|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 563.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 1 MQRVLTVFGTRPEAIKMAPLVRALRRHPEFDVTVCVTAQHRQ--MLDQVLSLFDI-VPDFDLDLmrQNQSLSELTANILN 77
Cdd:COG0381 1 MMKVLTVVGTRPEAIKMAPVIRALKKRPGFEHVLVHTGQHYDyeMSDQFFEELGIpKPDYDLGI--GSGSLAEQTARILE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 78 GVGPVFDAARPDIVLVHGDTTTTLAASLAAFYRHIPIGHVEAGLRTGNIwsPWPEELNRRVTDAVSSWHFAPSKRAAQNL 157
Cdd:COG0381 79 GLEEVLEEEKPDAVLVHGDTNSTLAAALAAFKLGIPVAHVEAGLRSFDR--PMPEEINRRLTDHISDLHFAPTELARENL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 158 YSEGMTPEQVVLTGNTVIDALLQTREKLTADPWLAKriaagfpFLDPARRLILVTGHRRESFG--EPLEHVCHALRELAT 235
Cdd:COG0381 157 LREGIPPERIFVTGNTVIDALLYVLERAEESDILEE-------LGLEPKKYILVTLHRRENVDdpERLENILEALRELAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 236 RHDdIELVYPMHlnPNVTGPVKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERP 315
Cdd:COG0381 230 RYD-LPVVFPVH--PRTRKRLEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLTDSGGIQEEAPSLGKPCLTLRDTTERP 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939405756 316 EALEAGTARLVGTDRGRIVAQVEALLNDRHEYEQMAHAVNPYGDGHASERIVAALEK 372
Cdd:COG0381 307 ETVEAGTNKLVGTDPERIVAAVERLLDDPAAYERMARAVNPYGDGNASERIVDILLR 363
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
3-370 |
4.40e-180 |
|
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: 505.45 E-value: 4.40e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 3 RVLTVFGTRPEAIKMAPLVRALRRHPEFDVTVCVTAQHRQMLDQVLSLFDIVPDFDLDLMRQNQSLSELTANILNGVGPV 82
Cdd:TIGR00236 2 KVMIVLGTRPEAIKMAPLIRALKKYPEIDSYVIVTAQHREMLDQVLDLFHLPPDYDLNIMSPGQTLGEITSNMLEGLEEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 83 FDAARPDIVLVHGDTTTTLAASLAAFYRHIPIGHVEAGLRTGNIWSPWPEELNRRVTDAVSSWHFAPSKRAAQNLYSEGM 162
Cdd:TIGR00236 82 LLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMPEEINRQLTGHIADLHFAPTEQAKDNLLRENV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 163 TPEQVVLTGNTVIDALLQTREKLTADPWLAkriaagfpFLDPARRLILVTGHRRESFGEPLEHVCHALRELATRHDDIEL 242
Cdd:TIGR00236 162 KADSIFVTGNTVIDALLTNVEIAYSSPVLS--------EFGEDKRMILLTLHRRENVGEPLENIFKAIREIVEEFEDVQI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 243 VYPMHLNPNVTGPVKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERPEALEAGT 322
Cdd:TIGR00236 234 VYPVHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVLVLRDTTERPETVEAGT 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1939405756 323 ARLVGTDRGRIVAQVEALLNDRHEYEQMAHAVNPYGDGHASERIVAAL 370
Cdd:TIGR00236 314 NKLVGTDKENITKAAKRLLTDPDEYKKMSNASNPYGDGEASERIVEEL 361
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
3-371 |
3.86e-164 |
|
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: 465.14 E-value: 3.86e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 3 RVLTVFGTRPEAIKMAPLVRALRRHPEFDVTVCVTAQHRQMLDQVLS---LFDIVPDFDLDLMRQNQSLSELTANILNGV 79
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGLELVLVVTGQHLDMLLGVLFffiLFLIKPDYDLDLMGDNQTLGAKTGGLLIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 80 GPVFDAARPDIVLVHGDTTTTLAASLAAFYRHIPIGHVEAGLRTGNIwsPWPEELNRRVTDAVSSWHFAPSKRAAQNLYS 159
Cdd:cd03786 81 EEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSFDL--GMPEEENRHRIDKLSDLHFAPTEEARENLLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 160 EGMTPEQVVLTGNTVIDALLQTREKLTADPWLAKriaagfpFLDPARRLILVTGHRRESF--GEPLEHVCHALRELATRH 237
Cdd:cd03786 159 EGEPPERIFVTGNTVIDALLSAALRIRDELVLSK-------LGLLEKKYILVTLHRRENVdsGERLEELLEALEELAEKY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 238 dDIELVYPMHLN--PNVTGPVKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERP 315
Cdd:cd03786 232 -DLIVVYPNHPRtrPRIREVGLKFLGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVLVLRDRTERP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939405756 316 EALEAGTARLVGTDRGRIVAQVEALLNDRHEYEQMAhAVNPYGDGHASERIVAALE 371
Cdd:cd03786 311 ERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRMS-AINPYGDGNASERIVDILE 365
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
22-371 |
1.44e-153 |
|
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: 436.97 E-value: 1.44e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 22 RALRRHPeFDVTVCVTAQH--RQMLDQVLSLFDI-VPDFDLDlmRQNQSLSELTANILNGVGPVFDAARPDIVLVHGDTT 98
Cdd:pfam02350 1 KALKADP-LELQLIVTGQHlsREMGDTFFEGFGIpKPDYLLN--SDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 99 TTLAASLAAFYRHIPIGHVEAGLRTGNIWSPWPEELNRRVTDAVSSWHFAPSKRAAQNLYSEGMTPEQVVLTGNTVIDAL 178
Cdd:pfam02350 78 ETLAGALAAFYLRIPVAHVEAGLRSFDLTEPMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 179 LQTREkltadpwlakRIAAGFPFL-DPARRLILVTGHRRESFGEP--LEHVCHALRELATRhDDIELVYPMHLNPNVTGP 255
Cdd:pfam02350 158 LLSRE----------EIEERSGILaKLGKRYVLVTFHRRENEDDPeaLRNILEALRALAER-PDVPVVFPVHNNPRTRRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 256 VKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERPEALEAGTARLVGTDRGRIVA 335
Cdd:pfam02350 227 LNERLEGYPRVRLIEPLGYLDFLSLLKRADLVITDSGGIQEEAPSLGVPVVNLRDTTERPEGREAGTNVLVGTDPERIVA 306
|
330 340 350
....*....|....*....|....*....|....*.
gi 1939405756 336 QVEALLNDRHEYEqmahavNPYGDGHASERIVAALE 371
Cdd:pfam02350 307 ALERLLEDPASYK------NPYGDGNASERIVDILE 336
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
280-367 |
2.32e-04 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 43.17 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 280 LMSKAHLIITDSGGIQ-EEAPALGVPVLVTRDT--TERPEA--LEAGTARLVGTDRGRIVAQVEALLNDRHEYEQMAHAV 354
Cdd:PRK13609 270 LFRVTSCMITKPGGITlSEAAALGVPVILYKPVpgQEKENAmyFERKGAAVVIRDDEEVFAKTEALLQDDMKLLQMKEAM 349
|
90
....*....|...
gi 1939405756 355 NPYGDGHASERIV 367
Cdd:PRK13609 350 KSLYLPEPADHIV 362
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 563.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 1 MQRVLTVFGTRPEAIKMAPLVRALRRHPEFDVTVCVTAQHRQ--MLDQVLSLFDI-VPDFDLDLmrQNQSLSELTANILN 77
Cdd:COG0381 1 MMKVLTVVGTRPEAIKMAPVIRALKKRPGFEHVLVHTGQHYDyeMSDQFFEELGIpKPDYDLGI--GSGSLAEQTARILE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 78 GVGPVFDAARPDIVLVHGDTTTTLAASLAAFYRHIPIGHVEAGLRTGNIwsPWPEELNRRVTDAVSSWHFAPSKRAAQNL 157
Cdd:COG0381 79 GLEEVLEEEKPDAVLVHGDTNSTLAAALAAFKLGIPVAHVEAGLRSFDR--PMPEEINRRLTDHISDLHFAPTELARENL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 158 YSEGMTPEQVVLTGNTVIDALLQTREKLTADPWLAKriaagfpFLDPARRLILVTGHRRESFG--EPLEHVCHALRELAT 235
Cdd:COG0381 157 LREGIPPERIFVTGNTVIDALLYVLERAEESDILEE-------LGLEPKKYILVTLHRRENVDdpERLENILEALRELAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 236 RHDdIELVYPMHlnPNVTGPVKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERP 315
Cdd:COG0381 230 RYD-LPVVFPVH--PRTRKRLEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLTDSGGIQEEAPSLGKPCLTLRDTTERP 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939405756 316 EALEAGTARLVGTDRGRIVAQVEALLNDRHEYEQMAHAVNPYGDGHASERIVAALEK 372
Cdd:COG0381 307 ETVEAGTNKLVGTDPERIVAAVERLLDDPAAYERMARAVNPYGDGNASERIVDILLR 363
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
3-370 |
4.40e-180 |
|
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: 505.45 E-value: 4.40e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 3 RVLTVFGTRPEAIKMAPLVRALRRHPEFDVTVCVTAQHRQMLDQVLSLFDIVPDFDLDLMRQNQSLSELTANILNGVGPV 82
Cdd:TIGR00236 2 KVMIVLGTRPEAIKMAPLIRALKKYPEIDSYVIVTAQHREMLDQVLDLFHLPPDYDLNIMSPGQTLGEITSNMLEGLEEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 83 FDAARPDIVLVHGDTTTTLAASLAAFYRHIPIGHVEAGLRTGNIWSPWPEELNRRVTDAVSSWHFAPSKRAAQNLYSEGM 162
Cdd:TIGR00236 82 LLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMPEEINRQLTGHIADLHFAPTEQAKDNLLRENV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 163 TPEQVVLTGNTVIDALLQTREKLTADPWLAkriaagfpFLDPARRLILVTGHRRESFGEPLEHVCHALRELATRHDDIEL 242
Cdd:TIGR00236 162 KADSIFVTGNTVIDALLTNVEIAYSSPVLS--------EFGEDKRMILLTLHRRENVGEPLENIFKAIREIVEEFEDVQI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 243 VYPMHLNPNVTGPVKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERPEALEAGT 322
Cdd:TIGR00236 234 VYPVHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVLVLRDTTERPETVEAGT 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1939405756 323 ARLVGTDRGRIVAQVEALLNDRHEYEQMAHAVNPYGDGHASERIVAAL 370
Cdd:TIGR00236 314 NKLVGTDKENITKAAKRLLTDPDEYKKMSNASNPYGDGEASERIVEEL 361
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
3-371 |
3.86e-164 |
|
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: 465.14 E-value: 3.86e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 3 RVLTVFGTRPEAIKMAPLVRALRRHPEFDVTVCVTAQHRQMLDQVLS---LFDIVPDFDLDLMRQNQSLSELTANILNGV 79
Cdd:cd03786 1 KILTVTGTRPEAIKLAPVLRALKKDPGLELVLVVTGQHLDMLLGVLFffiLFLIKPDYDLDLMGDNQTLGAKTGGLLIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 80 GPVFDAARPDIVLVHGDTTTTLAASLAAFYRHIPIGHVEAGLRTGNIwsPWPEELNRRVTDAVSSWHFAPSKRAAQNLYS 159
Cdd:cd03786 81 EEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSFDL--GMPEEENRHRIDKLSDLHFAPTEEARENLLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 160 EGMTPEQVVLTGNTVIDALLQTREKLTADPWLAKriaagfpFLDPARRLILVTGHRRESF--GEPLEHVCHALRELATRH 237
Cdd:cd03786 159 EGEPPERIFVTGNTVIDALLSAALRIRDELVLSK-------LGLLEKKYILVTLHRRENVdsGERLEELLEALEELAEKY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 238 dDIELVYPMHLN--PNVTGPVKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERP 315
Cdd:cd03786 232 -DLIVVYPNHPRtrPRIREVGLKFLGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVLVLRDRTERP 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939405756 316 EALEAGTARLVGTDRGRIVAQVEALLNDRHEYEQMAhAVNPYGDGHASERIVAALE 371
Cdd:cd03786 311 ERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRMS-AINPYGDGNASERIVDILE 365
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
22-371 |
1.44e-153 |
|
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: 436.97 E-value: 1.44e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 22 RALRRHPeFDVTVCVTAQH--RQMLDQVLSLFDI-VPDFDLDlmRQNQSLSELTANILNGVGPVFDAARPDIVLVHGDTT 98
Cdd:pfam02350 1 KALKADP-LELQLIVTGQHlsREMGDTFFEGFGIpKPDYLLN--SDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 99 TTLAASLAAFYRHIPIGHVEAGLRTGNIWSPWPEELNRRVTDAVSSWHFAPSKRAAQNLYSEGMTPEQVVLTGNTVIDAL 178
Cdd:pfam02350 78 ETLAGALAAFYLRIPVAHVEAGLRSFDLTEPMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 179 LQTREkltadpwlakRIAAGFPFL-DPARRLILVTGHRRESFGEP--LEHVCHALRELATRhDDIELVYPMHLNPNVTGP 255
Cdd:pfam02350 158 LLSRE----------EIEERSGILaKLGKRYVLVTFHRRENEDDPeaLRNILEALRALAER-PDVPVVFPVHNNPRTRRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 256 VKAILGDLRNVTLTGPQEYLPFVYLMSKAHLIITDSGGIQEEAPALGVPVLVTRDTTERPEALEAGTARLVGTDRGRIVA 335
Cdd:pfam02350 227 LNERLEGYPRVRLIEPLGYLDFLSLLKRADLVITDSGGIQEEAPSLGVPVVNLRDTTERPEGREAGTNVLVGTDPERIVA 306
|
330 340 350
....*....|....*....|....*....|....*.
gi 1939405756 336 QVEALLNDRHEYEqmahavNPYGDGHASERIVAALE 371
Cdd:pfam02350 307 ALERLLEDPASYK------NPYGDGNASERIVDILE 336
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
3-370 |
7.34e-29 |
|
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: 115.70 E-value: 7.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 3 RVLTVFGTRPEAIKMAPLVRALRRHPEFDVTVCVTAQHrqmldqvLS-------------LFDIVPDFDLDLM-RQNQSL 68
Cdd:TIGR03568 1 KICVVTGTRADYGLLRPLLKALQDDPDLELQLIVTGMH-------LSpeygntvneiekdGFDIDEKIEILLDsDSNAGM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 69 SELTANILNGVGPVFDAARPDIVLVHGDTTTTLAASLAAFYRHIPIGHVEAGLRT-GNIwspwpEELNRRVTDAVSSWHF 147
Cdd:TIGR03568 74 AKSMGLTIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAI-----DESIRHAITKLSHLHF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 148 APSKRAAQNLYSEGMTPEQVVLTGNTVIDALLQTrekltaDPWLAKRIAAGFPFlDPARRLILVTGH----RRESFGEPL 223
Cdd:TIGR03568 149 VATEEYRQRVIQMGEDPDRVFNVGSPGLDNILSL------DLLSKEELEEKLGI-DLDKPYALVTFHpvtlEKAEAEEQI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 224 EHVCHALRELatrHDDIELVYPmhlNPNVTGpvKAILGDLR-------NVTL---TGPQEYLpfvYLMSKAHLII--TDS 291
Cdd:TIGR03568 222 KELLKALDEL---NKNIIFTYP---NADAGS--RIINEAIEeyvekhpNFRLfksLGQERYL---SLLKNADAVIgnSSS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 292 GGIqeEAPALGVPVLvtrDTTERPEALEAGTARL-VGTDRGRIVAQVEALLNDrhEYEQMAHAV-NPYGDGHASERIVAA 369
Cdd:TIGR03568 291 GII--EAPSFGVPTI---NIGTRQKGRLRADSVIdVDPDKEEIVKAIEKALDP--AFKKSLKKVkNPYGDGNSSKRIIEI 363
|
.
gi 1939405756 370 L 370
Cdd:TIGR03568 364 L 364
|
|
| GT28_Beta-DGS-like |
cd17507 |
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ... |
67-370 |
1.68e-06 |
|
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: 49.62 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 67 SLSELTANI-LNGVGPVFDAARPDIVLVhgdtTTTLAASLAAFYRhipighveaglrtgnIWSPWPEELNRRVTDAV--S 143
Cdd:cd17507 76 SISNKAARLgLKKLKELLREEQPDVIIS----TFPLMSALVELFK---------------RKGLLPIPVYTVITDYVlhS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 144 SW-------HFAPSKRAAQNLYSEGMTPEQVVLTGNTVIDALLQTREKltaDPWLAKRiaagfpFLDPARRLILVTGHrr 216
Cdd:cd17507 137 TWihpevdrYFVASEEVKRELVERGVTPSQIKVTGIPVRPSFAEVRDK---DEARNEL------NLSPDKPTVLLMGG-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 217 esfGEPLEHVCHALRELATRHDDIELVYpmhlnpnVTGPVKAILGDLR-------NVTLTGpqeYLPFVY-LMSKAHLII 288
Cdd:cd17507 206 ---GGGMGPVKETVEALLDSLRAGQVLV-------VCGKNKKLYEKLSgleedyiNVRVLG---YVDDMNeLMAASDLVI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 289 TDSGGIQ-EEAPALGVPVLVTR-------DTTERPEALEAGtarLVGTDRGRIVAQVEALLNDRHEYEQMAHAvNPYGDG 360
Cdd:cd17507 273 TKPGGLTiSEALARGLPVIIYDpipgqeeENADFLENNGAG---IIARDPEELLEIVARLIDPPSLLRMMSEA-AKELKP 348
|
330
....*....|
gi 1939405756 361 HASERIVAAL 370
Cdd:cd17507 349 PAAAKVIADI 358
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
51-368 |
2.26e-06 |
|
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: 49.14 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 51 FDIVPDFDLDLM------RQNQSLSELTANILNGVGPVFDAAR------PDIVLVHGDTTTtLAASLAAFYRHIP-IGH- 116
Cdd:cd03785 41 AKLVPEAGIPFHtipisgLRRKGSLKNLKAPFKLLKGLRQARKilrkfkPDVVIGFGGYVS-GPVVLAARLLGIPlIIHe 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 117 --VEAGLrtGNIWspwpeeLNRRVTDAVSSWHFAPSKRAAQNlysegmtpeqVVLTGNTVIDALLQTREKLTADPwlakr 194
Cdd:cd03785 120 qnAVPGL--ANRL------LSRFADKVAVSFPETKKYFPAAK----------VVVTGNPVREEILNLRKELKRFG----- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 195 iaagfpfLDPARRLILVTGHrreSFG-EPL-EHVCHALRELATRhdDIELVYpmhlnpnVTGP-----VKAILGDLR-NV 266
Cdd:cd03785 177 -------LPPDKPTLLVFGG---SQGaRAInRAVPKALPKLLER--GIQVIH-------QTGKgdydeVKKLYEDLGiNV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 267 TLtgpqeyLPFVY----LMSKAHLIITDSG-GIQEEAPALGVPVL------VTRD-TTERPEALE-AGTARLV---GTDR 330
Cdd:cd03785 238 KV------FPFIDdmaaAYAAADLVISRAGaSTIAELTAAGKPAIlipypyAADDhQEANARALEkAGAAIVIdqeELTP 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 1939405756 331 GRIVAQVEALLNDRHEYEQMAHAVNPYGDGHASERIVA 368
Cdd:cd03785 312 EVLAEAILDLLNDPERLKKMAEAAKKLAKPDAAERIAD 349
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
20-372 |
8.77e-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: 47.53 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 20 LVRALRRHPeFDVTVCVTAQHRQMLDQVLSLFDIVPDFDLDLMRQNQSlseltanILNGVGPVFDAARPDIVLVHgDTTT 99
Cdd:cd03801 23 LARALAARG-HDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARR-------LLRELRPLLRLRKFDVVHAH-GLLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 100 TLAASLAAFYRHIPIGHVEAGLRTGNIWSPWPEElNRRVTDAVSSWHF-----APSKRAAQNLYSE-GMTPEQVVLTGNT 173
Cdd:cd03801 94 ALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAE-RRLLARAEALLRRadaviAVSEALRDELRALgGIPPEKIVVIPNG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 174 VIDALLQTREKLTadpwlakriaagfPFLDPARRLILVTGHRRESFGepLEHVCHALRELATRHDDIELVypmhlnpnVT 253
Cdd:cd03801 173 VDLERFSPPLRRK-------------LGIPPDRPVLLFVGRLSPRKG--VDLLLEALAKLLRRGPDVRLV--------IV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 254 GPVKAILGDLR--------NVTLTGPQEYLPFVYLMSKAHLIITDSggIQE-------EAPALGVPVLVTrDTTERPEAL 318
Cdd:cd03801 230 GGDGPLRAELEelelglgdRVRFLGFVPDEELPALYAAADVFVLPS--RYEgfglvvlEAMAAGLPVVAT-DVGGLPEVV 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939405756 319 EAGTARLV--GTDRGRIVAQVEALLNDRHEYEQMA-HAVNPYGDGHASERIVAALEK 372
Cdd:cd03801 307 EDGEGGLVvpPDDVEALADALLRLLADPELRARLGrAARERVAERFSWERVAERLLD 363
|
|
| MurG |
COG0707 |
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ... |
164-372 |
9.10e-05 |
|
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: 44.35 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 164 PEQVVLTGNTVIDALLQtrekltadpwLAKRIAAGFPFLDPARRLILVTGHrreSFG-EPL-EHVCHALRELATRhdDIE 241
Cdd:COG0707 154 KKKAVVTGNPVRKEILE----------LDRPEARAKLGLDPDKPTLLVFGG---SQGaRALnEAVPAALAALLEA--RLQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 242 LVypmHlnpnVTGPVKaILGDLRNVTLTGPQEY--LPFVY----LMSKAHLIITDSGGIQ-EEAPALGVP-VLVtrdtte 313
Cdd:COG0707 219 VV---H----QTGKGD-YEEVRAAYAAAIRPNAevFPFIDdmadAYAAADLVISRAGASTvAELAALGKPaILV------ 284
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939405756 314 rP-------------EALE-AGTARLV---GTDRGRIVAQVEALLNDRHEYEQMAHAVNPYGDGHASERIVAALEK 372
Cdd:COG0707 285 -PlphaaddhqtknaRALVeAGAAVLIpqsELTPEKLAEALEELLEDPERLAKMAEAARALARPDAAERIADLILE 359
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
11-351 |
1.57e-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: 43.48 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 11 RPEAIKMAPLVRALRRHpEFDVTVcVT-----------AQHRQMLDQV-LSLFDIVPDFDLDLMRQNQSLSELTANILNG 78
Cdd:cd03794 14 GAAAARVYELAKELVRR-GHEVTV-LTpspnyplgrifAGATETKDGIrVIRVKLGPIKKNGLIRRLLNYLSFALAALLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 79 VgpVFDAARPDIVLVHGDT-TTTLAASLAAFYRHIPIGHveaglrtgNIWSPWPEelNRRVTDAVSSWHF---------- 147
Cdd:cd03794 92 L--LVREERPDVIIAYSPPiTLGLAALLLKKLRGAPFIL--------DVRDLWPE--SLIALGVLKKGSLlkllkklerk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 148 ---------APSKRAAQNLYSEGMTPEQVVLTGNTVidallqtreKLTADPWLAKRIAAgFPFLDPARRLILVTGhrreS 218
Cdd:cd03794 160 lyrladaiiVLSPGLKEYLLRKGVPKEKIIVIPNWA---------DLEEFKPPPKDELR-KKLGLDDKFVVVYAG----N 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 219 FGEP--LEHVCHALRELAtRHDDIELVY------PMHLNPnvtgpvKAILGDLRNVTLTGPQEYLPFVYLMSKA--HLII 288
Cdd:cd03794 226 IGKAqgLETLLEAAERLK-RRPDIRFLFvgdgdeKERLKE------LAKARGLDNVTFLGRVPKEEVPELLSAAdvGLVP 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939405756 289 TDSGGIQE--------EAPALGVPVLVTRDTTERPEALEAGTARLVGTDR-GRIVAQVEALLNDRHEYEQMA 351
Cdd:cd03794 299 LKDNPANRgsspsklfEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDpEALADAILELLDDPELRRAMG 370
|
|
| PRK13609 |
PRK13609 |
diacylglycerol glucosyltransferase; Provisional |
280-367 |
2.32e-04 |
|
diacylglycerol glucosyltransferase; Provisional
Pssm-ID: 237445 [Multi-domain] Cd Length: 380 Bit Score: 43.17 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 280 LMSKAHLIITDSGGIQ-EEAPALGVPVLVTRDT--TERPEA--LEAGTARLVGTDRGRIVAQVEALLNDRHEYEQMAHAV 354
Cdd:PRK13609 270 LFRVTSCMITKPGGITlSEAAALGVPVILYKPVpgQEKENAmyFERKGAAVVIRDDEEVFAKTEALLQDDMKLLQMKEAM 349
|
90
....*....|...
gi 1939405756 355 NPYGDGHASERIV 367
Cdd:PRK13609 350 KSLYLPEPADHIV 362
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
226-326 |
7.78e-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: 40.85 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 226 VCHALRELATRHDDIELVYPMHLNPNVTGPV-KAILGDLRNVTLTGPQEYLPFVYLMS-KAHLIITDS-----GGIQEEA 298
Cdd:cd01635 128 LLEALALLKARLPDLVLVLVGGGGEREEEEAlAAALGLLERVVIIGGLVDDEVLELLLaAADVFVLPSrsegfGLVLLEA 207
|
90 100
....*....|....*....|....*...
gi 1939405756 299 PALGVPVLVTRDTTERPEALEAGTARLV 326
Cdd:cd01635 208 MAAGKPVIATDVGGIPEFVVDGENGLLV 235
|
|
| murG |
PRK00726 |
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional |
164-372 |
3.12e-03 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
Pssm-ID: 234825 [Multi-domain] Cd Length: 357 Bit Score: 39.34 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 164 PEQVVLTGNTVidallqtREKLTADPWLAKRIAagfpfLDPARRLILVTGhrresfG----EPL-EHVCHALRELAtrhD 238
Cdd:PRK00726 153 KPKAVVTGNPV-------REEILALAAPPARLA-----GREGKPTLLVVG------GsqgaRVLnEAVPEALALLP---E 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939405756 239 DIELVypmhlnpNVTGP-----VKAILGDLRNVTLTgpqeylPFVYLM----SKAHLIITDSGG--IQEEApALGVPVL- 306
Cdd:PRK00726 212 ALQVI-------HQTGKgdleeVRAAYAAGINAEVV------PFIDDMaaayAAADLVICRAGAstVAELA-AAGLPAIl 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939405756 307 -----VTRD-TTERPEALE-AGTARLV---GTDRGRIVAQVEALLNDRHEYEQMAHAVNPYGDGHASERIVAALEK 372
Cdd:PRK00726 278 vplphAADDhQTANARALVdAGAALLIpqsDLTPEKLAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEE 353
|
|
| |
