|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-364 |
3.40e-169 |
|
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: 475.77 E-value: 3.40e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 1 MKILVTGGGTGGHIYPALSFVDYVRSIDptAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKS 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERG--AEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 81 YREAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFPDKKTVLV 160
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 161 GNPRGQEVKNSQKSAILASYDLDPKKKTVLVFGGSQGALKINQAIIEAIPLFAKKDYQLLYASGDRYYQEIEEKIGmsKD 240
Cdd:COG0707 161 GNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEARLQVVHQTGKGDYEEVRAAYA--AA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 241 AFPNISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQ 320
Cdd:COG0707 239 IRPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489219162 321 NLIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRLVQEVIK 364
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAK 362
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-364 |
2.14e-160 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 453.43 E-value: 2.14e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 1 MKILVTGGGTGGHIYPALSFVDYVRsiDPTAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKS 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELK--KRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 81 YREAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFPDKKTVLV 160
Cdd:PRK00726 80 VLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 161 GNPRGQEVKNSQKSAilASYDLDPKKKTVLVFGGSQGALKINQAIIEAIPLFaKKDYQLLYASGDRYYQEIEEKIgmskD 240
Cdd:PRK00726 160 GNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALL-PEALQVIHQTGKGDLEEVRAAY----A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 241 AFPNISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQ 320
Cdd:PRK00726 233 AGINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489219162 321 NLIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRLVQEVIK 364
Cdd:PRK00726 313 KLAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELAR 356
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
2-358 |
9.59e-157 |
|
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: 443.97 E-value: 9.59e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 2 KILVTGGGTGGHIYPALSFVDYVRSIDptAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKSY 81
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRG--AEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 82 REAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFPDKKTVLVG 161
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 162 NPRGQEVKNSQKSaiLASYDLDPKKKTVLVFGGSQGALKINQAIIEAIPLFAKKDYQLLYASGDRYYQEIEEKIgmsKDA 241
Cdd:cd03785 159 NPVREEILNLRKE--LKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERGIQVIHQTGKGDYDEVKKLY---EDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 242 FPNISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQN 321
Cdd:cd03785 234 GINVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEV 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 489219162 322 LIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRL 358
Cdd:cd03785 314 LAEAILDLLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-359 |
2.80e-114 |
|
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: 336.18 E-value: 2.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 1 MKILVTGGGTGGHIYPALSFVDYVRSIDptAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKS 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRG--VEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 81 YREAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFpdkKTVLV 160
Cdd:TIGR01133 79 VFKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 161 GNPRGQEVKNSQ-KSAILAsydLDPKKKTVLVFGGSQGALKINQAIIEAIPLFAKKDYQLLYASGDRYYQEIEEKIgmsk 239
Cdd:TIGR01133 156 GNPVRKEIRSLPvPRERFG---RREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIVHQGGKGDLEKVKNVY---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 240 DAFPNISIRPYID-QMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVtNDHQTKNAQSLVNAGAVKMIADNELN 318
Cdd:TIGR01133 229 QELGQEKIVTFIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELL 307
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489219162 319 SQNLIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRLV 359
Cdd:TIGR01133 308 PEKLLEALLKLLLDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
188-355 |
3.61e-51 |
|
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: 168.28 E-value: 3.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 188 TVLVFGGSQGALKINQAIIEAIPLFAKK-DYQLLYASGDRYYQEIEEKIGMSKdafPNISIRPYIDQMAEVMANSDLLIG 266
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLELKgELQVLHQTGKGDLEEVKIDYAELG---INYEVFPFIDNMAEYIKAADLVIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 267 RAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQNLIECVDAIMSDENVRMEMAKASKEQ 346
Cdd:pfam04101 78 RAGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKAS 157
|
....*....
gi 489219162 347 GIGDASERL 355
Cdd:pfam04101 158 GFKDAAKRL 166
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
1-364 |
3.40e-169 |
|
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: 475.77 E-value: 3.40e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 1 MKILVTGGGTGGHIYPALSFVDYVRSIDptAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKS 80
Cdd:COG0707 3 KRILIAGGGTGGHIFPALALAEELRERG--AEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 81 YREAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFPDKKTVLV 160
Cdd:COG0707 81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 161 GNPRGQEVKNSQKSAILASYDLDPKKKTVLVFGGSQGALKINQAIIEAIPLFAKKDYQLLYASGDRYYQEIEEKIGmsKD 240
Cdd:COG0707 161 GNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEARLQVVHQTGKGDYEEVRAAYA--AA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 241 AFPNISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQ 320
Cdd:COG0707 239 IRPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489219162 321 NLIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRLVQEVIK 364
Cdd:COG0707 319 KLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAK 362
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
1-364 |
2.14e-160 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 453.43 E-value: 2.14e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 1 MKILVTGGGTGGHIYPALSFVDYVRsiDPTAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKS 80
Cdd:PRK00726 2 KKILLAGGGTGGHVFPALALAEELK--KRGWEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 81 YREAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFPDKKTVLV 160
Cdd:PRK00726 80 VLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 161 GNPRGQEVKNSQKSAilASYDLDPKKKTVLVFGGSQGALKINQAIIEAIPLFaKKDYQLLYASGDRYYQEIEEKIgmskD 240
Cdd:PRK00726 160 GNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALL-PEALQVIHQTGKGDLEEVRAAY----A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 241 AFPNISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQ 320
Cdd:PRK00726 233 AGINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489219162 321 NLIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRLVQEVIK 364
Cdd:PRK00726 313 KLAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELAR 356
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
2-358 |
9.59e-157 |
|
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: 443.97 E-value: 9.59e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 2 KILVTGGGTGGHIYPALSFVDYVRSIDptAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKSY 81
Cdd:cd03785 1 KILIAGGGTGGHIFPALALAEELRKRG--AEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 82 REAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFPDKKTVLVG 161
Cdd:cd03785 79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 162 NPRGQEVKNSQKSaiLASYDLDPKKKTVLVFGGSQGALKINQAIIEAIPLFAKKDYQLLYASGDRYYQEIEEKIgmsKDA 241
Cdd:cd03785 159 NPVREEILNLRKE--LKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERGIQVIHQTGKGDYDEVKKLY---EDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 242 FPNISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQN 321
Cdd:cd03785 234 GINVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEV 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 489219162 322 LIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRL 358
Cdd:cd03785 314 LAEAILDLLNDPERLKKMAEAAKKLAKPDAAERIADL 350
|
|
| murG |
TIGR01133 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ... |
1-359 |
2.80e-114 |
|
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: 336.18 E-value: 2.80e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 1 MKILVTGGGTGGHIYPALSFVDYVRSIDptAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKS 80
Cdd:TIGR01133 1 KKIALAAGGTGGHIFPALAVAEELIKRG--VEVLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 81 YREAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFpdkKTVLV 160
Cdd:TIGR01133 79 VFKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 161 GNPRGQEVKNSQ-KSAILAsydLDPKKKTVLVFGGSQGALKINQAIIEAIPLFAKKDYQLLYASGDRYYQEIEEKIgmsk 239
Cdd:TIGR01133 156 GNPVRKEIRSLPvPRERFG---RREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIVHQGGKGDLEKVKNVY---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 240 DAFPNISIRPYID-QMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPYVtNDHQTKNAQSLVNAGAVKMIADNELN 318
Cdd:TIGR01133 229 QELGQEKIVTFIDeNMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELL 307
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489219162 319 SQNLIECVDAIMSDENVRMEMAKASKEQGIGDASERLFRLV 359
Cdd:TIGR01133 308 PEKLLEALLKLLLDPANLENMAEAARKLAKPDAAKRIAELI 348
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
188-355 |
3.61e-51 |
|
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: 168.28 E-value: 3.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 188 TVLVFGGSQGALKINQAIIEAIPLFAKK-DYQLLYASGDRYYQEIEEKIGMSKdafPNISIRPYIDQMAEVMANSDLLIG 266
Cdd:pfam04101 1 TILVTGGSQGARALNELVLSVLPLLELKgELQVLHQTGKGDLEEVKIDYAELG---INYEVFPFIDNMAEYIKAADLVIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 267 RAGATSIAEFTALGLPAILIPSPYVTNDHQTKNAQSLVNAGAVKMIADNELNSQNLIECVDAIMSDENVRMEMAKASKEQ 346
Cdd:pfam04101 78 RAGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKAS 157
|
....*....
gi 489219162 347 GIGDASERL 355
Cdd:pfam04101 158 GFKDAAKRL 166
|
|
| Glyco_transf_28 |
pfam03033 |
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ... |
3-143 |
2.95e-47 |
|
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: 157.06 E-value: 2.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 3 ILVTGGGTGGHIYPALSFVDYVRSIDPTAEflYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKSYR 82
Cdd:pfam03033 1 IVLAGGGTGGHVFPALALAKELKKRGHEVR--VLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489219162 83 EAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAI 143
Cdd:pfam03033 79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
|
|
| PRK12446 |
PRK12446 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed |
2-348 |
1.29e-44 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
Pssm-ID: 171505 [Multi-domain] Cd Length: 352 Bit Score: 156.94 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 2 KILVTGGGTGGHIYPALSFVDYVrsIDPTAEFLYIGATRGLENKIVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKSY 81
Cdd:PRK12446 3 KIVFTGGGSAGHVTPNLAIIPYL--KEDNWDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 82 REAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNSVPGITNKFLTRYVDKIAIAFQDAAHYFPDKKTVLVG 161
Cdd:PRK12446 81 MDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVIYTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 162 NPRGQEVKNSQKSAILASYDLDPKKKTVLVFGGSQGALKINQAIIEAIPLFAKKdYQLLYASGDryyQEIEEKIgMSKDA 241
Cdd:PRK12446 161 SPVREEVLKGNREKGLAFLGFSRKKPVITIMGGSLGAKKINETVREALPELLLK-YQIVHLCGK---GNLDDSL-QNKEG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 242 FPNISirpYI-DQMAEVMANSDLLIGRAGATSIAEFTALGLPAILIP-SPYVTNDHQTKNAQSLVNAGAVKMIADNELNS 319
Cdd:PRK12446 236 YRQFE---YVhGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPlSKFASRGDQILNAESFERQGYASVLYEEDVTV 312
|
330 340 350
....*....|....*....|....*....|
gi 489219162 320 QNLIECVDAI-MSDENVRMEMAKASKEQGI 348
Cdd:PRK12446 313 NSLIKHVEELsHNNEKYKTALKKYNGKEAI 342
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
85-359 |
1.27e-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: 83.14 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 85 KKILREFQPDVVIGTGGYVSGAVVYA--ASVLKIP--TIIHEQNSVPGITNKFLTRYV---DKIA-IAFQDAAHYFPDKK 156
Cdd:cd17507 90 KELLREEQPDVIISTFPLMSALVELFkrKGLLPIPvyTVITDYVLHSTWIHPEVDRYFvasEEVKrELVERGVTPSQIKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 157 TVLVGNPRGQEVKNsqKSAILASYDLDPKKKTVLVFGGSQGALKInQAIIEAIpLFAKKDYQLLYASGDRyyQEIEEKIG 236
Cdd:cd17507 170 TGIPVRPSFAEVRD--KDEARNELNLSPDKPTVLLMGGGGGMGPV-KETVEAL-LDSLRAGQVLVVCGKN--KKLYEKLS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 237 MSKDAFPNISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILI-PSPyvtnDHQTKNAQSLVNAGAVKMIADN 315
Cdd:cd17507 244 GLEEDYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYdPIP----GQEEENADFLENNGAGIIARDP 319
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489219162 316 ElnsqNLIECVDAIMSDE---NVRMEMAKASKEQGIGDASERLFRLV 359
Cdd:cd17507 320 E----ELLEIVARLIDPPsllRMMSEAAKELKPPAAAKVIADILSLL 362
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
2-336 |
3.36e-15 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 74.51 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 2 KILVTGGGTGGHIYPALSFVDYVRSIDptAEFLYIGATRGLEnkIVPPTGIPFktleiqgfkrklsldnvktvqlflksy 81
Cdd:COG1819 1 RILFVTLGGRGHVNPLLALARALRARG--HEVTFATGPDFAD--LVEAAGLEF--------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 82 reakkilREFQPDVVIGTGGYVSGAVvyAASVLKIPTIIHeqnSVPgitnkfltryvdkiaiAFQDAAHYFPDkKTVLVG 161
Cdd:COG1819 50 -------VDWRPDLVVSDPLALAAAL--AAEALGIPVVSL---TPP----------------ELEYPRPPDPA-NVRFVG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 162 NPRgqevkNSQKSAILASYDLDPKKKTVLV-FGGSQ-GALKINQAIIEAiplFAKKDYQLLYASGDRYYQEIEEkigmsk 239
Cdd:COG1819 101 PLL-----PDGPAELPPWLEEDAGRPLVYVtLGTSAnDRADLLRAVLEA---LADLGVRVVVTTGGLDPAELGP------ 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 240 dAFPNISIRPYIDQmAEVMANSDLLIGRAGATSIAEFTALGLPAILIPspyVTNDhQTKNAQSLVNAGAVKMIADNELNS 319
Cdd:COG1819 167 -LPDNVRVVDYVPQ-DALLPRADAVVHHGGAGTTAEALRAGVPQVVVP---FGGD-QPLNAARVERLGAGLALPPRRLTA 240
|
330
....*....|....*..
gi 489219162 320 QNLIECVDAIMSDENVR 336
Cdd:COG1819 241 EALRAALRRLLADPSYR 257
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
85-353 |
2.89e-13 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 70.14 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 85 KKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTI-------IHEQNSVPGITNKFL-TRYVDKIAIAFQdaahyFPDKK 156
Cdd:PRK13609 97 KLLLQAEKPDIVINTFPIIAVPELKKQTGISIPTYnvltdfcLHKIWVHREVDRYFVaTDHVKKVLVDIG-----VPPEQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 157 TVLVGNPRGQEVKNS-QKSAILASYDLDPKKKTVLVFGGSQGALKINQAIIEAipLFAKKDYQLLYASG--DRYYQEIEE 233
Cdd:PRK13609 172 VVETGIPIRSSFELKiNPDIIYNKYQLCPNKKILLIMAGAHGVLGNVKELCQS--LMSVPDLQVVVVCGknEALKQSLED 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 234 KIGMSKDAfpnISIRPYIDQMAEVMANSDLLIGRAGATSIAEFTALGLPAILI-PSPyvtnDHQTKNAQSLVNAGAVKMI 312
Cdd:PRK13609 250 LQETNPDA---LKVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKGAAVVI 322
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489219162 313 ADNElnsqNLIECVDAIMSDENVRMEMAKASKEQGIGDASE 353
Cdd:PRK13609 323 RDDE----EVFAKTEALLQDDMKLLQMKEAMKSLYLPEPAD 359
|
|
| COG4671 |
COG4671 |
Predicted glycosyl transferase [General function prediction only]; |
179-333 |
3.29e-11 |
|
Predicted glycosyl transferase [General function prediction only];
Pssm-ID: 443708 [Multi-domain] Cd Length: 391 Bit Score: 64.10 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 179 SYDLDPKKKTVLV-FGGSQGALKINQAIIEAIPLFAKKDYQLL-----YASGDRYyQEIEEKIGmskdAFPNISIRPYID 252
Cdd:COG4671 209 ALGLLPEEPLILVsAGGGGDGAELLEAALAAAELLPPPDHRWLlvtgpFMPAADR-AALRARAA----ALPNVTVERFTP 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 253 QMAEVMANSDLLIGRAGATSIAEFTALGLPAILIPSPyVTNDHQTKNAQSLVNAGAVKMIADNELNSQNLIECVDAIMSD 332
Cdd:COG4671 284 DFEALLAAADLSVSMGGYNTVCEILSTGKPALIVPRT-APRTEQLIRAERLAELGLVDVLHPEDLTPEALARAIAAALAR 362
|
.
gi 489219162 333 E 333
Cdd:COG4671 363 P 363
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
173-357 |
7.02e-11 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 62.89 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 173 KSAILASYDLDPKKKTVLVFGGSQGALKINQAIIEAIpLFAKKDYQLLYASGDRyyQEIEEKIGMSKDAFPNISIRPYID 252
Cdd:PRK13608 189 QKQWLIDNNLDPDKQTILMSAGAFGVSKGFDTMITDI-LAKSANAQVVMICGKS--KELKRSLTAKFKSNENVLILGYTK 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 253 QMAEVMANSDLLIGRAGATSIAEFTALGLPAILI-PSPyvtnDHQTKNAQSLVNAGAVKmIADnelNSQNLIECVDAIMS 331
Cdd:PRK13608 266 HMNEWMASSQLMITKPGGITISEGLARCIPMIFLnPAP----GQELENALYFEEKGFGK-IAD---TPEEAIKIVASLTN 337
|
170 180
....*....|....*....|....*.
gi 489219162 332 DENVRMEMAKASKEQGIGDASERLFR 357
Cdd:PRK13608 338 GNEQLTNMISTMEQDKIKYATQTICR 363
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
46-345 |
1.16e-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: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 46 IVPPTGIPFKTLEIQGFKRKLSLDNVKTVQLFLKSYREAKKILREFQPDVVIGTGGYVSGAVVYAASVLKIPTIIHEQNS 125
Cdd:cd03801 36 VLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 126 VPGITNK-------------FLTRYVDKIaIAFQDA-------AHYFPDKKTVLVGNPrgqeVKNSQKSAILASYDLDPK 185
Cdd:cd03801 116 EPGRLLLllaaerrllaraeALLRRADAV-IAVSEAlrdelraLGGIPPEKIVVIPNG----VDLERFSPPLRRKLGIPP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 186 KKTVLVFGGSQGALKINQAIIEAIPLFAKKDYQ---LLYASGDRYYQEIEEkigMSKDAFPNISIRPYI--DQMAEVMAN 260
Cdd:cd03801 191 DRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDvrlVIVGGDGPLRAELEE---LELGLGDRVRFLGFVpdEELPALYAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 261 SDLLIgragATSIAEftALGLP---AILIPSPYVTNDhqtknaqslvNAGAVKMIADNEL-------NSQNLIECVDAIM 330
Cdd:cd03801 268 ADVFV----LPSRYE--GFGLVvleAMAAGLPVVATD----------VGGLPEVVEDGEGglvvppdDVEALADALLRLL 331
|
330
....*....|....*
gi 489219162 331 SDENVRMEMAKASKE 345
Cdd:cd03801 332 ADPELRARLGRAARE 346
|
|
| GT1_Gtf-like |
cd03784 |
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ... |
1-361 |
1.05e-07 |
|
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: 53.32 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 1 MKILVTGGGTGGHIYPALSFVD-------YVRSIdpTAEFLYIGATRGLENKIVPpTGIPFKTLEIQGFKRKLSLDNVKT 73
Cdd:cd03784 1 MRILFVPFPGQGHVNPMLPLAKalaarghEVTVA--TPPFNFADLVEAAGLTFVP-VGDDPDELELDSETNLGPDSLLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 74 VQLFLKSYREA-----KKILREFQPDVVIGTGGYVSGAVVyaASVLKIPTIIH-------EQNSVPGITNKFLTRYVDKI 141
Cdd:cd03784 78 LRRLLKAADELlddllAALRSSWKPDLVIADPFAYAGPLV--AEELGIPSVRLftgpatlLSAYLHPFGVLNLLLSSLLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 142 AIAFQDAA---------HYFPDKK------------------TVLVGNPRGQEVKNSQKSAILASYD----------LDP 184
Cdd:cd03784 156 PELFLDPLlevldrlreRLGLPPFslvllllrlvpplyvigpTFPSLPPDRPRLPSVLGGLRIVPKNgplpdelwewLDK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 185 K--KKTVLV-FGgSQGALKINQAIIEAIPLFAKKDYQLLYASGDryyqeieEKIGMSKDAFPNISIRPYIDQMaEVMANS 261
Cdd:cd03784 236 QppRSVVYVsFG-SMVRDLPEELLELIAEALASLGQRFLWVVGP-------DPLGGLERLPDNVLVVKWVPQD-ELLAHP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 262 --DLLIGRAGATSIAEFTALGLPAILIPspyVTNDhQTKNAQSLVNAGAVKMIADNELNSQNLIECVDAIMSDEnVRMEM 339
Cdd:cd03784 307 avGAFVTHGGWNSTLEALYAGVPMVVVP---LFAD-QPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDE-SYRRA 381
|
410 420
....*....|....*....|..
gi 489219162 340 AKASKEQGIGDASERLFRLVQE 361
Cdd:cd03784 382 AELLAELREEDGAPSAADVVER 403
|
|
| GT4_AmsD-like |
cd03820 |
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ... |
77-345 |
1.84e-06 |
|
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.
Pssm-ID: 340847 [Multi-domain] Cd Length: 351 Bit Score: 49.16 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 77 FLKSYREAKKILREFQPDVVIGTGgyVSGAVVYAASVLKIPTIIHEQNS--------VPGITNKFLTRYVDKIAI---AF 145
Cdd:cd03820 72 YFKKVRRLRKYLKNNKPDVVISFR--TSLLTFLALIGLKSKLIVWEHNNyeaynkglRRLLLRRLLYKRADKIVVlteAD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 146 QDAAHYFPDKKTVLVGNPrgqevknsqKSAILASYDLDPKKKTVLvfggSQGALKINQAI---IEAIPLFAKK--DYQLL 220
Cdd:cd03820 150 KLKKYKQPNSNVVVIPNP---------LSFPSEEPSTNLKSKRIL----AVGRLTYQKGFdllIEAWALIAKKhpDWKLR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 221 -YASGDRyYQEIEEKI---GMSKdafpNISIRPYIDQMAEVMANSDLLIgragATS--------IAEFTALGLPAIL--I 286
Cdd:cd03820 217 iYGDGPE-REELEKLIdklGLED----RVKLLGPTKNIAEEYANSSIFV----LSSryegfpmvLLEAMAYGLPIISfdC 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489219162 287 PS--PYVTNDHqtKNAqSLVNAGAVKMIADNelnsqnliecVDAIMSDENVRMEMAKASKE 345
Cdd:cd03820 288 PTgpSEIIEDG--ENG-LLVPNGDVDALAEA----------LLRLMEDEELRKKMGKNARK 335
|
|
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
181-293 |
4.33e-06 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 48.04 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489219162 181 DLDPKKKTVLVFGGSQGALKInQAIIEAI--PLFAKK----DYQLLYASGDRyyQEIEEKIgMSKDAFPNISIRPYIDQM 254
Cdd:PLN02605 201 GMDEDLPAVLLMGGGEGMGPL-EETARALgdSLYDKNlgkpIGQVVVICGRN--KKLQSKL-ESRDWKIPVKVRGFVTNM 276
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489219162 255 AEVMANSDLLIGRAGATSIAEFTALGLPAIL---IPS------PYVTN 293
Cdd:PLN02605 277 EEWMGACDCIITKAGPGTIAEALIRGLPIILngyIPGqeegnvPYVVD 324
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