|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-363 |
5.05e-158 |
|
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: 447.65 E-value: 5.05e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERG--AEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPAQKVVMT 160
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 161 GNPRAQQVANIKKSGALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKRDYQTLFVTGQVHYEKIRNGLsATAL 240
Cdd:COG0707 161 GNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEARLQVVHQTGKGDYEEVRAAY-AAAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 241 APNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTS 320
Cdd:COG0707 240 RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489736762 321 LVAALDGLLQSTTHRETMAANAKKLGMPDAADQLLHVLETVIK 363
Cdd:COG0707 320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAK 362
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-363 |
2.74e-154 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 438.03 E-value: 2.74e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELKKRG--WEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPAQKVVMT 160
Cdd:PRK00726 80 VLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 161 GNPRAQQVANIKKSGalAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKrDYQTLFVTGQVHYEKIRNGLsatAL 240
Cdd:PRK00726 160 GNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPE-ALQVIHQTGKGDLEEVRAAY---AA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 241 APNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTS 320
Cdd:PRK00726 234 GINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEK 313
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489736762 321 LVAALDGLLQSTTHRETMAANAKKLGMPDAADQLLHVLETVIK 363
Cdd:PRK00726 314 LAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELAR 356
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
2-355 |
1.25e-145 |
|
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: 415.85 E-value: 1.25e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 2 RLMISGGGTGGHIYPALALIDALKAHdpEAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSV 81
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKR--GAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 82 VTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPAQKVVMTG 161
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 162 NPRAQQVANIKKsgALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKRDYQTLFVTGQVHYEKIRNGLSatALA 241
Cdd:cd03785 159 NPVREEILNLRK--ELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERGIQVIHQTGKGDYDEVKKLYE--DLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 242 PNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTSL 321
Cdd:cd03785 235 INVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330 340 350
....*....|....*....|....*....|....
gi 489736762 322 VAALDGLLQSTTHRETMAANAKKLGMPDAADQLL 355
Cdd:cd03785 315 AEAILDLLNDPERLKKMAEAAKKLAKPDAAERIA 348
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-354 |
3.02e-110 |
|
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: 325.78 E-value: 3.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 1 MRLMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVE--VLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFpaqKVVMT 160
Cdd:TIGR01133 79 VFKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 161 GNPRAQQVANIKKsgALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKRDYQTLFVTGQVHYEKIRNGLSatAL 240
Cdd:TIGR01133 156 GNPVRKEIRSLPV--PRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIVHQGGKGDLEKVKNVYQ--EL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 241 APNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVtNDHQTKNAQSLVNAGAAELIKEADLTGTS 320
Cdd:TIGR01133 232 GQEKIVTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEK 310
|
330 340 350
....*....|....*....|....*....|....
gi 489736762 321 LVAALDGLLQSTTHRETMAANAKKLGMPDAADQL 354
Cdd:TIGR01133 311 LLEALLKLLLDPANLENMAEAARKLAKPDAAKRI 344
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
3-143 |
1.93e-48 |
|
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: 160.15 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 3 LMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSVV 82
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHE--VRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489736762 83 TARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAI 143
Cdd:pfam03033 79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-363 |
5.05e-158 |
|
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: 447.65 E-value: 5.05e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERG--AEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPAQKVVMT 160
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 161 GNPRAQQVANIKKSGALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKRDYQTLFVTGQVHYEKIRNGLsATAL 240
Cdd:COG0707 161 GNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEARLQVVHQTGKGDYEEVRAAY-AAAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 241 APNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTS 320
Cdd:COG0707 240 RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489736762 321 LVAALDGLLQSTTHRETMAANAKKLGMPDAADQLLHVLETVIK 363
Cdd:COG0707 320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAK 362
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-363 |
2.74e-154 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 438.03 E-value: 2.74e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELKKRG--WEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPAQKVVMT 160
Cdd:PRK00726 80 VLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 161 GNPRAQQVANIKKSGalAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKrDYQTLFVTGQVHYEKIRNGLsatAL 240
Cdd:PRK00726 160 GNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPE-ALQVIHQTGKGDLEEVRAAY---AA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 241 APNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTS 320
Cdd:PRK00726 234 GINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEK 313
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489736762 321 LVAALDGLLQSTTHRETMAANAKKLGMPDAADQLLHVLETVIK 363
Cdd:PRK00726 314 LAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELAR 356
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
2-355 |
1.25e-145 |
|
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: 415.85 E-value: 1.25e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 2 RLMISGGGTGGHIYPALALIDALKAHdpEAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSV 81
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKR--GAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 82 VTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPAQKVVMTG 161
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 162 NPRAQQVANIKKsgALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKRDYQTLFVTGQVHYEKIRNGLSatALA 241
Cdd:cd03785 159 NPVREEILNLRK--ELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERGIQVIHQTGKGDYDEVKKLYE--DLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 242 PNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTSL 321
Cdd:cd03785 235 INVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVL 314
|
330 340 350
....*....|....*....|....*....|....
gi 489736762 322 VAALDGLLQSTTHRETMAANAKKLGMPDAADQLL 355
Cdd:cd03785 315 AEAILDLLNDPERLKKMAEAAKKLAKPDAAERIA 348
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-354 |
3.02e-110 |
|
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: 325.78 E-value: 3.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 1 MRLMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRGVE--VLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFpaqKVVMT 160
Cdd:TIGR01133 79 VFKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 161 GNPRAQQVANIKKsgALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELNKRDYQTLFVTGQVHYEKIRNGLSatAL 240
Cdd:TIGR01133 156 GNPVRKEIRSLPV--PRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIVHQGGKGDLEKVKNVYQ--EL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 241 APNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVtNDHQTKNAQSLVNAGAAELIKEADLTGTS 320
Cdd:TIGR01133 232 GQEKIVTFIDENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPEK 310
|
330 340 350
....*....|....*....|....*....|....
gi 489736762 321 LVAALDGLLQSTTHRETMAANAKKLGMPDAADQL 354
Cdd:TIGR01133 311 LLEALLKLLLDPANLENMAEAARKLAKPDAAKRI 344
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
3-143 |
1.93e-48 |
|
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: 160.15 E-value: 1.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 3 LMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSVV 82
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHE--VRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489736762 83 TARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAI 143
Cdd:pfam03033 79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
2-361 |
5.42e-45 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 157.71 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 2 RLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSV 81
Cdd:PRK12446 3 KIVFTGGGSAGHVTPNLAIIPYLKEDN--WDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 82 VTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPAQKVVMTG 161
Cdd:PRK12446 81 MDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVIYTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 162 NPRAQQVANIKKSGALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPELnKRDYQTLFVTGQVHYEKIRNGLSATala 241
Cdd:PRK12446 161 SPVREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPEL-LLKYQIVHLCGKGNLDDSLQNKEGY--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 242 pnVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVP-SPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTS 320
Cdd:PRK12446 237 --RQFEYVHGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPlSKFASRGDQILNAESFERQGYASVLYEEDVTVNS 314
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489736762 321 LVAALDGLlqsTTHRETMAANAKKLGMPDAADQLLHVLETV 361
Cdd:PRK12446 315 LIKHVEEL---SHNNEKYKTALKKYNGKEAIQTIIDHISEA 352
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
188-354 |
2.16e-38 |
|
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: 134.76 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 188 TALIFGGSRGAARINAAAVAAIPELN-KRDYQTLFVTGQVHYEKIRNGLSAtaLAPNVKIEPYIKNMPAILPEVAVILGR 266
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLElKGELQVLHQTGKGDLEEVKIDYAE--LGINYEVFPFIDNMAEYIKAADLVISR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 267 AGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKEADLTGTSLVAALDGLLQSTTHRETMAANAKKLG 346
Cdd:pfam04101 79 AGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKASG 158
|
....*...
gi 489736762 347 MPDAADQL 354
Cdd:pfam04101 159 FKDAAKRL 166
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
3-356 |
1.19e-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: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 3 LMISGGGTGGHIYPALALIDALKAHDPEAQVQ----FVGTHRGLESRIVPERGIDFKTIKI-----QGFKRSLSLQNVKT 73
Cdd:cd17507 2 LILTASTGGGHIQAAQALKEAFREKFDNYEVIiedlLKYSNPVVNKILKRGEKLYKKAPTLyklfyNLTSDRLNSISNKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 74 VYLFLKSVvtaRKYIKAFKPDVVVGTGGYVSGAV-VFAASQMH-IP--TVI-----HEQnsvvgvtnkFLSRFVDKIAIS 144
Cdd:cd17507 82 ARLGLKKL---KELLREEQPDVIISTFPLMSALVeLFKRKGLLpIPvyTVItdyvlHST---------WIHPEVDRYFVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 145 FESARSQF-----PAQKVVMTGNP-RAQQVANIKKSGALAQFDLDPDIPTALIFGGSRGAARINAAavaaIPELNK--RD 216
Cdd:cd17507 150 SEEVKRELvergvTPSQIKVTGIPvRPSFAEVRDKDEARNELNLSPDKPTVLLMGGGGGMGPVKET----VEALLDslRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 217 YQTLFVTGQVH--YEKIRnglSATALAPNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILV-PSPyvtnD 293
Cdd:cd17507 226 GQVLVVCGKNKklYEKLS---GLEEDYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYdPIP----G 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489736762 294 HQTKNAQSLVNAGAAELIKeADLTGTSLVAaldgLLQSTTHRETMAANAKKLGMPDAADQLLH 356
Cdd:cd17507 299 QEEENADFLENNGAGIIAR-DPEELLEIVA----RLIDPPSLLRMMSEAAKELKPPAAAKVIA 356
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
2-346 |
9.26e-16 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 76.43 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 2 RLMISGGGTGGHIYPALALIDALKA--HDpeaqVQFVGTHRGLEsrIVPERGIDFKtikiqgfkrslslqnvktvylflk 79
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRArgHE----VTFATGPDFAD--LVEAAGLEFV------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 80 svvtarkyikAFKPDVVVGTGGYVSGAVvfAASQMHIPTVIHeqnsvvgvtnkfLSRfvdkiaiSFESARSQFPAQkVVM 159
Cdd:COG1819 51 ----------DWRPDLVVSDPLALAAAL--AAEALGIPVVSL------------TPP-------ELEYPRPPDPAN-VRF 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 160 TGNPRAqqvaniKKSGALAQFDL-DPDIPTALI-FGGSrgAARINAAAVAAIPELNKRDYQTLFVTGQVHYEKIRnglsa 237
Cdd:COG1819 99 VGPLLP------DGPAELPPWLEeDAGRPLVYVtLGTS--ANDRADLLRAVLEALADLGVRVVVTTGGLDPAELG----- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 238 tALAPNVKIEPYIkNMPAILPEVAVILGRAGATSIAEITALGIPSILVPspyVTNDhQTKNAQSLVNAGAAELIKEADLT 317
Cdd:COG1819 166 -PLPDNVRVVDYV-PQDALLPRADAVVHHGGAGTTAEALRAGVPQVVVP---FGGD-QPLNAARVERLGAGLALPPRRLT 239
|
330 340
....*....|....*....|....*....
gi 489736762 318 GTSLVAALDGLLQSTTHREtmaaNAKKLG 346
Cdd:COG1819 240 AEALRAALRRLLADPSYRE----RAARLA 264
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
151-358 |
1.64e-07 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 52.42 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 151 QFPAQKVVMTGNP-RAQQVANIKKSGALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIpeLNKRDYQTLFVTGQvhYE 229
Cdd:PRK13609 166 GVPPEQVVETGIPiRSSFELKINPDIIYNKYQLCPNKKILLIMAGAHGVLGNVKELCQSL--MSVPDLQVVVVCGK--NE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 230 KIRNGLSAT-ALAPN-VKIEPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILV-PSPyvtnDHQTKNAQSLVNAG 306
Cdd:PRK13609 242 ALKQSLEDLqETNPDaLKVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKG 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489736762 307 AAELIKEADltgtSLVAALDGLLQSTTHRETMAANAKKLGMPDAADQLLHVL 358
Cdd:PRK13609 318 AAVVIRDDE----EVFAKTEALLQDDMKLLQMKEAMKSLYLPEPADHIVDDI 365
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
128-351 |
4.67e-06 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 48.04 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 128 GVTNKFL-SRFVDKIAIsfesaRSQFPAQKVVMTGNP-RAQQVANIKKSGALA-QFDLDPDIPTALIFGGSRG-----AA 199
Cdd:PLN02605 150 GVTRCFCpSEEVAKRAL-----KRGLEPSQIRVYGLPiRPSFARAVRPKDELRrELGMDEDLPAVLLMGGGEGmgpleET 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 200 RINAAAVAAIPELNKRDYQTLFVTGQvhYEKIRNGLSATALAPNVKIEPYIKNMPAILPEVAVILGRAGATSIAEITALG 279
Cdd:PLN02605 225 ARALGDSLYDKNLGKPIGQVVVICGR--NKKLQSKLESRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRG 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 280 IPSIL---VPS------PYVtndhqtknaqslVNAGAAELIKeaDLTGTSLVAAlDGLLQSTTHRETMAANAKKLGMPDA 350
Cdd:PLN02605 303 LPIILngyIPGqeegnvPYV------------VDNGFGAFSE--SPKEIARIVA-EWFGDKSDELEAMSENALKLARPEA 367
|
.
gi 489736762 351 A 351
Cdd:PLN02605 368 V 368
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
1-358 |
3.82e-05 |
|
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: 45.23 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRI-------------VPERGIDFKTIKIQGFKRSLS 67
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKALAARG--HEVTVATPPFNFADLVeaagltfvpvgddPDELELDSETNLGPDSLLELL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 68 LQNVKTVYLFLKSVVtaRKYIKAFKPDVVVGTGGYVSGAVVFAAsqMHIPTVIH-------EQNSVVGVTNKFLSRFVDK 140
Cdd:cd03784 79 RRLLKAADELLDDLL--AALRSSWKPDLVIADPFAYAGPLVAEE--LGIPSVRLftgpatlLSAYLHPFGVLNLLLSSLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 141 IAISFESA--------RSQFPAQKVVMTGNPRAQQVANIKKSGALAQFDLDPDIPTALIFGGSRGAARINAAAVAAIPEL 212
Cdd:cd03784 155 EPELFLDPllevldrlRERLGLPPFSLVLLLLRLVPPLYVIGPTFPSLPPDRPRLPSVLGGLRIVPKNGPLPDELWEWLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 213 NKRDYQTLFVT-----------------------GQVHYEKIRNGL--SATALAPNVKIEPYIkNMPAIL--PEVAVILG 265
Cdd:cd03784 235 KQPPRSVVYVSfgsmvrdlpeelleliaealaslGQRFLWVVGPDPlgGLERLPDNVLVVKWV-PQDELLahPAVGAFVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489736762 266 RAGATSIAEITALGIPSILVPspyVTNDhQTKNAQSLVNAGAAELIKEADLTGTSLVAALDGLLQSTTHRETMAANAKKL 345
Cdd:cd03784 314 HGGWNSTLEALYAGVPMVVVP---LFAD-QPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAELLAELR 389
|
410
....*....|....*
gi 489736762 346 GM--PDAADQLLHVL 358
Cdd:cd03784 390 EEdgAPSAADVVERL 404
|
|
| |
