|
Name |
Accession |
Description |
Interval |
E-value |
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
1-373 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 272978 Cd Length: 365 Bit Score: 603.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 1 MKVLTVFGTRPEAIKMAPLVHALAKDPDFDAKVCVTAQHREMLDQVLNLFSIVPDYDLNIMQPGQGLTEITCRILEGLKP 80
Cdd:TIGR00236 1 LKVMIVLGTRPEAIKMAPLIRALKKYPEIDSYVIVTAQHREMLDQVLDLFHLPPDYDLNIMSPGQTLGEITSNMLEGLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 81 ILADFKPDVVLVHGDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTGRLAMYHFAPTENSRQNLLREA 160
Cdd:TIGR00236 81 LLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMPEEINRQLTGHIADLHFAPTEQAKDNLLREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 161 IPENRIFVTGNTVIDALIWVRDRVLANDELraelaehyPFLSSDKKMILVTGHRRESFGRGFERICHALAEIAAANQNVQ 240
Cdd:TIGR00236 161 VKADSIFVTGNTVIDALLTNVEIAYSSPVL--------SEFGEDKRMILLTLHRRENVGEPLENIFKAIREIVEEFEDVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 241 IVYPVHLNPNVSEPVNRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERPEAITAG 320
Cdd:TIGR00236 233 IVYPVHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVLVLRDTTERPETVEAG 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489108125 321 TVRLVGTDPQRIVEEVTRLLHDDNEYQTMSRAHNPYGDGQACGRILHALKNNR 373
Cdd:TIGR00236 313 TNKLVGTDKENITKAAKRLLTDPDEYKKMSNASNPYGDGEASERIVEELLNHY 365
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
1-372 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 587.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 1 MKVLTVFGTRPEAIKMAPLVHALAKDPDFDAKVCVTAQHRE--MLDQVLNLFSI-VPDYDLNImqPGQGLTEITCRILEG 77
Cdd:COG0381 2 MKVLTVVGTRPEAIKMAPVIRALKKRPGFEHVLVHTGQHYDyeMSDQFFEELGIpKPDYDLGI--GSGSLAEQTARILEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 78 LKPILADFKPDVVLVHGDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLysPWPEEANRTLTGRLAMYHFAPTENSRQNLL 157
Cdd:COG0381 80 LEEVLEEEKPDAVLVHGDTNSTLAAALAAFKLGIPVAHVEAGLRSFDR--PMPEEINRRLTDHISDLHFAPTELARENLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 158 REAIPENRIFVTGNTVIDALIWVRDRVLANDELrAELAEhypflsSDKKMILVTGHRRESFG--RGFERICHALAEIAAA 235
Cdd:COG0381 158 REGIPPERIFVTGNTVIDALLYVLERAEESDIL-EELGL------EPKKYILVTLHRRENVDdpERLENILEALRELAER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 236 NqNVQIVYPVHlnPNVSEPVNRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERPE 315
Cdd:COG0381 231 Y-DLPVVFPVH--PRTRKRLEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLTDSGGIQEEAPSLGKPCLTLRDTTERPE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489108125 316 AITAGTVRLVGTDPQRIVEEVTRLLHDDNEYQTMSRAHNPYGDGQACGRILHALKNN 372
Cdd:COG0381 308 TVEAGTNKLVGTDPERIVAAVERLLDDPAAYERMARAVNPYGDGNASERIVDILLRY 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
2-370 |
1.54e-174 |
|
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family 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: 340819 [Multi-domain] Cd Length: 365 Bit Score: 490.18 E-value: 1.54e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 2 KVLTVFGTRPEAIKMAPLVHALAKDPDFDAKVCVTAQHREMLDQVLN---LFSIVPDYDLNIMQPGQGLTEITCRILEGL 78
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGLELVLVVTGQHLDMLLGVLFffiLFLIKPDYDLDLMGDNQTLGAKTGGLLIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 79 KPILADFKPDVVLVHGDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTgrLAMYHFAPTENSRQNLLR 158
Cdd:cd03786 81 EEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSFDLGMPEEENRHRIDK--LSDLHFAPTEEARENLLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 159 EAIPENRIFVTGNTVIDALIWVRDRVLANDELRAELAEhypflssDKKMILVTGHRRESF--GRGFERICHALAEIAAAN 236
Cdd:cd03786 159 EGEPPERIFVTGNTVIDALLSAALRIRDELVLSKLGLL-------EKKYILVTLHRRENVdsGERLEELLEALEELAEKY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 237 QnVQIVYPVHLN--PNVSEPVNRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERP 314
Cdd:cd03786 232 D-LIVVYPNHPRtrPRIREVGLKFLGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVLVLRDRTERP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489108125 315 EAITAGTVRLVGTDPQRIVEEVTRLLHDDNEYQTMSrAHNPYGDGQACGRILHALK 370
Cdd:cd03786 311 ERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRMS-AINPYGDGNASERIVDILE 365
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
21-370 |
1.50e-162 |
|
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.
Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 458.54 E-value: 1.50e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 21 HALAKDPdFDAKVCVTAQH--REMLDQVLNLFSI-VPDYDLNImqPGQGLTEITCRILEGLKPILADFKPDVVLVHGDTT 97
Cdd:pfam02350 1 KALKADP-LELQLIVTGQHlsREMGDTFFEGFGIpKPDYLLNS--DSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 98 TTIATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTGRLAMYHFAPTENSRQNLLREAIPENRIFVTGNTVIDAL 177
Cdd:pfam02350 78 ETLAGALAAFYLRIPVAHVEAGLRSFDLTEPMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 178 IWVRDRVLANDELRAELaehypflssDKKMILVTGHRRESFGRG--FERICHALAEIaAANQNVQIVYPVHLNPNVSEPV 255
Cdd:pfam02350 158 LLSREEIEERSGILAKL---------GKRYVLVTFHRRENEDDPeaLRNILEALRAL-AERPDVPVVFPVHNNPRTRRRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 256 NRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERPEAITAGTVRLVGTDPQRIVEE 335
Cdd:pfam02350 228 NERLEGYPRVRLIEPLGYLDFLSLLKRADLVITDSGGIQEEAPSLGVPVVNLRDTTERPEGREAGTNVLVGTDPERIVAA 307
|
330 340 350
....*....|....*....|....*....|....*
gi 489108125 336 VTRLLHDDNEYqtmsraHNPYGDGQACGRILHALK 370
Cdd:pfam02350 308 LERLLEDPASY------KNPYGDGNASERIVDILE 336
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
78-352 |
8.01e-03 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 38.17 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 78 LKPILADFKPDVVLvhgDTTTTIAtsLAAFYQR----IPVGHVeagLRTGDLYSPWPEEAnrtlTGRlamyHFAPTENSR 153
Cdd:PRK13609 96 LKLLLQAEKPDIVI---NTFPIIA--VPELKKQtgisIPTYNV---LTDFCLHKIWVHRE----VDR----YFVATDHVK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 154 QNLLREAIPENRIFVTGntvidalIWVRdRVLANDELRAELAEHYPfLSSDKKMILVTGHrresfGRGFERICHALAEIA 233
Cdd:PRK13609 160 KVLVDIGVPPEQVVETG-------IPIR-SSFELKINPDIIYNKYQ-LCPNKKILLIMAG-----AHGVLGNVKELCQSL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 234 AANQNVQIVYPVHLNPNVSEPVN----------RILGHVENViliepqDYmpfvwLMNHAWLILTDSGGIQ-EEAPSLGK 302
Cdd:PRK13609 226 MSVPDLQVVVVCGKNEALKQSLEdlqetnpdalKVFGYVENI------DE-----LFRVTSCMITKPGGITlSEAAALGV 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489108125 303 PVLVMRET--TERPEAI---TAGTVrLVGTDPQRIVEEVTRLLHDDNEYQTMSRA 352
Cdd:PRK13609 295 PVILYKPVpgQEKENAMyfeRKGAA-VVIRDDEEVFAKTEALLQDDMKLLQMKEA 348
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
1-373 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 272978 Cd Length: 365 Bit Score: 603.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 1 MKVLTVFGTRPEAIKMAPLVHALAKDPDFDAKVCVTAQHREMLDQVLNLFSIVPDYDLNIMQPGQGLTEITCRILEGLKP 80
Cdd:TIGR00236 1 LKVMIVLGTRPEAIKMAPLIRALKKYPEIDSYVIVTAQHREMLDQVLDLFHLPPDYDLNIMSPGQTLGEITSNMLEGLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 81 ILADFKPDVVLVHGDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTGRLAMYHFAPTENSRQNLLREA 160
Cdd:TIGR00236 81 LLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMPEEINRQLTGHIADLHFAPTEQAKDNLLREN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 161 IPENRIFVTGNTVIDALIWVRDRVLANDELraelaehyPFLSSDKKMILVTGHRRESFGRGFERICHALAEIAAANQNVQ 240
Cdd:TIGR00236 161 VKADSIFVTGNTVIDALLTNVEIAYSSPVL--------SEFGEDKRMILLTLHRRENVGEPLENIFKAIREIVEEFEDVQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 241 IVYPVHLNPNVSEPVNRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERPEAITAG 320
Cdd:TIGR00236 233 IVYPVHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVLVLRDTTERPETVEAG 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489108125 321 TVRLVGTDPQRIVEEVTRLLHDDNEYQTMSRAHNPYGDGQACGRILHALKNNR 373
Cdd:TIGR00236 313 TNKLVGTDKENITKAAKRLLTDPDEYKKMSNASNPYGDGEASERIVEELLNHY 365
|
|
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
1-372 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 587.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 1 MKVLTVFGTRPEAIKMAPLVHALAKDPDFDAKVCVTAQHRE--MLDQVLNLFSI-VPDYDLNImqPGQGLTEITCRILEG 77
Cdd:COG0381 2 MKVLTVVGTRPEAIKMAPVIRALKKRPGFEHVLVHTGQHYDyeMSDQFFEELGIpKPDYDLGI--GSGSLAEQTARILEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 78 LKPILADFKPDVVLVHGDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLysPWPEEANRTLTGRLAMYHFAPTENSRQNLL 157
Cdd:COG0381 80 LEEVLEEEKPDAVLVHGDTNSTLAAALAAFKLGIPVAHVEAGLRSFDR--PMPEEINRRLTDHISDLHFAPTELARENLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 158 REAIPENRIFVTGNTVIDALIWVRDRVLANDELrAELAEhypflsSDKKMILVTGHRRESFG--RGFERICHALAEIAAA 235
Cdd:COG0381 158 REGIPPERIFVTGNTVIDALLYVLERAEESDIL-EELGL------EPKKYILVTLHRRENVDdpERLENILEALRELAER 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 236 NqNVQIVYPVHlnPNVSEPVNRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERPE 315
Cdd:COG0381 231 Y-DLPVVFPVH--PRTRKRLEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLTDSGGIQEEAPSLGKPCLTLRDTTERPE 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489108125 316 AITAGTVRLVGTDPQRIVEEVTRLLHDDNEYQTMSRAHNPYGDGQACGRILHALKNN 372
Cdd:COG0381 308 TVEAGTNKLVGTDPERIVAAVERLLDDPAAYERMARAVNPYGDGNASERIVDILLRY 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
2-370 |
1.54e-174 |
|
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family 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: 340819 [Multi-domain] Cd Length: 365 Bit Score: 490.18 E-value: 1.54e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 2 KVLTVFGTRPEAIKMAPLVHALAKDPDFDAKVCVTAQHREMLDQVLN---LFSIVPDYDLNIMQPGQGLTEITCRILEGL 78
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGLELVLVVTGQHLDMLLGVLFffiLFLIKPDYDLDLMGDNQTLGAKTGGLLIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 79 KPILADFKPDVVLVHGDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTgrLAMYHFAPTENSRQNLLR 158
Cdd:cd03786 81 EEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSFDLGMPEEENRHRIDK--LSDLHFAPTEEARENLLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 159 EAIPENRIFVTGNTVIDALIWVRDRVLANDELRAELAEhypflssDKKMILVTGHRRESF--GRGFERICHALAEIAAAN 236
Cdd:cd03786 159 EGEPPERIFVTGNTVIDALLSAALRIRDELVLSKLGLL-------EKKYILVTLHRRENVdsGERLEELLEALEELAEKY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 237 QnVQIVYPVHLN--PNVSEPVNRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERP 314
Cdd:cd03786 232 D-LIVVYPNHPRtrPRIREVGLKFLGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVLVLRDRTERP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489108125 315 EAITAGTVRLVGTDPQRIVEEVTRLLHDDNEYQTMSrAHNPYGDGQACGRILHALK 370
Cdd:cd03786 311 ERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRMS-AINPYGDGNASERIVDILE 365
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
21-370 |
1.50e-162 |
|
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.
Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 458.54 E-value: 1.50e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 21 HALAKDPdFDAKVCVTAQH--REMLDQVLNLFSI-VPDYDLNImqPGQGLTEITCRILEGLKPILADFKPDVVLVHGDTT 97
Cdd:pfam02350 1 KALKADP-LELQLIVTGQHlsREMGDTFFEGFGIpKPDYLLNS--DSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 98 TTIATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEEANRTLTGRLAMYHFAPTENSRQNLLREAIPENRIFVTGNTVIDAL 177
Cdd:pfam02350 78 ETLAGALAAFYLRIPVAHVEAGLRSFDLTEPMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 178 IWVRDRVLANDELRAELaehypflssDKKMILVTGHRRESFGRG--FERICHALAEIaAANQNVQIVYPVHLNPNVSEPV 255
Cdd:pfam02350 158 LLSREEIEERSGILAKL---------GKRYVLVTFHRRENEDDPeaLRNILEALRAL-AERPDVPVVFPVHNNPRTRRRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 256 NRILGHVENVILIEPQDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLVMRETTERPEAITAGTVRLVGTDPQRIVEE 335
Cdd:pfam02350 228 NERLEGYPRVRLIEPLGYLDFLSLLKRADLVITDSGGIQEEAPSLGVPVVNLRDTTERPEGREAGTNVLVGTDPERIVAA 307
|
330 340 350
....*....|....*....|....*....|....*
gi 489108125 336 VTRLLHDDNEYqtmsraHNPYGDGQACGRILHALK 370
Cdd:pfam02350 308 LERLLEDPASY------KNPYGDGNASERIVDILE 336
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
2-369 |
5.40e-35 |
|
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate.
Pssm-ID: 274654 Cd Length: 364 Bit Score: 131.88 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 2 KVLTVFGTRPEAIKMAPLVHALAKDPDFDAKVCVTAQH---------REMLDQVLNLFSIVP---DYDlnimqPGQGLTE 69
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDPDLELQLIVTGMHlspeygntvNEIEKDGFDIDEKIEillDSD-----SNAGMAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 70 ITCRILEGLKPILADFKPDVVLVHGDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLYspwpEEANRTLTGRLAMYHFAPT 149
Cdd:TIGR03568 76 SMGLTIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTEGAI----DESIRHAITKLSHLHFVAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 150 ENSRQNLLREAIPENRIFVTGNTVIDALiwvrdrvLANDEL-RAELAEHYPFlSSDKKMILVTGH----RRESFGRGFER 224
Cdd:TIGR03568 152 EEYRQRVIQMGEDPDRVFNVGSPGLDNI-------LSLDLLsKEELEEKLGI-DLDKPYALVTFHpvtlEKAEAEEQIKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 225 ICHALAEIaaaNQNVQIVYpvhlnPNV---SEPVNRILGHV----ENVILIE--PQDYmpFVWLMNHAWLIL--TDSGGI 293
Cdd:TIGR03568 224 LLKALDEL---NKNIIFTY-----PNAdagSRIINEAIEEYvekhPNFRLFKslGQER--YLSLLKNADAVIgnSSSGII 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 294 qeEAPSLGKPVL------VMRETTErpeaitagTVRLVGTDPQRIVEEVTRLLhdDNEYQTM-SRAHNPYGDGQACGRIL 366
Cdd:TIGR03568 294 --EAPSFGVPTInigtrqKGRLRAD--------SVIDVDPDKEEIVKAIEKAL--DPAFKKSlKKVKNPYGDGNSSKRII 361
|
...
gi 489108125 367 HAL 369
Cdd:TIGR03568 362 EIL 364
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
73-352 |
4.06e-07 |
|
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: 51.38 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 73 RILEGLKPILADFKPDVVLVHgDTTTTIATSLAAFYQRIPVGHVEAGLRTGDLYSPWPEE----ANRTLTGRLAMYHFAP 148
Cdd:cd03801 69 RLLRELRPLLRLRKFDVVHAH-GLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAErrllARAEALLRRADAVIAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 149 TENSRQNLLRE-AIPENRIFVTGNTVidaliwvrDRVLANDELRAElaehyPFLSSDKKMILVTGhrRESFGRGFERICH 227
Cdd:cd03801 148 SEALRDELRALgGIPPEKIVVIPNGV--------DLERFSPPLRRK-----LGIPPDRPVLLFVG--RLSPRKGVDLLLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 228 ALAEIAAANQNVQ--IVYPVHlnPNVSEPVNRILGHVENVILIEPQDY--MPFVWLMNHAWLILTDSGGIQE---EAPSL 300
Cdd:cd03801 213 ALAKLLRRGPDVRlvIVGGDG--PLRAELEELELGLGDRVRFLGFVPDeeLPALYAAADVFVLPSRYEGFGLvvlEAMAA 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489108125 301 GKPVLvmreTTER---PEAITAGTVRLV--GTDPQRIVEEVTRLLHDDNEYQTMSRA 352
Cdd:cd03801 291 GLPVV----ATDVgglPEVVEDGEGGLVvpPDDVEALADALLRLLADPELRARLGRA 343
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
81-352 |
4.50e-06 |
|
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: 48.20 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 81 ILADFKPDVVL-----VhgdtttTIATSLAAFYQRIP-VGHvE----AGLrtgdlyspwpeeANRTLtGRLAMYHFAPTE 150
Cdd:COG0707 87 ILKRFKPDVVVgfggyV------SGPVGLAARLLGIPlVIH-EqnavPGL------------ANRLL-ARFADRVALAFP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 151 NSRQNLlreaiPENRIFVTGNTvidaliwVRDRVLANDelRAELAEHYPFlSSDKKMILVTGhrresfG-RGFERICHAL 229
Cdd:COG0707 147 ETKKYF-----PKKKAVVTGNP-------VRKEILELD--RPEARAKLGL-DPDKPTLLVFG------GsQGARALNEAV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 230 AEIAAA--NQNVQIVY---PVHLNPNVSEPVNRILGHVENViliepqdymPFVWLMNHAW----LILTDSGGIQ-EEAPS 299
Cdd:COG0707 206 PAALAAllEARLQVVHqtgKGDYEEVRAAYAAAIRPNAEVF---------PFIDDMADAYaaadLVISRAGASTvAELAA 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489108125 300 LGKP-VLVmretterP----------------EAITAGTV----RLvgtDPQRIVEEVTRLLHDDNEYQTMSRA 352
Cdd:COG0707 277 LGKPaILV-------PlphaaddhqtknaralVEAGAAVLipqsEL---TPEKLAEALEELLEDPERLAKMAEA 340
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
81-366 |
6.14e-05 |
|
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: 44.51 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 81 ILADFKPDVVLVHGDTTTTIAtSLAAFYQRIP-VGH---VEAGLrtgdlyspwpeeANRTLtGRLA---MYHFAPTENSR 153
Cdd:cd03785 84 ILRKFKPDVVIGFGGYVSGPV-VLAARLLGIPlIIHeqnAVPGL------------ANRLL-SRFAdkvAVSFPETKKYF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 154 qnllreaiPENRIFVTGNTvidaliwVRDRVLANDELRAELAehypfLSSDKKMILVTGhrresfG-RGFERICHALAEI 232
Cdd:cd03785 150 --------PAAKVVVTGNP-------VREEILNLRKELKRFG-----LPPDKPTLLVFG------GsQGARAINRAVPKA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 233 AA--ANQNVQIVY---PVHLNPnVSEPVNRILGHVEnviliepqdYMPFVWLMNHAW----LILTDSG-GIQEEAPSLGK 302
Cdd:cd03785 204 LPklLERGIQVIHqtgKGDYDE-VKKLYEDLGINVK---------VFPFIDDMAAAYaaadLVISRAGaSTIAELTAAGK 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489108125 303 PVLVM-------RETTERPEAIT-AGTVRLV---GTDPQRIVEEVTRLLHDDNEYQTMSRAHNPYGDGQACGRIL 366
Cdd:cd03785 274 PAILIpypyaadDHQEANARALEkAGAAIVIdqeELTPEVLAEAILDLLNDPERLKKMAEAAKKLAKPDAAERIA 348
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
194-308 |
4.11e-04 |
|
glycosyltransferase family 1 and related proteins with GTB topology; 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: 340816 [Multi-domain] Cd Length: 235 Bit Score: 41.62 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 194 LAEHYPFLSSDKKMILVTGHRREsfGRGFERICHALAEIAAANQNVQIVYPVHLNPNVSEPVN-RILGHVENVILIEPQD 272
Cdd:cd01635 99 LALARLLVSLPLADKVSVGRLVP--EKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALaAALGLLERVVIIGGLV 176
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489108125 273 YMPFVWLM-NHAWLILTDS-----GGIQEEAPSLGKPVLVMR 308
Cdd:cd01635 177 DDEVLELLlAAADVFVLPSrsegfGLVLLEAMAAGKPVIATD 218
|
|
| TagB |
COG1887 |
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ... |
155-369 |
3.25e-03 |
|
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];
Pssm-ID: 441491 Cd Length: 369 Bit Score: 39.20 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 155 NLLREA--IPENRIFVTGNTVIDALIWVrdrvlANDELRAELAEHYPfLSSDKKMILV--TGHRRESFGRGFERI-CHAL 229
Cdd:COG1887 153 EIFRRAfgYPEGEVLETGYPRNDVLFDA-----DREELREELRERLG-IPEDKKVILYapTWRDDEDNFDDYLDLdLERL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 230 AEIAAANQNVqIVYPvHlnPNVSEPVNRILGhvENVILIEpqDYMPFVWLMNHAWLILTDSGGIQEEAPSLGKPVLV--- 306
Cdd:COG1887 227 AELLGDDYVL-LVRL-H--PFVKDSLDEKYS--DRIIDVS--DYPDINDLLLASDVLITDYSSVMFDFALLDRPIIFyay 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489108125 307 -------MRETTERPEAITAGTVrlvGTDPQRIVEEVTRLLHDD----NEYQTMSRAHNPYGDGQACGRILHAL 369
Cdd:COG1887 299 dleeyrdERGFYFDYEEDAPGPV---VTTFEELIDAIEDILENGdeyaEKYKAFRERFFPYDDGNASERVVDAI 369
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
78-352 |
8.01e-03 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 38.17 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 78 LKPILADFKPDVVLvhgDTTTTIAtsLAAFYQR----IPVGHVeagLRTGDLYSPWPEEAnrtlTGRlamyHFAPTENSR 153
Cdd:PRK13609 96 LKLLLQAEKPDIVI---NTFPIIA--VPELKKQtgisIPTYNV---LTDFCLHKIWVHRE----VDR----YFVATDHVK 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 154 QNLLREAIPENRIFVTGntvidalIWVRdRVLANDELRAELAEHYPfLSSDKKMILVTGHrresfGRGFERICHALAEIA 233
Cdd:PRK13609 160 KVLVDIGVPPEQVVETG-------IPIR-SSFELKINPDIIYNKYQ-LCPNKKILLIMAG-----AHGVLGNVKELCQSL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 234 AANQNVQIVYPVHLNPNVSEPVN----------RILGHVENViliepqDYmpfvwLMNHAWLILTDSGGIQ-EEAPSLGK 302
Cdd:PRK13609 226 MSVPDLQVVVVCGKNEALKQSLEdlqetnpdalKVFGYVENI------DE-----LFRVTSCMITKPGGITlSEAAALGV 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489108125 303 PVLVMRET--TERPEAI---TAGTVrLVGTDPQRIVEEVTRLLHDDNEYQTMSRA 352
Cdd:PRK13609 295 PVILYKPVpgQEKENAMyfeRKGAA-VVIRDDEEVFAKTEALLQDDMKLLQMKEA 348
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
81-352 |
9.03e-03 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 37.71 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 81 ILADFKPDVVLVHGDTTTTIATS-LAAFYQRIPVGHV------EAGLRTGDLYSPWPEEANRTLTG---RLAMYHFAPTE 150
Cdd:cd03794 93 LVREERPDVIIAYSPPITLGLAAlLLKKLRGAPFILDvrdlwpESLIALGVLKKGSLLKLLKKLERklyRLADAIIVLSP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 151 NSRQNLLREAIPENRIFVTGNTVIDALIwvrdRVLANDELRAELAEhypflsSDKKMILVTGhrreSFG--RGFERICHA 228
Cdd:cd03794 173 GLKEYLLRKGVPKEKIIVIPNWADLEEF----KPPPKDELRKKLGL------DDKFVVVYAG----NIGkaQGLETLLEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489108125 229 lAEIAAANQNVQIVY--PVHLNPNVSEPVNRILghVENVILIEPQDY--MPFvwLMN--HAWLI-LTDSGGIQEEAPS-- 299
Cdd:cd03794 239 -AERLKRRPDIRFLFvgDGDEKERLKELAKARG--LDNVTFLGRVPKeeVPE--LLSaaDVGLVpLKDNPANRGSSPSkl 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489108125 300 -----LGKPVLVMRETTERPEAITAGTVRLV-GTDPQRIVEEVTRLLHDDNEYQTMSRA 352
Cdd:cd03794 314 feymaAGKPILASDDGGSDLAVEINGCGLVVePGDPEALADAILELLDDPELRRAMGEN 372
|
|
| |
