQSLEDLQETNPdALKVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKGAA 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506241181 310 YLVADADvegpEFARKLRELIEDEDVRARMAAAARAQKTRDAAGLLADAVME 361
Cdd:PRK13609 320 VVIRDDE----EVFAKTEALLQDDMKLLQMKEAMKSLYLPEPADHIVDDILA 367
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
8-334 |
5.36e-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: 54.08 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 8 GGTAGHInpaLALADVLKQRGCEVRFAGTPTGvearlvreagiPFTPFEAQGFNRNHPLTLPKAVLTIQKSTTLARRWFD 87
Cdd:cd03801 14 GGAERHV---RELARALAARGHDVTVLTPADP-----------GEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 88 EIQPDAVVGFGGYVCIPVARAAEQRGIPVVVHEQNSVMGMANKYLAKR--------------AAAVCLTYEHAAEALA-- 151
Cdd:cd03801 80 LRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAErrllaraeallrraDAVIAVSEALRDELRAlg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 152 --DKSRVRVTGNPVRESVFSATReqgRARFGVPEGARMLLVTGgSL----GARHLNQAVAALKDGLLAYgDLHIVQVTGP 225
Cdd:cd03801 160 giPPEKIVVIPNGVDLERFSPPL---RRKLGIPPDRPVLLFVG-RLsprkGVDLLLEALAKLLRRGPDV-RLVIVGGDGP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 226 KELDAVREQLALSPeqqaRWQLLGYTDH--MGDAMAAADIVVsragatslaeisaraLPALLVPFPFATedhqtMNAQAC 303
Cdd:cd03801 235 LRAELEELELGLGD----RVRFLGFVPDeeLPALYAAADVFV---------------LPSRYEGFGLVV-----LEAMAA 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 506241181 304 ---------------VEAGAAYLVADADVEgPEFARKLRELIEDED 334
Cdd:cd03801 291 glpvvatdvgglpevVEDGEGGLVVPPDDV-EALADALLRLLADPE 335
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
128-285 |
5.93e-08 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 53.82 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 128 ANKYLAKRAAAVCLtyehaaealaDKSRVRVTGNPVRESVFSATREQGRAR--FGVPEGARMLLVTGGSLGARHLNQAVA 205
Cdd:PLN02605 157 PSEEVAKRALKRGL----------EPSQIRVYGLPIRPSFARAVRPKDELRreLGMDEDLPAVLLMGGGEGMGPLEETAR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 206 ALKDGLLAYG----DLHIVQVTGpkeldavREQLALSPEQQARW----QLLGYTDHMGDAMAAADIVVSRAGATSLAEIS 277
Cdd:PLN02605 227 ALGDSLYDKNlgkpIGQVVVICG-------RNKKLQSKLESRDWkipvKVRGFVTNMEEWMGACDCIITKAGPGTIAEAL 299
|
....*...
gi 506241181 278 ARALPALL 285
Cdd:PLN02605 300 IRGLPIIL 307
|
|
| Glyco_trans_4_4 |
pfam13579 |
Glycosyl transferase 4-like domain; |
17-162 |
2.97e-07 |
|
Glycosyl transferase 4-like domain;
Pssm-ID: 433325 [Multi-domain] Cd Length: 158 Bit Score: 49.71 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 17 ALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGfnRNHPLTLPKAVLTIqksttlaRRWFDEIQPDAVVG 96
Cdd:pfam13579 7 VLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPP--RPSPLADLAALRRL-------RRLLRAERPDVVHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 97 FGGYVCIPVARAAEQRGIPVVVHEQN-----------SVMGMANKYLAKRAAAVCLTYEHAAEALA----DKSRVRVTGN 161
Cdd:pfam13579 78 HSPTAGLAARLARRRRGVPLVVTVHGlaldygsgwkrRLARALERRLLRRADAVVVVSEAEAELLRalgvPAARVVVVPN 157
|
.
gi 506241181 162 P 162
Cdd:pfam13579 158 G 158
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
8-332 |
1.60e-06 |
|
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.
Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 49.28 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 8 GGTAGHInpaLALADVLKQRGCEVRFAGT-PTGVEARLVREAGIPFTPFEaqgfnrnhPLTLPKAVLTIQKsttLARRWf 86
Cdd:cd03819 11 GGAETYI---LDLARALAERGHRVLVVTAgGPLLPRLRQIGIGLPGLKVP--------LLRALLGNVRLAR---LIRRE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 87 deiQPDAV-VGFGGYVCIPvARAAEQRGIPVVVHEQNSV-MGMANKYLAK-------RAAAVC-LTYEHAAEAL-ADKSR 155
Cdd:cd03819 76 ---RIDLIhAHSRAPAWLG-WLASRLTGVPLVTTVHGSYlATYHPKDFALavrargdRVIAVSeLVRDHLIEALgVDPER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 156 VRVTGNPVRESVFSATREQG-RARFGVPEGARMLLVTG---GSLGARHLNQAVAALKDGLlaygDLHIVQVTGPKELDAV 231
Cdd:cd03819 152 IRVIPNGVDTDRFPPEAEAEeRAQLGLPEGKPVVGYVGrlsPEKGWLLLVDAAAELKDEP----DFRLLVAGDGPERDEI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 232 REQLALSPEQQaRWQLLGYTDHMGDAMAAADIVVSragaTSLAEISAR-ALPALLVPFPFATEDHqtmNAQA-CVEAGAA 309
Cdd:cd03819 228 RRLVERLGLRD-RVTFTGFREDVPAALAASDVVVL----PSLHEEFGRvALEAMACGTPVVATDV---GGAReIVVHGRT 299
|
330 340
....*....|....*....|....
gi 506241181 310 -YLVADADVEgpEFARKLRELIED 332
Cdd:cd03819 300 gLLVPPGDAE--ALADAIRAAKLL 321
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
83-334 |
7.83e-06 |
|
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: 47.31 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 83 RRWFDEIQPDAV--VGFGGYVCIPVArAAEQRGIPVV------VHEQNSVMGMA--NKYLAKRAAAVCLTYEHAAEALA- 151
Cdd:cd03807 72 AKLIRKRNPDVVhtWMYHADLIGGLA-AKLAGGVKVIwsvrssNIPQRLTRLVRklCLLLSKFSPATVANSSAVAEFHQe 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 152 ---DKSRVRVTGNPVRESVFSAT---REQGRARFGVPEGARMLlvtgGSLGA-----RHLN--QAVAALKDgllAYGDLH 218
Cdd:cd03807 151 qgyAKNKIVVIYNGIDLFKLSPDdasRARARRRLGLAEDRRVI----GIVGRlhpvkDHSDllRAAALLVE---THPDLR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 219 IVQV-TGPKELDAVREQLALSPEqqARWQLLGYTDHMGDAMAAADIVVSragaTSLAE-ISARALPALLVPFPFATEDHQ 296
Cdd:cd03807 224 LLLVgRGPERPNLERLLLELGLE--DRVHLLGERSDVPALLPAMDIFVL----SSRTEgFPNALLEAMACGLPVVATDVG 297
|
250 260 270
....*....|....*....|....*....|....*...
gi 506241181 297 tmNAQACVEAGAAYLVADADVEGpeFARKLRELIEDED 334
Cdd:cd03807 298 --GAAELVDDGTGFLVPAGDPQA--LADAIRALLEDPE 331
|
|
| GT4_GT28_WabH-like |
cd03811 |
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
1-365 |
2.58e-05 |
|
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.
Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 45.81 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 1 MLIV---LSGGGTAghiNPALALADVLKQRGCEVRFAGTPTGVEARLVREAGIPFTPFEAQGFNRNHPLtLPKAVLTIqk 77
Cdd:cd03811 2 ILFVipsLSGGGAE---RVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLG-LLKAILKL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 78 sttlaRRWFDEIQPDAVVGFGGYVCIpVARAAEQRGIPVVVHEQNSV--------MGMANKYLAKRAAA-VCLTyEHAAE 148
Cdd:cd03811 76 -----KRILKRAKPDVVISFLGFATY-IVAKLAAARSKVIAWIHSSLsklyylkkKLLLKLKLYKKADKiVCVS-KGIKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 149 ALAD-----KSRVRVTGNPVResvFSATREQGRARFGVPEGARMLLVTGGSL----GARHLNQAVAALKDGLLAYgDLHI 219
Cdd:cd03811 149 DLIRlgpspPEKIEVIYNPID---IDRIRALAKEPILNEPEDGPVILAVGRLdpqkGHDLLIEAFAKLRKKYPDV-KLVI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 220 VqvtGPKELDAVREQLALSPEQQARWQLLGYTDHMGDAMAAADIVVSragaTSLAEisaralpallvPFPFatedhqtmn 299
Cdd:cd03811 225 L---GDGPLREELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVL----SSRYE-----------GFPN--------- 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241181 300 aqACVEAGAAYL--VAdADVEGPefarklRELIEDEDVRARMAAAARAQKTRDAAGLLADAVMEAARA 365
Cdd:cd03811 278 --VLLEAMALGTpvVS-TDCPGP------REILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRE 336
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
86-266 |
3.27e-05 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 45.44 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 86 FDEIQPDAVVgfggyV------CIPVARAAEQRGIPVVvH-------------EQnsvmgmANKYLAKRAAAVCLTY-EH 145
Cdd:COG0381 84 LEEEKPDAVL-----VhgdtnsTLAAALAAFKLGIPVA-HveaglrsfdrpmpEE------INRRLTDHISDLHFAPtEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 146 AAEALA----DKSRVRVTGNPVRESVFSATREQGR----ARFGVPEGaRMLLVTG---GSLGARH-LNQAVAALKDgLLA 213
Cdd:COG0381 152 ARENLLregiPPERIFVTGNTVIDALLYVLERAEEsdilEELGLEPK-KYILVTLhrrENVDDPErLENILEALRE-LAE 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506241181 214 YGDLHIVQVTGPKELDAVREQLALSPeqqaRWQL---LGYTDhMGDAMAAADIVVS 266
Cdd:COG0381 230 RYDLPVVFPVHPRTRKRLEEFLGGHP----NIRLiepLGYLD-FLNLMKRAYLVLT 280
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
152-289 |
9.65e-05 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 44.02 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 152 DKSRVRVTGNPVRESvFSAT--REQGRARFGVPEGARMLLVTGGSLG-ARHLNQAvaaLKDGLLAYGDLHIVQVTG-PKE 227
Cdd:PRK13608 168 DPSTVKVTGIPIDNK-FETPidQKQWLIDNNLDPDKQTILMSAGAFGvSKGFDTM---ITDILAKSANAQVVMICGkSKE 243
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241181 228 LdavREQLALSPEQQARWQLLGYTDHMGDAMAAADIVVSRAGATSLAEISARALPAL-LVPFP 289
Cdd:PRK13608 244 L---KRSLTAKFKSNENVLILGYTKHMNEWMASSQLMITKPGGITISEGLARCIPMIfLNPAP 303
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
86-266 |
5.91e-04 |
|
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.
Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 41.37 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 86 FDEIQPDAVVGFGG-YVCIPVARAAEQRGIPVV-------VHEQNSvmGM---ANKYLAKRAAAVCLTY-EHAAEALA-- 151
Cdd:pfam02350 62 LAEEKPDLVLVLGDtNETLAGALAAFYLRIPVAhveaglrSFDLTE--PMpeeINRHAIDKLSDLHFAPtEEARENLLqe 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241181 152 --DKSRVRVTGNPVRESVFsATREQGRARFGVPEGA--RMLLVTG----GSLGARHLNQAVAALKDgLLAYGDLHIVqVT 223
Cdd:pfam02350 140 gePPERIFVTGNTVIDALL-LSREEIEERSGILAKLgkRYVLVTFhrreNEDDPEALRNILEALRA-LAERPDVPVV-FP 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 506241181 224 GPKElDAVREQLALSPEQQARWQL---LGYTDHMGdAMAAADIVVS 266
Cdd:pfam02350 217 VHNN-PRTRRRLNERLEGYPRVRLiepLGYLDFLS-LLKRADLVIT 260
|
|
| |
