|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
75-454 |
0e+00 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 719.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 75 VLILMSDTGGGHRASAEAIRDAFKIEFGDDYRIIIKDVWKEYTGWPLNDMERQYKFMVKHVGLWSVAFHGTSPKWIHKSY 154
Cdd:PLN02605 1 VLILMSDTGGGHRASAEAIKDAFQLEFGDEYQVFIVDLWKEHTPWPFNQLPRSYKFLVKHPQLWKMTYHGTNPRLIHQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 155 LSALAAYYAKEIEAGLMEYKPDIIISVHPLMQHIPLWVMKWQG--LHKKVIFVTVITDLNTCHRTWFHHGVSRCYCPSKE 232
Cdd:PLN02605 81 FAATSAFVAREVAKGLMKYKPDIIVSVHPLMQHVPLRVLRWQGkeLGKKIPFTTVVTDLGTCHPTWFHKGVTRCFCPSEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 233 VAKRALVDGLDDSQIRVFGLPVRPSFPRTILNKNELRKELEIDLNLPAVLLMGGGEGMGPVQKTALALGDSLYNSKESNP 312
Cdd:PLN02605 161 VAKRALKRGLEPSQIRVYGLPIRPSFARAVRPKDELRRELGMDEDLPAVLLMGGGEGMGPLEETARALGDSLYDKNLGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 313 IGQLIVICGRNKVLASTLASHEWKIPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILNDYIPGQEKGNVP 392
Cdd:PLN02605 241 IGQVVVICGRNKKLQSKLESRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILNGYIPGQEEGNVP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18397057 393 YVVDNGAGVFTRSPKETAKIVADWFSNNKEELKKMSENALKLSQPEAVFDIVKDIHHLSQQQ 454
Cdd:PLN02605 321 YVVDNGFGAFSESPKEIARIVAEWFGDKSDELEAMSENALKLARPEAVFDIVHDLHELVRQR 382
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
75-451 |
3.06e-135 |
|
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: 393.99 E-value: 3.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 75 VLILMSDTGGGHRASAEAIRDAFKIEFgDDYRIIIKDVWKEYTGWPLNDMERQYKFMVKHVGLWSVAFHGTSPKWIHKSY 154
Cdd:cd17507 1 VLILTASTGGGHIQAAQALKEAFREKF-DNYEVIIEDLLKYSNPVVNKILKRGEKLYKKAPTLYKLFYNLTSDRLNSISN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 155 LSALaaYYAKEIEAGLMEYKPDIIISVHPLMQHIPLWVMKWQGLhkKVIFVTVITDLNtCHRTWFHHGVSRCYCPSKEVA 234
Cdd:cd17507 80 KAAR--LGLKKLKELLREEQPDVIISTFPLMSALVELFKRKGLL--PIPVYTVITDYV-LHSTWIHPEVDRYFVASEEVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 235 KRALVDGLDDSQIRVFGLPVRPSFPRTIlNKNELRKELEIDLNLPAVLLMGGGEGMGPVQKTALALGDSLYNskesnpiG 314
Cdd:cd17507 155 RELVERGVTPSQIKVTGIPVRPSFAEVR-DKDEARNELNLSPDKPTVLLMGGGGGMGPVKETVEALLDSLRA-------G 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 315 QLIVICGRNKVLASTLASHEWK-IPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILNDYIPGQEKGNVPY 393
Cdd:cd17507 227 QVLVVCGKNKKLYEKLSGLEEDyINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDPIPGQEEENADF 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 18397057 394 VVDNGAGVFTRSPKETAKIVADWFSnNKEELKKMSENALKLSQPeAVFDIVKDIHHLS 451
Cdd:cd17507 307 LENNGAGIIARDPEELLEIVARLID-PPSLLRMMSEAAKELKPP-AAAKVIADILSLL 362
|
|
| MGDG_synth |
pfam06925 |
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of ... |
86-254 |
2.96e-76 |
|
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of approximately 180 residues within plant and bacterial monogalactosyldiacylglycerol (MGDG) synthase (EC:2.4.1.46). In Arabidopsis, there are two types of MGDG synthase which differ in their N-terminal portion: type A and type B.
Pssm-ID: 284368 Cd Length: 169 Bit Score: 235.72 E-value: 2.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 86 HRASAEAIRDAFKIEFGDDYRIIIKDVWKEYTGWPLNDMERQYKFMVKHVGLWSVAFHGTSPKWIHKSYLSALAAYYAKE 165
Cdd:pfam06925 1 HNQAAEALREAFNNEFGDEYQVVVHDSLKELNPFLIKFVLRSYLFLVKHSPLYRLLYYGTEPKIPHKSILAKLATFFARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 166 IEAGLMEYKPDIIISVHPLMQHIPLWVMKWQGLHKKVIFVTVITDLNTCHRTWFHHGVSRCYCPSKEVAKRALVDGLDDS 245
Cdd:pfam06925 81 LAALLEEFQPDIIISTHPLPAAVPLSVLKSKGLLKRVLVVTVVTDFRTCHPFWLHPEIDRYYVPSKEVKKEALEKGIDPS 160
|
....*....
gi 18397057 246 QIRVFGLPV 254
Cdd:pfam06925 161 NIKVTGIPV 169
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
242-447 |
2.46e-17 |
|
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: 83.25 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 242 LDDSQIRVFGLPVRPSFPRtiLNKNELRKELEIDLNLPAVllmgggegmgpvqktaLALG-------------DSLYNSK 308
Cdd:COG0707 152 FPKKKAVVTGNPVRKEILE--LDRPEARAKLGLDPDKPTL----------------LVFGgsqgaralneavpAALAALL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 309 ESNPigQLIVICGRNKvLASTLASHEWKI--PVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILndyIP-- 384
Cdd:COG0707 214 EARL--QVVHQTGKGD-YEEVRAAYAAAIrpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAIL---VPlp 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 385 ----GQEKGNVPYVVDNGAGVFTRSPKETAKIVADWFS---NNKEELKKMSENALKLSQPEAVFDIVKDI 447
Cdd:COG0707 288 haadDHQTKNARALVEAGAAVLIPQSELTPEKLAEALEellEDPERLAKMAEAARALARPDAAERIADLI 357
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02605 |
PLN02605 |
monogalactosyldiacylglycerol synthase |
75-454 |
0e+00 |
|
monogalactosyldiacylglycerol synthase
Pssm-ID: 215325 [Multi-domain] Cd Length: 382 Bit Score: 719.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 75 VLILMSDTGGGHRASAEAIRDAFKIEFGDDYRIIIKDVWKEYTGWPLNDMERQYKFMVKHVGLWSVAFHGTSPKWIHKSY 154
Cdd:PLN02605 1 VLILMSDTGGGHRASAEAIKDAFQLEFGDEYQVFIVDLWKEHTPWPFNQLPRSYKFLVKHPQLWKMTYHGTNPRLIHQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 155 LSALAAYYAKEIEAGLMEYKPDIIISVHPLMQHIPLWVMKWQG--LHKKVIFVTVITDLNTCHRTWFHHGVSRCYCPSKE 232
Cdd:PLN02605 81 FAATSAFVAREVAKGLMKYKPDIIVSVHPLMQHVPLRVLRWQGkeLGKKIPFTTVVTDLGTCHPTWFHKGVTRCFCPSEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 233 VAKRALVDGLDDSQIRVFGLPVRPSFPRTILNKNELRKELEIDLNLPAVLLMGGGEGMGPVQKTALALGDSLYNSKESNP 312
Cdd:PLN02605 161 VAKRALKRGLEPSQIRVYGLPIRPSFARAVRPKDELRRELGMDEDLPAVLLMGGGEGMGPLEETARALGDSLYDKNLGKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 313 IGQLIVICGRNKVLASTLASHEWKIPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILNDYIPGQEKGNVP 392
Cdd:PLN02605 241 IGQVVVICGRNKKLQSKLESRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIRGLPIILNGYIPGQEEGNVP 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18397057 393 YVVDNGAGVFTRSPKETAKIVADWFSNNKEELKKMSENALKLSQPEAVFDIVKDIHHLSQQQ 454
Cdd:PLN02605 321 YVVDNGFGAFSESPKEIARIVAEWFGDKSDELEAMSENALKLARPEAVFDIVHDLHELVRQR 382
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
75-451 |
3.06e-135 |
|
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: 393.99 E-value: 3.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 75 VLILMSDTGGGHRASAEAIRDAFKIEFgDDYRIIIKDVWKEYTGWPLNDMERQYKFMVKHVGLWSVAFHGTSPKWIHKSY 154
Cdd:cd17507 1 VLILTASTGGGHIQAAQALKEAFREKF-DNYEVIIEDLLKYSNPVVNKILKRGEKLYKKAPTLYKLFYNLTSDRLNSISN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 155 LSALaaYYAKEIEAGLMEYKPDIIISVHPLMQHIPLWVMKWQGLhkKVIFVTVITDLNtCHRTWFHHGVSRCYCPSKEVA 234
Cdd:cd17507 80 KAAR--LGLKKLKELLREEQPDVIISTFPLMSALVELFKRKGLL--PIPVYTVITDYV-LHSTWIHPEVDRYFVASEEVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 235 KRALVDGLDDSQIRVFGLPVRPSFPRTIlNKNELRKELEIDLNLPAVLLMGGGEGMGPVQKTALALGDSLYNskesnpiG 314
Cdd:cd17507 155 RELVERGVTPSQIKVTGIPVRPSFAEVR-DKDEARNELNLSPDKPTVLLMGGGGGMGPVKETVEALLDSLRA-------G 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 315 QLIVICGRNKVLASTLASHEWK-IPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILNDYIPGQEKGNVPY 393
Cdd:cd17507 227 QVLVVCGKNKKLYEKLSGLEEDyINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYDPIPGQEEENADF 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 18397057 394 VVDNGAGVFTRSPKETAKIVADWFSnNKEELKKMSENALKLSQPeAVFDIVKDIHHLS 451
Cdd:cd17507 307 LENNGAGIIARDPEELLEIVARLID-PPSLLRMMSEAAKELKPP-AAAKVIADILSLL 362
|
|
| MGDG_synth |
pfam06925 |
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of ... |
86-254 |
2.96e-76 |
|
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of approximately 180 residues within plant and bacterial monogalactosyldiacylglycerol (MGDG) synthase (EC:2.4.1.46). In Arabidopsis, there are two types of MGDG synthase which differ in their N-terminal portion: type A and type B.
Pssm-ID: 284368 Cd Length: 169 Bit Score: 235.72 E-value: 2.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 86 HRASAEAIRDAFKIEFGDDYRIIIKDVWKEYTGWPLNDMERQYKFMVKHVGLWSVAFHGTSPKWIHKSYLSALAAYYAKE 165
Cdd:pfam06925 1 HNQAAEALREAFNNEFGDEYQVVVHDSLKELNPFLIKFVLRSYLFLVKHSPLYRLLYYGTEPKIPHKSILAKLATFFARE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 166 IEAGLMEYKPDIIISVHPLMQHIPLWVMKWQGLHKKVIFVTVITDLNTCHRTWFHHGVSRCYCPSKEVAKRALVDGLDDS 245
Cdd:pfam06925 81 LAALLEEFQPDIIISTHPLPAAVPLSVLKSKGLLKRVLVVTVVTDFRTCHPFWLHPEIDRYYVPSKEVKKEALEKGIDPS 160
|
....*....
gi 18397057 246 QIRVFGLPV 254
Cdd:pfam06925 161 NIKVTGIPV 169
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
71-464 |
9.29e-42 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 152.57 E-value: 9.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 71 RIKTVLILMSDTGGGHRASAEAIRDAFKiEFGDDyRIIIKDVWKEYTGWpLNDMERQYKFMVKHVG--LWSVAFHGTSPK 148
Cdd:PRK13609 3 KNPKVLILTAHYGNGHVQVAKTLEQTFR-QKGIK-DVIVCDLFGESHPV-ITEITKYLYLKSYTIGkeLYRLFYYGVEKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 149 WiHKSYLSALAAYYAKEIEAGLMEYKPDIIISVHPlMQHIPlwvmkwqGLHKKVIFV----TVITDLnTCHRTWFHHGVS 224
Cdd:PRK13609 80 Y-DKKIFSWYANFGRKRLKLLLQAEKPDIVINTFP-IIAVP-------ELKKQTGISiptyNVLTDF-CLHKIWVHREVD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 225 RCYCPSKEVaKRALVD-GLDDSQIRVFGLPVRPSF-----PRTILNKNELRKELEIDLNLPAvllmgggegmgpvqktal 298
Cdd:PRK13609 150 RYFVATDHV-KKVLVDiGVPPEQVVETGIPIRSSFelkinPDIIYNKYQLCPNKKILLIMAG------------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 299 ALGdSLYNSKE------SNPIGQLIVICGRNKVLASTLASHEWKIP--VKVRGFETQMEKWMGACDCIITKAGPGTIAEA 370
Cdd:PRK13609 211 AHG-VLGNVKElcqslmSVPDLQVVVVCGKNEALKQSLEDLQETNPdaLKVFGYVENIDELFRVTSCMITKPGGITLSEA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 371 LICGLPIILNDYIPGQEKGNVPYVVDNGAGVFTRSPKETAKIVADWFSnNKEELKKMSENALKLSQPEAVFDIVKDIhhL 450
Cdd:PRK13609 290 AALGVPVILYKPVPGQEKENAMYFERKGAAVVIRDDEEVFAKTEALLQ-DDMKLLQMKEAMKSLYLPEPADHIVDDI--L 366
|
410
....*....|....
gi 18397057 451 SQQQQRIPLFNEFS 464
Cdd:PRK13609 367 AENHVEPNLAQSFT 380
|
|
| PRK13608 |
PRK13608 |
diacylglycerol glucosyltransferase; Provisional |
170-463 |
1.80e-30 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 184179 [Multi-domain] Cd Length: 391 Bit Score: 121.83 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 170 LMEYKPDIIISVHPlmqhIPLWVMKWQGLHKKVIFVTVITDLnTCHRTWFHHGVSRCYCPSKEVaKRALVD-GLDDSQIR 248
Cdd:PRK13608 100 LIKEKPDLILLTFP----TPVMSVLTEQFNINIPVATVMTDY-RLHKNWITPYSTRYYVATKET-KQDFIDvGIDPSTVK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 249 VFGLPVRPSFPRTILNKNELRKElEIDLNLPAVLLmgggegmgpvqkTALALGDS------LYNSKESNPIGQLIVICGR 322
Cdd:PRK13608 174 VTGIPIDNKFETPIDQKQWLIDN-NLDPDKQTILM------------SAGAFGVSkgfdtmITDILAKSANAQVVMICGK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 323 NKVLASTLAShEWK--IPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILNDYIPGQEKGNVPYVVDNGAG 400
Cdd:PRK13608 241 SKELKRSLTA-KFKsnENVLILGYTKHMNEWMASSQLMITKPGGITISEGLARCIPMIFLNPAPGQELENALYFEEKGFG 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 401 VFTRSPKETAKIVADwFSNNKEELKKMSENALKLSQPEAVFDIVKD----IHHLSQQQQ---RIPLFNEF 463
Cdd:PRK13608 320 KIADTPEEAIKIVAS-LTNGNEQLTNMISTMEQDKIKYATQTICRDlldlIGHSSQPQEiygKVPLYARF 388
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
247-445 |
7.14e-19 |
|
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: 87.66 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 247 IRVFGLPVRPSfprtILNKNELRKELEIDLNLPavllmgggegmgpvqkTALALGDSLY----N-------SKESNPIGQ 315
Cdd:cd03785 154 VVVTGNPVREE----ILNLRKELKRFGLPPDKP----------------TLLVFGGSQGaraiNravpkalPKLLERGIQ 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 316 LIVICGRNKVLASTLASHEWKIPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILndyIP-------GQEK 388
Cdd:cd03785 214 VIHQTGKGDYDEVKKLYEDLGINVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAIL---IPypyaaddHQEA 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18397057 389 gNVPYVVDNGAGVFTR----SPKETAKIVADWfSNNKEELKKMSENALKLSQPEAVFDIVK 445
Cdd:cd03785 291 -NARALEKAGAAIVIDqeelTPEVLAEAILDL-LNDPERLKKMAEAAKKLAKPDAAERIAD 349
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
242-447 |
2.46e-17 |
|
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: 83.25 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 242 LDDSQIRVFGLPVRPSFPRtiLNKNELRKELEIDLNLPAVllmgggegmgpvqktaLALG-------------DSLYNSK 308
Cdd:COG0707 152 FPKKKAVVTGNPVRKEILE--LDRPEARAKLGLDPDKPTL----------------LVFGgsqgaralneavpAALAALL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 309 ESNPigQLIVICGRNKvLASTLASHEWKI--PVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILndyIP-- 384
Cdd:COG0707 214 EARL--QVVHQTGKGD-YEEVRAAYAAAIrpNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAIL---VPlp 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 385 ----GQEKGNVPYVVDNGAGVFTRSPKETAKIVADWFS---NNKEELKKMSENALKLSQPEAVFDIVKDI 447
Cdd:COG0707 288 haadDHQTKNARALVEAGAAVLIPQSELTPEKLAEALEellEDPERLAKMAEAARALARPDAAERIADLI 357
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
315-447 |
2.02e-14 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 74.40 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 315 QLIVICGRNKvLASTLASHEWKIPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILndyIP-------GQE 387
Cdd:PRK00726 214 QVIHQTGKGD-LEEVRAAYAAGINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAIL---VPlphaaddHQT 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18397057 388 KgNVPYVVDNGAGV------FTrsPKETAKIVADWFsNNKEELKKMSENALKLSQPEAVFDIVKDI 447
Cdd:PRK00726 290 A-NARALVDAGAALlipqsdLT--PEKLAEKLLELL-SDPERLEAMAEAARALGKPDAAERLADLI 351
|
|
| Glyco_tran_28_C |
pfam04101 |
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ... |
315-447 |
3.38e-07 |
|
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: 50.02 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 315 QLIVICGRNKVLASTLASHEWKIPVKVRGFETQMEKWMGACDCIITKAGPGTIAEALICGLPIILndyIPGQEKG----- 389
Cdd:pfam04101 32 QVLHQTGKGDLEEVKIDYAELGINYEVFPFIDNMAEYIKAADLVISRAGAGTIAELLALGKPAIL---VPNPSAArghqd 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18397057 390 -NVPYVVDNGAG----VFTRSPKETAKIVADWFSNNKEELKKMSENALklsqpEAVFDIVKDI 447
Cdd:pfam04101 109 nNAKELVKAGAAlvilQKELTPEKLIEALLKLLLNPLRLAEMAKASKA-----SGFKDAAKRL 166
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
164-434 |
8.45e-06 |
|
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: 47.92 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 164 KEIEAGLMEYKPDIIIsVHPLMQHIPLWVMKWQGLHKKVI-----FVTVITDLNTCHRTW------FHHGVSRCYCPSKE 232
Cdd:cd03801 72 RELRPLLRLRKFDVVH-AHGLLAALLAALLALLLGAPLVVtlhgaEPGRLLLLLAAERRLlaraeaLLRRADAVIAVSEA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 233 VAKRALVD-GLDDSQIRVFGLPVRPSFPRTILNKNELRKELEIDLNLPAVLLMgggegmgpvQKTALALGDSLYNSKESN 311
Cdd:cd03801 151 LRDELRALgGIPPEKIVVIPNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSP---------RKGVDLLLEALAKLLRRG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 312 PIGQLiVICGRNKVLASTLASHEWKIPVKVR--GF--ETQMEKWMGACDCII----TKAGPGTIAEALICGLPIILNDYi 383
Cdd:cd03801 222 PDVRL-VIVGGDGPLRAELEELELGLGDRVRflGFvpDEELPALYAAADVFVlpsrYEGFGLVVLEAMAAGLPVVATDV- 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 18397057 384 pgqekGNVPYVVDNGAGVFTRSPKETAKIVA--DWFSNNKEELKKMSENALKL 434
Cdd:cd03801 300 -----GGLPEVVEDGEGGLVVPPDDVEALADalLRLLADPELRARLGRAARER 347
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
339-436 |
2.71e-04 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 40.74 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 339 VKVRGFETQMEKWMGACDCII----TKAGPGTIAEALICGLPIILNDYipgqekGNVPYVVDNGAGVFTRSPKETAKIVA 414
Cdd:COG0438 5 VPRKGLDLLLEALLAAADVFVlpsrSEGFGLVLLEAMAAGLPVIATDV------GGLPEVIEDGETGLLVPPGDPEALAE 78
|
90 100
....*....|....*....|....
gi 18397057 415 --DWFSNNKEELKKMSENALKLSQ 436
Cdd:COG0438 79 aiLRLLEDPELRRRLGEAARERAE 102
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
155-434 |
7.96e-04 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 41.56 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 155 LSALAAYYAKEIEAGLMEYKPDIIISVH-PLMQHIPLWVMKWQgLHKKVIFvtVITDLNTCHRT------------WFHH 221
Cdd:cd03794 79 LNYLSFALAALLKLLVREERPDVIIAYSpPITLGLAALLLKKL-RGAPFIL--DVRDLWPESLIalgvlkkgsllkLLKK 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 222 GVSRCY-------CPSKEVAKRALVDGLDDSQIRVFglpvrPSFPRTILNKNELRKELEIDLNLPavllmgggegmgpvQ 294
Cdd:cd03794 156 LERKLYrladaiiVLSPGLKEYLLRKGVPKEKIIVI-----PNWADLEEFKPPPKDELRKKLGLD--------------D 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 295 KTALALGDSLY-------------NSKESNPIGQLIVICGRNKVLASTLAShEWKIP-VKVRGF--ETQMEKWMGACDC- 357
Cdd:cd03794 217 KFVVVYAGNIGkaqgletlleaaeRLKRRPDIRFLFVGDGDEKERLKELAK-ARGLDnVTFLGRvpKEEVPELLSAADVg 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 358 --------IITKAGPGTIAEALICGLPIILNDyipgqEKGNVPYVVDNGAGVFTR--SPKETAKIVaDWFSNNKEELKKM 427
Cdd:cd03794 296 lvplkdnpANRGSSPSKLFEYMAAGKPILASD-----DGGSDLAVEINGCGLVVEpgDPEALADAI-LELLDDPELRRAM 369
|
....*..
gi 18397057 428 SENALKL 434
Cdd:cd03794 370 GENGREL 376
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
343-443 |
2.24e-03 |
|
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.
Pssm-ID: 340848 [Multi-domain] Cd Length: 377 Bit Score: 40.04 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 343 GFETQMEKW--MGACDCII----TKAGPGTIAEALICGLPIILNDYIPGQEkgnvpyVVDNGAGVFTR-SPKETAKIVAD 415
Cdd:cd03821 268 GPLYGEAKWalYASADLFVlpsySENFGNVVAEALACGLPVVITDKCGLSE------LVEAGCGVVVDpNVSSLAEALAE 341
|
90 100
....*....|....*....|....*...
gi 18397057 416 WFSNNKEElKKMSENALKLSQPEAVFDI 443
Cdd:cd03821 342 ALRDPADR-KRLGEMARRARQVEENFSW 368
|
|
| YjiC |
COG1819 |
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]; |
339-415 |
2.58e-03 |
|
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
Pssm-ID: 441424 [Multi-domain] Cd Length: 268 Bit Score: 39.45 E-value: 2.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18397057 339 VKVRGFETQMEkWMGACDCIITKAGPGTIAEALICGLPIILndyIPGQE--KGNVPYVVDNGAGVFTRSPKETAKIVAD 415
Cdd:COG1819 171 VRVVDYVPQDA-LLPRADAVVHHGGAGTTAEALRAGVPQVV---VPFGGdqPLNAARVERLGAGLALPPRRLTAEALRA 245
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
354-433 |
3.22e-03 |
|
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.
Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 38.02 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 354 ACDCII----TKAGPGTIAEALICGLPIILNDYipgqeKGNVPYVVDNGAGVF--TRSPKETAKIVaDWFSNNKEELKKM 427
Cdd:pfam00534 78 IADVFVlpsrYEGFGIVLLEAMACGLPVIASDV-----GGPPEVVKDGETGFLvkPNNAEALAEAI-DKLLEDEELRERL 151
|
....*.
gi 18397057 428 SENALK 433
Cdd:pfam00534 152 GENARK 157
|
|
| GT4_WbnK-like |
cd03807 |
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ... |
364-434 |
3.39e-03 |
|
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.
Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 39.61 E-value: 3.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18397057 364 PGTIAEALICGLPIILNDYipgqekGNVPYVVDNGAG--VFTRSPKETAKIVaDWFSNNKEELKKMSENALKL 434
Cdd:cd03807 278 PNALLEAMACGLPVVATDV------GGAAELVDDGTGflVPAGDPQALADAI-RALLEDPEKRARLGRAARER 343
|
|
| GT4_WavL-like |
cd03819 |
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ... |
339-412 |
5.33e-03 |
|
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: 38.88 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18397057 339 VKVRGFETQMEKWMGACDCII----TKAGPGTIAEALICGLPIILNDyIPGQ----EKGNVPYVVDNGAGVFTRSPKETA 410
Cdd:cd03819 240 VTFTGFREDVPAALAASDVVVlpslHEEFGRVALEAMACGTPVVATD-VGGAreivVHGRTGLLVPPGDAEALADAIRAA 318
|
..
gi 18397057 411 KI 412
Cdd:cd03819 319 KL 320
|
|
| |
